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Conserved domains on  [gi|1207996400|ref|NP_001339539|]
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propionyl-CoA carboxylase alpha chain, mitochondrial isoform i [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PccA super family cl44129
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-197 3.23e-115

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


The actual alignment was detected with superfamily member COG4770:

Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 344.31  E-value: 3.23e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADIRINGWA 80
Cdd:COG4770   255 MGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPFTQEDIKLRGHA 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400  81 VECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVI 160
Cdd:COG4770   335 IECRINAEDPARGF-LPSPGTITRLRPPGG-PGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIARMRRALAEFVI 412

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1207996400 161 RGVTHNIALLREVIINSRFVKGDISTKFLSDVYPDGF 197
Cdd:COG4770   413 EGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELL 449
PCC_BT pfam18140
Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A ...
 210-338 7.06e-37

Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A carboxylase (PCC), present in Roseobacter denitrificans. PCC is a mitochondrial biotin-dependent enzyme that is essential for the catabolism of certain amino acids, cholesterol, and fatty acids with an odd number of carbon atoms. Since this domain mediates biotin carboxylase-carboxyltransferase interactions it is referred to as the BT domain. The BT domain is located between biotin carboxylase and the biotin carboxyl carrier protein domains. The BT domain shares some structural similarity with the pyruvate carboxylase tetramerization domain of pyruvate carboxylase.


:

Pssm-ID: 465666 [Multi-domain]  Cd Length: 126  Bit Score: 130.83  E-value: 7.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400 210 LLAIASSLFVAFQLRAQHFqENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLASPLLS 289
Cdd:pfam18140   1 LAAIAAAIHAVRELRARRI-SGQLRGHSRPVGDDWVVVVGGGDEPVTVVVEEDGDEFEVTVDGETVTVSSDWRPGDPLFR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1207996400 290 VSVDGTQRTVQClSREAGGnMSIQFLGTVYKVNILTRLAAELNKFMLEK 338
Cdd:pfam18140  80 GTVDGEPVTVQV-ERRAGG-YRLRHRGTSFKVQVLTPRAAELAKLMPEK 126
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 346-412 6.37e-29

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


:

Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 107.50  E-value: 6.37e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207996400 346 VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 412
Cdd:cd06850     1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-197 3.23e-115

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 344.31  E-value: 3.23e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADIRINGWA 80
Cdd:COG4770   255 MGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPFTQEDIKLRGHA 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400  81 VECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVI 160
Cdd:COG4770   335 IECRINAEDPARGF-LPSPGTITRLRPPGG-PGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIARMRRALAEFVI 412

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1207996400 161 RGVTHNIALLREVIINSRFVKGDISTKFLSDVYPDGF 197
Cdd:COG4770   413 EGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELL 449
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-189 8.22e-89

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 276.30  E-value: 8.22e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADIRINGWA 80
Cdd:PRK08591  255 IGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSIKQEDIVFRGHA 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400  81 VECRVYAEDPYKSFgLPSIGRLSQYqeplHLP---GVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDN 157
Cdd:PRK08591  335 IECRINAEDPAKNF-MPSPGKITRY----HPPggpGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAIARMKRALSE 409

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1207996400 158 YVIRGVTHNIALLREVIINSRFVKGDISTKFL 189
Cdd:PRK08591  410 FVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYL 441
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 1-189 1.66e-71

acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 129605 [Multi-domain]  Cd Length: 449  Bit Score: 231.57  E-value: 1.66e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADIRINGWA 80
Cdd:TIGR00514 255 MGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPLSLKQEDVVVRGHA 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400  81 VECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVI 160
Cdd:TIGR00514 335 IECRINAEDPIKTF-LPSPGRITRYLPPGG-PGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAIARMKRALSEFII 412

                         170       180
                  ....*....|....*....|....*....
gi 1207996400 161 RGVTHNIALLREVIINSRFVKGDISTKFL 189
Cdd:TIGR00514 413 DGIKTTIPFHQRILEDENFQHGGTNIHYL 441
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 82-189 9.86e-52

Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.


