NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1370453360|ref|XP_024303260|]
View 

2-Hydroxyacid oxidase 2 isoform X4 [Homo sapiens]

Protein Classification

alpha-hydroxy-acid oxidizing protein( domain architecture ID 10120247)

FMN-dependent alpha-hydroxyacid oxidizing protein such as bacterial lactate dehydrogenase and eukaryotic 2-hydroxy-acid oxidase

CATH:  3.20.20.70
EC:  1.-.-.-
Gene Ontology:  GO:0010181|GO:0016491
PubMed:  12206759|11257493
SCOP:  4000080

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
 21-256 2.28e-111

Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.


:

Pssm-ID: 239203 [Multi-domain]  Cd Length: 299  Bit Score: 326.33  E-value: 2.28e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  21 DFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPD 100
Cdd:cd02809     2 DLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 101 GEMSTARAAQAAGICYITSTFASCSLEDIVIAAPeGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRR- 179
Cdd:cd02809    82 GELATARAAAAAGIPFTLSTVSTTSLEEVAAAAP-GPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRRLt 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 180 -HDIRnQLRRnltLTDLQ-----------------------------------SPKKIDALTEVVAAVKGKIEVYLDGGV 223
Cdd:cd02809   161 wDDLA-WLRS---QWKGPlilkgiltpedalravdagadgivvsnhggrqldgAPATIDALPEIVAAVGGRIEVLLDGGI 236

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1370453360 224 RTGNDVLKALALGAKCIFLGRPILWGLAckAAG 256
Cdd:cd02809   237 RRGTDVLKALALGADAVLIGRPFLYGLA--AGG 267
 
Name Accession Description Interval E-value
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
 21-256 2.28e-111

Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.


Pssm-ID: 239203 [Multi-domain]  Cd Length: 299  Bit Score: 326.33  E-value: 2.28e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  21 DFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPD 100
Cdd:cd02809     2 DLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 101 GEMSTARAAQAAGICYITSTFASCSLEDIVIAAPeGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRR- 179
Cdd:cd02809    82 GELATARAAAAAGIPFTLSTVSTTSLEEVAAAAP-GPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRRLt 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 180 -HDIRnQLRRnltLTDLQ-----------------------------------SPKKIDALTEVVAAVKGKIEVYLDGGV 223
Cdd:cd02809   161 wDDLA-WLRS---QWKGPlilkgiltpedalravdagadgivvsnhggrqldgAPATIDALPEIVAAVGGRIEVLLDGGI 236

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1370453360 224 RTGNDVLKALALGAKCIFLGRPILWGLAckAAG 256
Cdd:cd02809   237 RRGTDVLKALALGADAVLIGRPFLYGLA--AGG 267
FMN_dh pfam01070
FMN-dependent dehydrogenase;
26-256 4.89e-102

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 304.45  E-value: 4.89e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  26 AREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPDGEMST 105
Cdd:pfam01070   1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 106 ARAAQAAGICYITSTFASCSLEDIViAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRRHDIRN- 184
Cdd:pfam01070  81 ARAAAAAGIPFVLSTVSSTSLEEVA-AAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNg 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 185 ----------------------------------------QLRRNLTLTDLQ---------------------------- 196
Cdd:pfam01070 160 ftlpprltprnlldlalhprwalgvlrrggaggaaafvgsQFDPALTWDDLAwlrerwkgplvvkgilspedakraveag 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370453360 197 ----------------SPKKIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLAckAAG 256
Cdd:pfam01070 240 vdgivvsnhggrqldgAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLA--AGG 313
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
 17-257 7.77e-92

FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440915 [Multi-domain]  Cd Length: 357  Bit Score: 278.55  E-value: 7.77e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  17 VCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCL 96
Cdd:COG1304     5 LSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGGL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  97 VWPDGEMSTARAAQAAGICYITSTFASCSLEDiVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCG 176
Cdd:COG1304    85 AHPDGELALARAAAAAGIPMGLSTQSTTSLEE-VAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVLG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 177 NRRHDIRN-----------------------------------QLRRNLTLTDL-----QSPKK---------------- 200
Cdd:COG1304   164 RRERDLREgfsqpprltprnlleaathprwalglaslaawldtNFDPSLTWDDIawlreRWPGPlivkgvlspedarrav 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 201 -----------------------IDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLAckAAGR 257
Cdd:COG1304   244 dagvdgidvsnhggrqldggpptIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLA--AGGE 321
PLN02535 PLN02535
glycolate oxidase
 17-253 1.56e-64

glycolate oxidase


Pssm-ID: 215294  Cd Length: 364  Bit Score: 208.54  E-value: 1.56e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  17 VCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCL 96
Cdd:PLN02535    6 VNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  97 VWPDGEMSTARAAQAAGICYITSTFASCSLEDiVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCG 176
Cdd:PLN02535   86 AHPEGEIATARAAAACNTIMVLSFMASCTVEE-VASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 177 NRRHDIRNQL----RRNL-------------------------------------TLTDLQ------------------- 196
Cdd:PLN02535  165 RREADIKNKMispqLKNFegllstevvsdkgsgleafasetfdaslswkdiewlrSITNLPilikgvltredaikavevg 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370453360 197 ----------------SPKKIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACK 253
Cdd:PLN02535  245 vagiivsnhgarqldySPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAK 317
 
Name Accession Description Interval E-value
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
 21-256 2.28e-111

Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.


Pssm-ID: 239203 [Multi-domain]  Cd Length: 299  Bit Score: 326.33  E-value: 2.28e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  21 DFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPD 100
Cdd:cd02809     2 DLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 101 GEMSTARAAQAAGICYITSTFASCSLEDIVIAAPeGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRR- 179
Cdd:cd02809    82 GELATARAAAAAGIPFTLSTVSTTSLEEVAAAAP-GPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRRLt 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 180 -HDIRnQLRRnltLTDLQ-----------------------------------SPKKIDALTEVVAAVKGKIEVYLDGGV 223
Cdd:cd02809   161 wDDLA-WLRS---QWKGPlilkgiltpedalravdagadgivvsnhggrqldgAPATIDALPEIVAAVGGRIEVLLDGGI 236

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1370453360 224 RTGNDVLKALALGAKCIFLGRPILWGLAckAAG 256
Cdd:cd02809   237 RRGTDVLKALALGADAVLIGRPFLYGLA--AGG 267
FMN_dh pfam01070
FMN-dependent dehydrogenase;
26-256 4.89e-102

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 304.45  E-value: 4.89e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  26 AREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPDGEMST 105
Cdd:pfam01070   1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 106 ARAAQAAGICYITSTFASCSLEDIViAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRRHDIRN- 184
Cdd:pfam01070  81 ARAAAAAGIPFVLSTVSSTSLEEVA-AAAGGPLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNg 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 185 ----------------------------------------QLRRNLTLTDLQ---------------------------- 196
Cdd:pfam01070 160 ftlpprltprnlldlalhprwalgvlrrggaggaaafvgsQFDPALTWDDLAwlrerwkgplvvkgilspedakraveag 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370453360 197 ----------------SPKKIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLAckAAG 256
Cdd:pfam01070 240 vdgivvsnhggrqldgAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLA--AGG 313
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
 17-257 7.77e-92

FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440915 [Multi-domain]  Cd Length: 357  Bit Score: 278.55  E-value: 7.77e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  17 VCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCL 96
Cdd:COG1304     5 LSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGGL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  97 VWPDGEMSTARAAQAAGICYITSTFASCSLEDiVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCG 176
Cdd:COG1304    85 AHPDGELALARAAAAAGIPMGLSTQSTTSLEE-VAAAAPAPLWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVLG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 177 NRRHDIRN-----------------------------------QLRRNLTLTDL-----QSPKK---------------- 200
Cdd:COG1304   164 RRERDLREgfsqpprltprnlleaathprwalglaslaawldtNFDPSLTWDDIawlreRWPGPlivkgvlspedarrav 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 201 -----------------------IDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLAckAAGR 257
Cdd:COG1304   244 dagvdgidvsnhggrqldggpptIDALPEIRAAVGGRIPVIADGGIRRGLDVAKALALGADAVGLGRPFLYGLA--AGGE 321
FCB2_FMN cd02922
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ...
 21-252 2.38e-72

Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) is a respiratory enzyme located in the intermembrane space of fungal mitochondria which catalyzes the oxidation of L-lactate to pyruvate. FCB2 also participates in a short electron-transport chain involving cytochrome c and cytochrome oxidase which ultimately directs the reducing equivalents gained from L-lactate oxidation to oxygen, yielding one molecule of ATP for every L-lactate molecule consumed. FCB2 is composed of 2 domains: a C-terminal flavin-binding domain, which includes the active site for lacate oxidation, and an N-terminal b2-cytochrome domain, required for efficient cytochrome c reduction. FCB2 is a homotetramer and contains two noncovalently bound cofactors, FMN and heme per subunit.


Pssm-ID: 239238 [Multi-domain]  Cd Length: 344  Bit Score: 228.25  E-value: 2.38e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  21 DFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPD 100
Cdd:cd02922     2 DFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 101 GEMSTARAAQAAGICYITSTFASCSLEDIVIAAPEGL-RWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRR 179
Cdd:cd02922    82 GELNLARAAGKHGILQMISTNASCSLEEIVDARPPDQpLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 180 HDIRNQLRR----------------------------NLTLTDLQ----------------------------------- 196
Cdd:cd02922   162 RDERLKAEEavsdgpagkktkakgggagramsgfidpTLTWDDIKwlrkhtklpivlkgvqtvedavlaaeygvdgivls 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370453360 197 ---------SPKKIDALTEVV---AAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLAC 252
Cdd:cd02922   242 nhggrqldtAPAPIEVLLEIRkhcPEVFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSA 309
PLN02535 PLN02535
glycolate oxidase
 17-253 1.56e-64

glycolate oxidase


Pssm-ID: 215294  Cd Length: 364  Bit Score: 208.54  E-value: 1.56e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  17 VCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCL 96
Cdd:PLN02535    6 VNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  97 VWPDGEMSTARAAQAAGICYITSTFASCSLEDiVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCG 176
Cdd:PLN02535   86 AHPEGEIATARAAAACNTIMVLSFMASCTVEE-VASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 177 NRRHDIRNQL----RRNL-------------------------------------TLTDLQ------------------- 196
Cdd:PLN02535  165 RREADIKNKMispqLKNFegllstevvsdkgsgleafasetfdaslswkdiewlrSITNLPilikgvltredaikavevg 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370453360 197 ----------------SPKKIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACK 253
Cdd:PLN02535  245 vagiivsnhgarqldySPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAK 317
LMO_FMN cd03332
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ...
 17-251 1.58e-62

L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that catalyzes the conversion of L-lactate and oxygen to acetate, carbon dioxide, and water. LMO is a member of the family of alpha-hydroxy acid oxidases. It is thought to be a homooctamer with two- and four- fold axes in the center of the octamer.


