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Conserved domains on  [gi|30520019|ref|NP_848768|]
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saccharopine dehydrogenase-like oxidoreductase isforom 1 [Mus musculus]

Protein Classification

trans-acting enoyl reductase family protein( domain architecture ID 11461686)

trans-acting enoyl reductase family protein may be involved in the reduction of the double bond between C-4 and C-5 during phthiocerol dimycocerosates (DIM A) and glycosylated phenolphthiocerol dimycocerosates (PGL) biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3268 COG3268
Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];
1-425 5.37e-80

Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];


:

Pssm-ID: 442499 [Multi-domain]  Cd Length: 368  Bit Score: 251.30  E-value: 5.37e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019   1 MATeqRPFHLVVFGASGFTGQFVTEEVAREqiaseqssRLPWAVAGRSKEKLQQVlekaAQKLGRPSLssevGVIICDIS 80
Cdd:COG3268   1 MTE--REFDIVVYGATGYTGRLVAEYLARR--------GLRPALAGRNAAKLEAV----AAELGAADL----PLRVADLD 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019  81 NPASLDEMAKQAKLVLNCVGPYRFYGEPVVKACIENGTSCIDICGEPQFLELMHAKYHEKAAEKGVYIIGSSGFDSIPAD 160
Cdd:COG3268  63 DPASLAALLAGTRVVLNTVGPFARTGEPLVEACLAAGTHYLDLTGEPDWVRRMIDRYDAAARAAGARIVPACGFDSVPSD 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019 161 LGVLYTRNQMNGtLTAVESFLTINTGPEGlcihdGTWKSAIYGFGDKGSLRKLRSvscLKPVPiVGTKLKRRWPVSYCRE 240
Cdd:COG3268 143 LGAALLQERLPE-ADRLTLAVRAKGGFSG-----GTAASMLEALAAGGADRRNGR---LVRVP-YALRTREDFPDGGPQQ 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019 241 lNSYSIPFLGSDISVVKRTQRYLhenledspvQYAAYVTVGGITSVIKLMFAGLFFLFFVKFSIGRQLLIKfpWLFSFGy 320
Cdd:COG3268 213 -GAWTAPWGDVNTAVVRRSNALL---------NYEEYMAVPKGAARALALAAGLGALLAAAVPPLRRLLKR--VLPKPG- 279

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019 321 fskQGPTQKQMDETSFTMTFFGQGYShGTCVEknkpniricTQVKGPEaGYVATPIAMVQAAMTFLSDAsdlPKGGGVFT 400
Cdd:COG3268 280 ---EGPSEEERERGRFVVWGEARTAG-GRRVR---------ARVRGPG-GYGLTAKMLAEAALRLLADD---PVRGGFLT 342

                       410       420
                ....*....|....*....|....*.
gi 30520019 401 PGAAFSrTKLIDRLNKH-GIEFSVIS 425
Cdd:COG3268 343 PATAFG-AALVLRLLAVaGLTFEVEE 367
 
Name Accession Description Interval E-value
COG3268 COG3268
Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];
1-425 5.37e-80

Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];


Pssm-ID: 442499 [Multi-domain]  Cd Length: 368  Bit Score: 251.30  E-value: 5.37e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019   1 MATeqRPFHLVVFGASGFTGQFVTEEVAREqiaseqssRLPWAVAGRSKEKLQQVlekaAQKLGRPSLssevGVIICDIS 80
Cdd:COG3268   1 MTE--REFDIVVYGATGYTGRLVAEYLARR--------GLRPALAGRNAAKLEAV----AAELGAADL----PLRVADLD 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019  81 NPASLDEMAKQAKLVLNCVGPYRFYGEPVVKACIENGTSCIDICGEPQFLELMHAKYHEKAAEKGVYIIGSSGFDSIPAD 160
Cdd:COG3268  63 DPASLAALLAGTRVVLNTVGPFARTGEPLVEACLAAGTHYLDLTGEPDWVRRMIDRYDAAARAAGARIVPACGFDSVPSD 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019 161 LGVLYTRNQMNGtLTAVESFLTINTGPEGlcihdGTWKSAIYGFGDKGSLRKLRSvscLKPVPiVGTKLKRRWPVSYCRE 240
Cdd:COG3268 143 LGAALLQERLPE-ADRLTLAVRAKGGFSG-----GTAASMLEALAAGGADRRNGR---LVRVP-YALRTREDFPDGGPQQ 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019 241 lNSYSIPFLGSDISVVKRTQRYLhenledspvQYAAYVTVGGITSVIKLMFAGLFFLFFVKFSIGRQLLIKfpWLFSFGy 320
Cdd:COG3268 213 -GAWTAPWGDVNTAVVRRSNALL---------NYEEYMAVPKGAARALALAAGLGALLAAAVPPLRRLLKR--VLPKPG- 279