Pssm-ID: 214878 [Multi-domain]  Cd Length: 107  Bit Score: 168.75  E-value: 9.86e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400   82 ECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIR 161
Cdd:smart00878   1 ECRINAEDPANGF-LPSPGRITRYRFPGG-PGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIR 78

                           90       100
                   ....*....|....*....|....*...
gi 1207996400  162 GVTHNIALLREVIINSRFVKGDISTKFL 189
Cdd:smart00878  79 GVKTNIPFLRALLRHPDFRAGDVDTGFL 106
Biotin_carb_C pfam02785
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 82-191 3.19e-51

Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.


Pssm-ID: 426981 [Multi-domain]  Cd Length: 108  Bit Score: 167.67  E-value: 3.19e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400  82 ECRVYAEDPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIR 161
Cdd:pfam02785   1 EARIYAEDPDNNF-LPSPGKVTRYRFP-GGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIE 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1207996400 162 GVTHNIALLREVIINSRFVKGDISTKFLSD 191
Cdd:pfam02785  79 GVKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
PCC_BT pfam18140
Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A ...
 210-338 7.06e-37

Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A carboxylase (PCC), present in Roseobacter denitrificans. PCC is a mitochondrial biotin-dependent enzyme that is essential for the catabolism of certain amino acids, cholesterol, and fatty acids with an odd number of carbon atoms. Since this domain mediates biotin carboxylase-carboxyltransferase interactions it is referred to as the BT domain. The BT domain is located between biotin carboxylase and the biotin carboxyl carrier protein domains. The BT domain shares some structural similarity with the pyruvate carboxylase tetramerization domain of pyruvate carboxylase.


Pssm-ID: 465666 [Multi-domain]  Cd Length: 126  Bit Score: 130.83  E-value: 7.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400 210 LLAIASSLFVAFQLRAQHFqENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLASPLLS 289
Cdd:pfam18140   1 LAAIAAAIHAVRELRARRI-SGQLRGHSRPVGDDWVVVVGGGDEPVTVVVEEDGDEFEVTVDGETVTVSSDWRPGDPLFR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1207996400 290 VSVDGTQRTVQClSREAGGnMSIQFLGTVYKVNILTRLAAELNKFMLEK 338
Cdd:pfam18140  80 GTVDGEPVTVQV-ERRAGG-YRLRHRGTSFKVQVLTPRAAELAKLMPEK 126
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 346-412 6.37e-29

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 107.50  E-value: 6.37e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207996400 346 VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 412
Cdd:cd06850     1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 349-413 2.22e-22

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 99.83  E-value: 2.22e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207996400  349 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 413
Cdd:PRK12999  1081 APMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 349-412 1.43e-21

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 97.46  E-value: 1.43e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207996400  349 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 412
Cdd:COG1038   1081 APMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 346-412 4.43e-20

Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 83.42  E-value: 4.43e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207996400 346 VLRSPMPGVVVA-----VSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 412
Cdd:pfam00364   2 EIKSPMIGESVRegvveWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
pyruv_carbox TIGR01235
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ...
 349-413 6.24e-15

pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 130302 [Multi-domain]  Cd Length: 1143  Bit Score: 77.17  E-value: 6.24e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207996400  349 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 413
Cdd:TIGR01235 1079 APMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-197 3.23e-115

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 344.31  E-value: 3.23e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADIRINGWA 80
Cdd:COG4770   255 MGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLPFTQEDIKLRGHA 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400  81 VECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVI 160
Cdd:COG4770   335 IECRINAEDPARGF-LPSPGTITRLRPPGG-PGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIARMRRALAEFVI 412

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1207996400 161 RGVTHNIALLREVIINSRFVKGDISTKFLSDVYPDGF 197
Cdd:COG4770   413 EGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELL 449
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-189 8.22e-89

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 276.30  E-value: 8.22e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADIRINGWA 80
Cdd:PRK08591  255 IGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLSIKQEDIVFRGHA 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400  81 VECRVYAEDPYKSFgLPSIGRLSQYqeplHLP---GVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDN 157
Cdd:PRK08591  335 IECRINAEDPAKNF-MPSPGKITRY----HPPggpGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAIARMKRALSE 409

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1207996400 158 YVIRGVTHNIALLREVIINSRFVKGDISTKFL 189
Cdd:PRK08591  410 FVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYL 441
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-207 4.55e-85