Pssm-ID: 239448 [Multi-domain]  Cd Length: 383  Bit Score: 204.05  E-value: 1.58e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  17 VCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCL 96
Cdd:cd03332    19 VDPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQEL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  97 VWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCG 176
Cdd:cd03332    99 FHPDAELATARAAAELGVPYILSTASSSSIEDVAAAAGDAPRWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLG 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 177 NRRHDIRN---------------------------------------------------------QLRRNLTLTDL---- 195
Cdd:cd03332   179 WRPRDLDLgylpflrgigianyfsdpvfrkklaepvgedpeapppmeaavarfvsvfsgpsltweDLAFLREWTDLpivl 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 196 ---QSPK----------------------------KIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGR 244
Cdd:cd03332   259 kgiLHPDdarraveagvdgvvvsnhggrqvdgsiaALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALALGAKAVLIGR 338


                  ....*..
gi 1370453360 245 PILWGLA 251
Cdd:cd03332   339 PYAYGLA 345
PLN02493 PLN02493
probable peroxisomal (S)-2-hydroxy-acid oxidase
 14-279 3.66e-60

probable peroxisomal (S)-2-hydroxy-acid oxidase


Pssm-ID: 166134 [Multi-domain]  Cd Length: 367  Bit Score: 197.65  E-value: 3.66e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  14 MSLVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGF 93
Cdd:PLN02493    1 MEITNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  94 HCLVWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAAPeGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTP 173
Cdd:PLN02493   81 QKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 174 VCGNRRHDIRN-----------------------------------QLRRNLTLTDLQ---------------------- 196
Cdd:PLN02493  160 RLGRRESDIKNrftlppnltlknfegldlgkmdeandsglasyvagQIDRTLSWKDVQwlqtitklpilvkgvltgedar 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 197 ----------------------SPKKIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKA 254
Cdd:PLN02493  240 iaiqagaagiivsnhgarqldyVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEG 319

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1370453360 255 -AG-----RSLR-SIETWSSFPGCKKKGPITR 279
Cdd:PLN02493  320 eAGvrkvlQMLRdEFELTMALSGCRSLKEISR 351
LOX_like_FMN cd04737
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ...
 16-256 2.23e-59

L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240088 [Multi-domain]  Cd Length: 351  Bit Score: 194.97  E-value: 2.23e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  16 LVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHC 95
Cdd:cd04737     5 IINLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  96 LVWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVC 175
Cdd:cd04737    85 LAHATGEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGGPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 176 GNRRHDIRN-----------------------------QLRRNLTLTDLQ------------------------------ 196
Cdd:cd04737   165 GNREADIRNkfqfpfgmpnlnhfsegtgkgkgiseiyaAAKQKLSPADIEfiakisglpvivkgiqspedadvainagad 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370453360 197 --------------SPKKIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKAAG 256
Cdd:cd04737   245 giwvsnhggrqldgGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLALGGAQ 318
MDH_FMN cd04736
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ...
 21-253 1.41e-48

Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of homologous FMN-dependent a-hydroxy acid oxidizing enzymes that oxidizes (S)-mandelate to phenylglyoxalate. MDH is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240087  Cd Length: 361  Bit Score: 166.93  E-value: 1.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  21 DFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPD 100
Cdd:cd04736     2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 101 GEMSTARAAQAAGICYITSTFASCSLEDIVIAApEGLRWFQLYV-HPDLQlnKQLIQRVESLGFKALVITLDTPVCGNRR 179
Cdd:cd04736    82 GDLALARAAAKAGIPFVLSTASNMSIEDVARQA-DGDLWFQLYVvHRELA--ELLVKRALAAGYTTLVLTTDVAVNGYRE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 180 HDIRNQ--------------------------------------------------LRRNL------------------- 190
Cdd:cd04736   159 RDLRNGfaipfrytprvlldgilhprwllrflrngmpqlanfasddaidvevqaalMSRQMdasfnwqdlrwlrdlwphk 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 191 -------------------------------TLTDLQSPkkIDALTEVVAAVkgKIEVYLDGGVRTGNDVLKALALGAKC 239
Cdd:cd04736   239 llvkgivtaedakrcielgadgvilsnhggrQLDDAIAP--IEALAEIVAAT--YKPVLIDSGIRRGSDIVKALALGANA 314