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019 321 fskQGPTQKQMDETSFTMTFFGQGYShGTCVEknkpniricTQVKGPEaGYVATPIAMVQAAMTFLSDAsdlPKGGGVFT 400
Cdd:COG3268 280 ---EGPSEEERERGRFVVWGEARTAG-GRRVR---------ARVRGPG-GYGLTAKMLAEAALRLLADD---PVRGGFLT 342

                       410       420
                ....*....|....*....|....*.
gi 30520019 401 PGAAFSrTKLIDRLNKH-GIEFSVIS 425
Cdd:COG3268 343 PATAFG-AALVLRLLAVaGLTFEVEE 367
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 10-149 1.33e-20

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 86.88  E-value: 1.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019    10 LVVFGAsGFTGQFVTEEVAREQiaseqsSRLPWAVAGRSKEKLQQVLEKAAQKlgrpslssEVGVIICDISNPAS-LDEM 88
Cdd:pfam03435   1 VLIIGA-GSVGQGVAPLLARHF------DVDRITVADRTLEKAQALAAKLGGV--------RFIAVAVDADNYEAvLAAL 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30520019    89 AKQAKLVLNCVGPYrfYGEPVVKACIENGTSCIDICgepqFLELMHAKYHEKAAEKGVYII 149
Cdd:pfam03435  66 LKEGDLVVNLSPPT--LSLDVLKACIETGVHYVDTS----YLREAVLALHEKAKDAGVTAV 120
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 57-151 5.92e-04

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 40.22  E-value: 5.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019  57 EKAAQKLGRPSLSSEVGVIIcdisnPASLDEMAKQAK--LVLNCVGPYRFYGEPVVKACIENGTSCIDICGEPQFLEL-- 132
Cdd:cd24146  36 AKVGKDLGELGGGAPLGVKV-----TDDLDAVLAATKpdVVVHATTSFLADVAPQIERLLEAGLNVITTCEELFYPWArd 110

                        90       100
                ....*....|....*....|.
gi 30520019 133 --MHAKYHEKAAEKGVYIIGS 151
Cdd:cd24146 111 peLAEELDALAKENGVTVLGT 131
 
Name Accession Description Interval E-value
COG3268 COG3268
Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];
1-425 5.37e-80

Uncharacterized conserved protein, related to short-chain dehydrogenases [Function unknown];


Pssm-ID: 442499 [Multi-domain]  Cd Length: 368  Bit Score: 251.30  E-value: 5.37e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019   1 MATeqRPFHLVVFGASGFTGQFVTEEVAREqiaseqssRLPWAVAGRSKEKLQQVlekaAQKLGRPSLssevGVIICDIS 80
Cdd:COG3268   1 MTE--REFDIVVYGATGYTGRLVAEYLARR--------GLRPALAGRNAAKLEAV----AAELGAADL----PLRVADLD 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019  81 NPASLDEMAKQAKLVLNCVGPYRFYGEPVVKACIENGTSCIDICGEPQFLELMHAKYHEKAAEKGVYIIGSSGFDSIPAD 160
Cdd:COG3268  63 DPASLAALLAGTRVVLNTVGPFARTGEPLVEACLAAGTHYLDLTGEPDWVRRMIDRYDAAARAAGARIVPACGFDSVPSD 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019 161 LGVLYTRNQMNGtLTAVESFLTINTGPEGlcihdGTWKSAIYGFGDKGSLRKLRSvscLKPVPiVGTKLKRRWPVSYCRE 240
Cdd:COG3268 143 LGAALLQERLPE-ADRLTLAVRAKGGFSG-----GTAASMLEALAAGGADRRNGR---LVRVP-YALRTREDFPDGGPQQ 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019 241 lNSYSIPFLGSDISVVKRTQRYLhenledspvQYAAYVTVGGITSVIKLMFAGLFFLFFVKFSIGRQLLIKfpWLFSFGy 320
Cdd:COG3268 213 -GAWTAPWGDVNTAVVRRSNALL---------NYEEYMAVPKGAARALALAAGLGALLAAAVPPLRRLLKR--VLPKPG- 279

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019 321 fskQGPTQKQMDETSFTMTFFGQGYShGTCVEknkpniricTQVKGPEaGYVATPIAMVQAAMTFLSDAsdlPKGGGVFT 400
Cdd:COG3268 280 ---EGPSEEERERGRFVVWGEARTAG-GRRVR---------ARVRGPG-GYGLTAKMLAEAALRLLADD---PVRGGFLT 342

                       410       420
                ....*....|....*....|....*.
gi 30520019 401 PGAAFSrTKLIDRLNKH-GIEFSVIS 425
Cdd:COG3268 343 PATAFG-AALVLRLLAVaGLTFEVEE 367
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 10-149 1.33e-20