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 266.51  E-value: 4.55e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADIRINGWA 80
Cdd:PRK06111  255 MGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSFTQDDIKRSGHA 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400  81 VECRVYAEDPyKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVI 160
Cdd:PRK06111  335 IEVRIYAEDP-KTF-FPSPGKITDLTLPGG-EGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLHDALEELKV 411

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1207996400 161 RGVTHNIALLREVIINSRFVKGDISTKFLSDvypdgfkgHMLTKSEK 207
Cdd:PRK06111  412 EGIKTNIPLLLQVLEDPVFKAGGYTTGFLTK--------QLVKKSTK 450
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
1-191 1.71e-84

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 266.46  E-value: 1.71e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400   1 MGEQAVALARAVKYSSAGTVEFLVdSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADIRINGWA 80
Cdd:PRK08654  255 MGEAAVKAAKAINYENAGTVEFLY-SNGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELSFKQEDITIRGHA 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400  81 VECRVYAEDPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVI 160
Cdd:PRK08654  334 IECRINAEDPLNDF-APSPGKIKRYRSP-GGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIARMRRALYEYVI 411

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1207996400 161 RGVTHNIALLREVIINSRFVKGDISTKFLSD 191
Cdd:PRK08654  412 VGVKTNIPFHKAVMENENFVRGNLHTHFIEE 442
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
1-191 1.13e-71

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 231.91  E-value: 1.13e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADIRINGWA 80
Cdd:PRK05586  255 MGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSIKQEDIKINGHS 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400  81 VECRVYAEDPYKSFgLPSIGRLSQyqepLHLPG---VRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDN 157
Cdd:PRK05586  335 IECRINAEDPKNGF-MPCPGKIEE----LYIPGglgVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQKMKRALGE 409

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1207996400 158 YVIRGVTHNIALLREVIINSRFVKGDISTKFLSD 191
Cdd:PRK05586  410 FIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 1-189 1.66e-71

acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 129605 [Multi-domain]  Cd Length: 449  Bit Score: 231.57  E-value: 1.66e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADIRINGWA 80
Cdd:TIGR00514 255 MGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPLSLKQEDVVVRGHA 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400  81 VECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVI 160
Cdd:TIGR00514 335 IECRINAEDPIKTF-LPSPGRITRYLPPGG-PGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAIARMKRALSEFII 412

                         170       180
                  ....*....|....*....|....*....
gi 1207996400 161 RGVTHNIALLREVIINSRFVKGDISTKFL 189
Cdd:TIGR00514 413 DGIKTTIPFHQRILEDENFQHGGTNIHYL 441
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 3-191 1.59e-68

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 235.03  E-value: 1.59e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400    3 EQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLR------HKQADIRI 76
Cdd:PRK12999   261 EAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGATLHdleigiPSQEDIRL 340

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400   77 NGWAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQ-PGSDISIYYDPMISKLITYGSDRTEALKRMADAL 155
Cdd:PRK12999   341 RGYAIQCRITTEDPANNF-MPDTGRITAYRSPGG-FGVRLDGGNAfAGAEITPYYDSLLVKLTAWGRTFEQAVARMRRAL 418

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1207996400  156 DNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSD 191
Cdd:PRK12999   419 REFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDE 454
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 3-189 8.13e-65

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 214.62  E-value: 8.13e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400   3 EQAVALARAVKYSSAGTVEFLVD-SKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADIRINGWAV 81
Cdd:PRK12833  259 ASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRFAQGDIALRGAAL 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400  82 ECRVYAEDPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIR 161
Cdd:PRK12833  339 ECRINAEDPLRDF-FPNPGRIDALVWP-QGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAALARAARALRELRID 416

                         170       180
                  ....*....|....*....|....*...
gi 1207996400 162 GVTHNIALLREVIINSRFVKGDISTKFL 189
Cdd:PRK12833  417 GMKTTAPLHRALLADADVRAGRFHTNFL 444
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
1-189 3.35e-64

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 213.04  E-value: 3.35e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADIRINGWA 80
Cdd:PRK07178  254 IGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLSYKQEDIQHRGFA 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400  81 VECRVYAEDPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVI 160
Cdd:PRK07178  334 LQFRINAEDPKNDF-LPSFGKITRYYAP-GGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEALDRGRRALDDMRV 411

                         170       180
                  ....*....|....*....|....*....
gi 1207996400 161 RGVTHNIALLREVIINSRFVKGDISTKFL 189
Cdd:PRK07178  412 QGVKTTIPYYQEILRNPEFRSGQFNTSFV 440
urea_carbox TIGR02712
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ...
 1-194 1.82e-63

urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including characterized members from Oleomonas sagaranensis (alpha class Proteobacterium) and yeasts such as Saccharomyces cerevisiae. The allophanate hydrolase domain of the yeast enzyme is not included in this model and is represented by an adjacent gene in Oleomonas sagaranensis. The fusion of urea carboxylase and allophanate hydrolase is designated urea amidolyase. The enzyme from Oleomonas sagaranensis was shown to be highly active on acetamide and formamide as well as urea. [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 274264 [Multi-domain]  Cd Length: 1201  Bit Score: 220.67  E-value: 1.82e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400    1 MGEQAVALARAVKYSSAGTVEFLVDSKKN-FYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQ--ADIRIN 77
Cdd:TIGR02712  253 LLAAAERLGEAVNYRSAGTVEFIYDEARDeFYFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGELPDFASlnISLTPR 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400   78 GWAVECRVYAEDPYKSFgLPSIGRLSQYQEPlhlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDN 157
Cdd:TIGR02712  333 GAAIEARVYAENPAKNF-QPSPGLLTDVQFP---DDVRVDTWVETGTEVSPEYDPMLAKIIVHGSDREDAILKLHQALAE 408

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1207996400  158 YVIRGVTHNIALLREVIINSRFVKGDISTKFLSD-VYP 194
Cdd:TIGR02712  409 TRVYGIETNLDYLRSILSSETFRSAQVSTRTLNSfVYT 446
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 5-188 4.52e-62

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 216.48  E-value: 4.52e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400    5 AVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHK------QADIRING 78
Cdd:COG1038    262 AVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSLDDPeigipsQEDIRLNG 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400   79 WAVECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSG-IQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDN 157
Cdd:COG1038    342 YAIQCRITTEDPANNF-MPDTGRITAYRSAGG-FGIRLDGGnAYTGAVITPYYDSLLVKVTAWGRTFEEAIRKMRRALRE 419

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1207996400  158 YVIRGVTHNIALLREVIINSRFVKGDISTKF 188
Cdd:COG1038    420 FRIRGVKTNIPFLENVLNHPDFLAGECTTSF 450
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
3-190 4.12e-58

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 196.50  E-value: 4.12e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400   3 EQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLrHKQADIRINGWAVE 82
Cdd:PRK08462  259 ETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL-PSQESIKLKGHAIE 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400  83 CRVYAEDPyKSFgLPSIGRLSQYqeplHLPG---VRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYV 159
Cdd:PRK08462  338 CRITAEDP-KKF-YPSPGKITKW----IAPGgrnVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIAKMKRALKEFK 411

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1207996400 160 IRGVTHNIALLREVIINSRFVKGDISTKFLS 190
Cdd:PRK08462  412 VEGIKTTIPFHLEMMENADFINNKYDTKYLE 442
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
 1-189 5.67e-52

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 180.78  E-value: 5.67e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADIRINGWA 80
Cdd:PRK08463  255 MGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEILDLEQSDIKPRGFA 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400  81 VECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVI 160
Cdd:PRK08463  335 IEARITAENVWKNF-IPSPGKITEYYPALG-PSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLAVNKLERALKEFVI 412

                         170       180
                  ....*....|....*....|....*....
gi 1207996400 161 RGVTHNIALLREVIINSRFVKGDISTKFL 189
Cdd:PRK08463  413 DGIRTTIPFLIAITKTREFRRGYFDTSYI 441
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 82-189 9.86e-52

Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.


Pssm-ID: 214878 [Multi-domain]  Cd Length: 107  Bit Score: 168.75  E-value: 9.86e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400   82 ECRVYAEDPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIR 161
Cdd:smart00878   1 ECRINAEDPANGF-LPSPGRITRYRFPGG-PGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIR 78

                           90       100
                   ....*....|....*....|....*...
gi 1207996400  162 GVTHNIALLREVIINSRFVKGDISTKFL 189
Cdd:smart00878  79 GVKTNIPFLRALLRHPDFRAGDVDTGFL 106
Biotin_carb_C pfam02785
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 82-191 3.19e-51

Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.