                         330
                  ....*....|....
gi 1370453360 240 IFLGRPILWGLACK 253
Cdd:cd04736   315 VLLGRATLYGLAAR 328
PLN02979 PLN02979
glycolate oxidase
 60-279 1.34e-45

glycolate oxidase


Pssm-ID: 166620  Cd Length: 366  Bit Score: 159.50  E-value: 1.34e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  60 LRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAAPeGLRW 139
Cdd:PLN02979   46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGP-GIRF 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 140 FQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRRHDIRN----------------------------------- 184
Cdd:PLN02979  125 FQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNrftlppnltlknfegldlgkmdeandsglasyvag 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 185 QLRRNLTLTDLQ--------------------------------------------SPKKIDALTEVVAAVKGKIEVYLD 220
Cdd:PLN02979  205 QIDRTLSWKDVQwlqtitklpilvkgvltgedariaiqagaagiivsnhgarqldyVPATISALEEVVKATQGRIPVFLD 284

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370453360 221 GGVRTGNDVLKALALGAKCIFLGRPILWGLACKAAG------RSLR-SIETWSSFPGCKKKGPITR 279
Cdd:PLN02979  285 GGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAgvrkvlQMLRdEFELTMALSGCRSLKEISR 350
lldD PRK11197
L-lactate dehydrogenase; Provisional
 14-257 5.02e-40

L-lactate dehydrogenase; Provisional


Pssm-ID: 183033  Cd Length: 381  Bit Score: 145.17  E-value: 5.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  14 MSLVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDTRTTIQGEEISAPICIAPTGF 93
Cdd:PRK11197    1 MIISAASDYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  94 HCLVWPDGEMSTARAAQAAGICYITSTFASCSLEDiVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTP 173
Cdd:PRK11197   81 TGMYARRGEVQAARAADAKGIPFTLSTVSVCPIEE-VAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 174 VCGNRRHDIRN-------QLRRNL-------------------TL----TDLQSPKKID--------------------- 202
Cdd:PRK11197  160 VPGARYRDAHSgmsgpnaAMRRYLqavthpqwawdvglngrphDLgnisAYLGKPTGLEdyigwlgnnfdpsiswkdlew 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 203 -------------------------------------------------ALTEVVAAVKGKIEVYLDGGVRTGNDVLKAL 233
Cdd:PRK11197  240 irdfwdgpmvikgildpedardavrfgadgivvsnhggrqldgvlssarALPAIADAVKGDITILADSGIRNGLDVVRMI 319

                         330       340
                  ....*....|....*....|....
gi 1370453360 234 ALGAKCIFLGRPILWGLAckAAGR 257
Cdd:PRK11197  320 ALGADTVLLGRAFVYALA--AAGQ 341
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 95-244 2.21e-07

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 50.66  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  95 CLVWPDGEMS---TARAAQAAGICYITSTFASCSLEDI---------VIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLG 162
Cdd:cd04722     5 LLAGGPSGDPvelAKAAAEAGADAIIVGTRSSDPEEAEtddkevlkeVAAETDLPLGVQLAINDAAAAVDIAAAAARAAG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 163 FKALVITLDtpvCGNRRHDIRNQLRR--------------NLTLTDLQSPKKIDALTEVV-------------------- 208
Cdd:cd04722    85 ADGVEIHGA---VGYLAREDLELIRElreavpdvkvvvklSPTGELAAAAAEEAGVDEVGlgngggggggrdavpiadll 161

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1370453360 209 -AAVKGKIEVYL--DGGVRTGNDVLKALALGAKCIFLGR 244
Cdd:cd04722   162 lILAKRGSKVPViaGGGINDPEDAAEALALGADGVIVGS 200
IDI-2_FMN cd02811
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ...
 55-265 6.99e-06

Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway.