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 86.88  E-value: 1.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019    10 LVVFGAsGFTGQFVTEEVAREQiaseqsSRLPWAVAGRSKEKLQQVLEKAAQKlgrpslssEVGVIICDISNPAS-LDEM 88
Cdd:pfam03435   1 VLIIGA-GSVGQGVAPLLARHF------DVDRITVADRTLEKAQALAAKLGGV--------RFIAVAVDADNYEAvLAAL 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30520019    89 AKQAKLVLNCVGPYrfYGEPVVKACIENGTSCIDICgepqFLELMHAKYHEKAAEKGVYII 149
Cdd:pfam03435  66 LKEGDLVVNLSPPT--LSLDVLKACIETGVHYVDTS----YLREAVLALHEKAKDAGVTAV 120
Lys9 COG1748
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine ...
 44-155 3.36e-15

Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine dehydrogenase, NADP-dependent is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441354 [Multi-domain]  Cd Length: 352  Bit Score: 76.41  E-value: 3.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019  44 VAGRSKEKLQQVLEKaaqklgrpslSSEVGVIICDISNPASLDEMAKQAKLVLNCVGPYRfyGEPVVKACIENGTSCIDI 123
Cdd:COG1748   5 LADRSLEKAEALAAS----------GPKVEAAQLDASDPEALAALIAGADLVINALPPYL--NLTVAEACIEAGVHYVDL 72

                        90       100       110
                ....*....|....*....|....*....|..
gi 30520019 124 CGEPQFLElMHAKYHEKAAEKGVYIIGSSGFD 155
Cdd:COG1748  73 SEDEPETE-AKLALDELAKEAGVTAIPGCGLA 103
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 11-155 4.09e-05

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 44.45  E-value: 4.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019  11 VVFGASGFTGQFVTEEVAREQIaseqssrlPWAVAGRSKEKLQQVLEKAAQklgrpslssevgVIICDISNPASLDEMAK 90
Cdd:COG0702   3 LVTGATGFIGRRVVRALLARGH--------PVRALVRDPEKAAALAAAGVE------------VVQGDLDDPESLAAALA 62

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30520019  91 QAKLVLNCVGP--------YRFYGEPVVKACIENG------TScidICGEPQFLELMHAKYHeKAAEKgvyIIGSSGFD 155
Cdd:COG0702  63 GVDAVFLLVPSgpggdfavDVEGARNLADAAKAAGvkrivyLS---ALGADRDSPSPYLRAK-AAVEE---ALRASGLP 134
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 57-151 5.92e-04

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 40.22  E-value: 5.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019  57 EKAAQKLGRPSLSSEVGVIIcdisnPASLDEMAKQAK--LVLNCVGPYRFYGEPVVKACIENGTSCIDICGEPQFLEL-- 132
Cdd:cd24146  36 AKVGKDLGELGGGAPLGVKV-----TDDLDAVLAATKpdVVVHATTSFLADVAPQIERLLEAGLNVITTCEELFYPWArd 110

                        90       100
                ....*....|....*....|.
gi 30520019 133 --MHAKYHEKAAEKGVYIIGS 151
Cdd:cd24146 111 peLAEELDALAKENGVTVLGT 131
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
9-101 2.15e-03

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 39.07  E-value: 2.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019   9 HLVVFGASGFTGQFVTEEvareqiASEQSSRLpWAVAgRSKEKLqqvlekaaqklgrPSLSSEVGVIICDISNPASLDEM 88
Cdd:COG2910   1 KIAVIGATGRVGSLIVRE------ALARGHEV-TALV-RNPEKL-------------PDEHPGLTVVVGDVLDPAAVAEA 59

                        90
                ....*....|...
gi 30520019  89 AKQAKLVLNCVGP 101
Cdd:COG2910  60 LAGADAVVSALGA 72
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 9-100 5.02e-03

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 38.39  E-value: 5.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019   9 HLVVFGASGFTGQFVTEEVAREqiaSEQSSrlpwaVAGRSKEKLQQVLEKAaqKLGRPSLSSEVGVIICDISNPASLDEM 88
Cdd:cd08939   3 HVLITGGSSGIGKALAKELVKE---GANVI-----IVARSESKLEEAVEEI--EAEANASGQKVSYISADLSDYEEVEQA 72

                        90
                ....*....|....*....
gi 30520019  89 AKQA-------KLVLNCVG 100
Cdd:cd08939  73 FAQAvekggppDLVVNCAG 91
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 11-100 7.92e-03

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 37.60  E-value: 7.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30520019  11 VVFGASGFTGQFVTEEVAREQIaseqssrlpWAVAG-RSKEKLQQVLEKAAQklgrpslssevgVIICDISNPASLDEMA 89
Cdd:cd05243   3 LVVGATGKVGRHVVRELLDRGY---------QVRALvRDPSQAEKLEAAGAE------------VVVGDLTDAESLAAAL 61

                        90
                ....*....|.
gi 30520019  90 KQAKLVLNCVG 100
Cdd:cd05243  62 EGIDAVISAAG 72
 
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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