Pssm-ID: 426981 [Multi-domain]  Cd Length: 108  Bit Score: 167.67  E-value: 3.19e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400  82 ECRVYAEDPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIR 161
Cdd:pfam02785   1 EARIYAEDPDNNF-LPSPGKVTRYRFP-GGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIE 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1207996400 162 GVTHNIALLREVIINSRFVKGDISTKFLSD 191
Cdd:pfam02785  79 GVKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
PCC_BT pfam18140
Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A ...
 210-338 7.06e-37

Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A carboxylase (PCC), present in Roseobacter denitrificans. PCC is a mitochondrial biotin-dependent enzyme that is essential for the catabolism of certain amino acids, cholesterol, and fatty acids with an odd number of carbon atoms. Since this domain mediates biotin carboxylase-carboxyltransferase interactions it is referred to as the BT domain. The BT domain is located between biotin carboxylase and the biotin carboxyl carrier protein domains. The BT domain shares some structural similarity with the pyruvate carboxylase tetramerization domain of pyruvate carboxylase.


Pssm-ID: 465666 [Multi-domain]  Cd Length: 126  Bit Score: 130.83  E-value: 7.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400 210 LLAIASSLFVAFQLRAQHFqENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLASPLLS 289
Cdd:pfam18140   1 LAAIAAAIHAVRELRARRI-SGQLRGHSRPVGDDWVVVVGGGDEPVTVVVEEDGDEFEVTVDGETVTVSSDWRPGDPLFR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1207996400 290 VSVDGTQRTVQClSREAGGnMSIQFLGTVYKVNILTRLAAELNKFMLEK 338
Cdd:pfam18140  80 GTVDGEPVTVQV-ERRAGG-YRLRHRGTSFKVQVLTPRAAELAKLMPEK 126
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 346-412 6.37e-29

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 107.50  E-value: 6.37e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207996400 346 VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 412
Cdd:cd06850     1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 1-68 1.81e-28

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 110.86  E-value: 1.81e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207996400   1 MGEQAVALARAVKYSSAGTVEFLVDSK-KNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLR 68
Cdd:pfam02786 141 LREAAVKIARHLGYVGAGTVEFALDPFsGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 349-413 2.22e-22

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 99.83  E-value: 2.22e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207996400  349 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 413
Cdd:PRK12999  1081 APMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 349-412 1.43e-21

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 97.46  E-value: 1.43e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207996400  349 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 412
Cdd:COG1038   1081 APMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 346-412 4.43e-20

Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 83.42  E-value: 4.43e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207996400 346 VLRSPMPGVVVA-----VSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 412
Cdd:pfam00364   2 EIKSPMIGESVRegvveWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 346-413 6.96e-20

Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440277 [Multi-domain]  Cd Length: 136  Bit Score: 84.95  E-value: 6.96e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207996400 346 VLRSPMPGVV-------VAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 413
Cdd:COG0511    62 AVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 266-413 2.25e-19

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 90.29  E-value: 2.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400 266 FSVEVDGSKLNV--TSTWNLASPLLSVSVDGTQRTVQclsreaggnmsiqflgtvykvniltrlAAELNKF-MLEKVTED 342
Cdd:PRK09282  468 FKVEVDGEKYEVkiEGVKAEGKRPFYLRVDGMPEEVV---------------------------VEPLKEIvVGGRPRAS 520

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207996400 343 TSSVLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 413
Cdd:PRK09282  521 APGAVTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
PRK08225 PRK08225
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 345-413 5.07e-18

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 181304 [Multi-domain]  Cd Length: 70  Bit Score: 77.91  E-value: 5.07e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207996400 345 SVLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 413
Cdd:PRK08225    2 TKVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
PRK06549 PRK06549
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 346-410 1.79e-17

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235826 [Multi-domain]  Cd Length: 130  Bit Score: 78.32  E-value: 1.79e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207996400 346 VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLV 410
Cdd:PRK06549   63 AMPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLI 127
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 1-62 6.79e-17

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 79.92  E-value: 6.79e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207996400   1 MGEQAVALARAVKYS-SAGTVEFLVDSKKNFYFLEMNTRLQVEH--PVTECITGLDLVQEMIRVA 62
Cdd:COG0439   190 IGELVARALRALGYRrGAFHTEFLLTPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLA 254
PRK05641 PRK05641
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 346-412 1.85e-15

putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 73.36  E-value: 1.85e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207996400 346 VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 412
Cdd:PRK05641   86 VVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
pyruv_carbox TIGR01235
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ...
 349-413 6.24e-15

pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 130302 [Multi-domain]  Cd Length: 1143  Bit Score: 77.17  E-value: 6.24e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207996400  349 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 413
Cdd:TIGR01235 1079 APMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
349-412 1.04e-12

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 69.57  E-value: 1.04e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207996400 349 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 412
Cdd:PRK14040  529 APLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 353-412 1.19e-11

Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 60.11  E-value: 1.19e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400 353 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 412
Cdd:cd06849    15 GTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 353-412 9.82e-10

Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 54.69  E-value: 9.82e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400 353 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 412
Cdd:COG0508    17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
PRK14042 PRK14042
pyruvate carboxylase subunit B; Provisional
 351-413 1.01e-09

pyruvate carboxylase subunit B; Provisional


Pssm-ID: 172536 [Multi-domain]  Cd Length: 596  Bit Score: 60.51  E-value: 1.01e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207996400 351 MPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 413
Cdd:PRK14042  532 IPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 353-412 3.95e-09

Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.


Pssm-ID: 133456 [Multi-domain]  Cd Length: 73  Bit Score: 52.83  E-value: 3.95e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400 353 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 412
Cdd:cd06663    14 GTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 353-413 5.38e-08

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 54.88  E-value: 5.38e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207996400 353 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 413
Cdd:TIGR01348  14 GEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
 348-392 6.06e-08

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 53.69  E-value: 6.06e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1207996400 348 RSPMPGVvvAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTV 392
Cdd:PLN02983  210 RSPAPGE--PPFVKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTI 252
PRK07051 PRK07051
biotin carboxyl carrier domain-containing protein;
347-413 2.91e-07

biotin carboxyl carrier domain-containing protein;


Pssm-ID: 180811 [Multi-domain]  Cd Length: 80  Bit Score: 47.70  E-value: 2.91e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207996400 347 LRSPMPGVV-------VAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 413
Cdd:PRK07051    6 IVSPLPGTFyrrpspdAPPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 355-413 4.86e-07

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 51.75  E-value: 4.86e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207996400 355 VVAVSVKPGDAVAEGQEICVIEAMK--MQnsMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 413
Cdd:PRK11855  135 VIEWLVKVGDTVEEDQSLITVETDKatME--IPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 353-413 5.46e-07

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 51.80  E-value: 5.46e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207996400 353 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 413
Cdd:TIGR01348 130 VTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLS 190
PRK05889 PRK05889
biotin/lipoyl-binding carrier protein;
347-409 2.22e-06

biotin/lipoyl-binding carrier protein;


Pssm-ID: 180306 [Multi-domain]  Cd Length: 71  Bit Score: 45.18  E-value: 2.22e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207996400 347 LRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLL 409
Cdd:PRK05889    5 VRAEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLI 67
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 355-413 3.42e-06

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 49.05  E-value: 3.42e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207996400 355 VVAVSVKPGDAVAEGQEICVIEAMK--MQnsMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 413
Cdd:PRK11855   18 VIEWLVKEGDTVEEDQPLVTVETDKatME--IPSPAAGVVKEIKVKVGDTVSVGGLLAVIE 76
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 353-412 2.24e-04

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 43.13  E-value: 2.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996400 353 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 412
Cdd:PTZ00144   59 GTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEI 118
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 353-409 2.80e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 42.62  E-value: 2.80e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207996400 353 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLL 409
Cdd:PRK14875   17 GKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 353-413 9.22e-04

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 41.53  E-value: 9.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207996400 353 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 413
Cdd:PRK11854  118 VEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFE 178
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 353-413 1.65e-03

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 40.76  E-value: 1.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207996400 353 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 413
Cdd:PRK11854  219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFE 279
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 353-413 2.14e-03

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 40.37  E-value: 2.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207996400 353 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 413
Cdd:PRK11854   15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFE 75
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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