Pssm-ID: 239205 [Multi-domain]  Cd Length: 326  Bit Score: 47.11  E-value: 6.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360  55 FKRIRLRPRYLR--DVSEVDTRTTIQGEEISAPICI-APTGFHclvwPDGE---MSTARAAQAAGIcyitsTFASCS--- 125
Cdd:cd02811    22 FDDVRLVHNALPelDLDDIDLSTEFLGKRLSAPLLIsAMTGGS----EKAKeinRNLAEAAEELGI-----AMGVGSqra 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 126 -LED-----------------IVIA-------APEGLRWFQ----------LYVHpdlqLN--KQLIQ---------RVE 159
Cdd:cd02811    93 aLEDpelaesftvvreappngPLIAnlgavqlNGYGVEEARravemieadaLAIH----LNplQEAVQpegdrdfrgWLE 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 160 SLgfKALVITLDTPV------CGNRRHDI---------------------------RNQLRRNLTLTDLQS---PKKiDA 203
Cdd:cd02811   169 RI--EELVKALSVPVivkevgFGISRETAkrladagvkaidvagaggtswarvenyRAKDSDQRLAEYFADwgiPTA-AS 245

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370453360 204 LTEVVAAVKgKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILwglacKAAGRS----LRSIETW 265
Cdd:cd02811   246 LLEVRSALP-DLPLIASGGIRNGLDIAKALALGADLVGMAGPFL-----KAALEGeeavIETIEQI 305
GltS_FMN cd02808
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ...
 201-257 7.80e-06

Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor.


Pssm-ID: 239202 [Multi-domain]  Cd Length: 392  Bit Score: 47.15  E-value: 7.80e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370453360 201 IDALTEVV-----AAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKAAGR 257
Cdd:cd02808   267 ELGLARAHqalvkNGLRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIALGCIQARK 328
Glu_synthase pfam01645
Conserved region in glutamate synthase; This family represents a region of the glutamate ...
 203-257 1.27e-05

Conserved region in glutamate synthase; This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organizms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster.


Pssm-ID: 396287 [Multi-domain]  Cd Length: 367  Bit Score: 46.56  E-value: 1.27e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370453360 203 ALTEVVAAVK-----GKIEVYLDGGVRTGNDVLKALALGAKCIFLGRPILWGLACKAAGR 257
Cdd:pfam01645 257 ALAEAHQTLKenglrDRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGCIMCRV 316
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
 203-245 2.23e-04

IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.


Pssm-ID: 238223 [Multi-domain]  Cd Length: 325  Bit Score: 42.50  E-value: 2.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1370453360 203 ALTEVVAAVKG-KIEVYLDGGVRTGNDVLKALALGAKCIFLGRP 245
Cdd:cd00381   185 AVADVAAAARDyGVPVIADGGIRTSGDIVKALAAGADAVMLGSL 228
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 220-244 8.49e-04

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 41.11  E-value: 8.49e-04
                          10        20
                  ....*....|....*....|....*
gi 1370453360 220 DGGVRTGNDVLKALALGAKCIFLGR 244
Cdd:PTZ00314  350 DGGIKNSGDICKALALGADCVMLGS 374
GuaB COG0516
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ...
 203-244 3.01e-03

IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440282 [Multi-domain]  Cd Length: 326  Bit Score: 39.04  E-value: 3.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1370453360 203 ALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGR 244
Cdd:COG0516   186 AAMDTVTEARMAIAIAADGGIGYIHDNAKALAAGADAVMLGS 227
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 203-244 4.18e-03

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 38.91  E-value: 4.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370453360 203 ALTEVVAAVKG-KIEVYLDGGVRTGNDVLKALALGAKCIFLGR 244
Cdd:pfam00478 311 AIYDVAEAAKKyGVPVIADGGIKYSGDIVKALAAGADAVMLGS 353
GltB2 COG0069
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ...
 202-237 5.03e-03

Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 439839  Cd Length: 728  Bit Score: 38.69  E-value: 5.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1370453360 202 DALTEVVAA-----VKGKIEVYLDGGVRTGNDVLKALALGA 237
Cdd:COG0069   423 LGLAEVHQTlvgngLRDRIRLIADGKLKTGRDVAIAAALGA 463
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH