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Conserved domains on  [gi|15832458|ref|NP_311231|]
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erythronate-4-phosphate dehydrogenase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

4-phosphoerythronate dehydrogenase( domain architecture ID 11487797)

4-phosphoerythronate dehydrogenase catalyzes the second step in the biosynthesis of the coenzyme pyridoxal 5'-phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
1-378 0e+00

erythronate-4-phosphate dehydrogenase PdxB; Provisional


:

Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 794.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458    1 MKILVDENMPYARDLFSRLGEVIAVPGRPIPVAQLADADALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQA 80
Cdd:PRK15438   1 MKILVDENMPYARELFSRLGEVKAVPGRPIPVAQLADADALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   81 GIGFSAAPGCNAIAVVEYVFSSLLMLAERDGFSLHERTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADCGDEGDFRS 160
Cdd:PRK15438  81 GIGFSAAPGCNAIAVVEYVFSSLLMLAERDGFSLHDRTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADRGDEGDFRS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  161 LDELVQRADILTFHTPLFKDGPYKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPEL 240
Cdd:PRK15438 161 LDELVQEADILTFHTPLFKDGPYKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPEL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  241 NVELLTKVDIGTPHIAGYTLEGKARGTTQVFEAYSKFIGHEQHVALDTLLPAPEFGRITLHGPLDQPTLKRLVHLVYDVR 320
Cdd:PRK15438 241 NVELLKKVDIGTPHIAGYTLEGKARGTTQVFEAYSKFIGHEQHVALDTLLPAPEFGRITLHGPLDQPTLKRLVHLVYDVR 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15832458  321 RDDAPLRKVAGIPGEFDKLRKNYLERREWSSLYVICDDASAASLLCKLGFNAVHHPAR 378
Cdd:PRK15438 321 RDDAPLRKVAGIPGEFDKLRKNYLERREWSSLYVICDDASAASLLCKLGFNAVHHPAR 378
 
Name Accession Description Interval E-value
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
1-378 0e+00

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 794.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458    1 MKILVDENMPYARDLFSRLGEVIAVPGRPIPVAQLADADALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQA 80
Cdd:PRK15438   1 MKILVDENMPYARELFSRLGEVKAVPGRPIPVAQLADADALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   81 GIGFSAAPGCNAIAVVEYVFSSLLMLAERDGFSLHERTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADCGDEGDFRS 160
Cdd:PRK15438  81 GIGFSAAPGCNAIAVVEYVFSSLLMLAERDGFSLHDRTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADRGDEGDFRS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  161 LDELVQRADILTFHTPLFKDGPYKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPEL 240
Cdd:PRK15438 161 LDELVQEADILTFHTPLFKDGPYKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPEL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  241 NVELLTKVDIGTPHIAGYTLEGKARGTTQVFEAYSKFIGHEQHVALDTLLPAPEFGRITLHGPLDQPTLKRLVHLVYDVR 320
Cdd:PRK15438 241 NVELLKKVDIGTPHIAGYTLEGKARGTTQVFEAYSKFIGHEQHVALDTLLPAPEFGRITLHGPLDQPTLKRLVHLVYDVR 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15832458  321 RDDAPLRKVAGIPGEFDKLRKNYLERREWSSLYVICDDASAASLLCKLGFNAVHHPAR 378
Cdd:PRK15438 321 RDDAPLRKVAGIPGEFDKLRKNYLERREWSSLYVICDDASAASLLCKLGFNAVHHPAR 378
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
2-343 0e+00

D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; D-Erythronate-4-phosphate Dehydrogenase (E. coli gene PdxB), a D-specific 2-hydroxyacid dehydrogenase family member, catalyzes the NAD-dependent oxidation of erythronate-4-phosphate, which is followed by transamination to form 4-hydroxy-L-threonine-4-phosphate within the de novo biosynthesis pathway of vitamin B6. D-Erythronate-4-phosphate dehydrogenase has the common architecture shared with D-isomer specific 2-hydroxyacid dehydrogenases but contains an additional C-terminal dimerization domain in addition to an NAD-binding domain and the "lid" domain. The lid domain corresponds to the catalytic domain of phosphoglycerate dehydrogenase and other proteins of the D-isomer specific 2-hydroxyacid dehydrogenase family, which include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240635 [Multi-domain]  Cd Length: 343  Bit Score: 525.17  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   2 KILVDENMPYARDLFSRLGEVIAVPGRPIPVAQLADADALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQAG 81
Cdd:cd12158   1 KILADENIPYAEELFSPLGEVTYLPGREITAEDLKDADVLLVRSVTKVNEALLEGSKVKFVGTATIGTDHIDTDYLKERG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  82 IGFSAAPGCNAIAVVEYVFSSLLMLAERDGFSLHERTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADCGDEGDFRSL 161
Cdd:cd12158  81 IGFANAPGCNANSVAEYVLSALLVLAQRQGFSLKGKTVGIVGVGNVGSRLARRLEALGMNVLLCDPPRAEAEGDPGFVSL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 162 DELVQRADILTFHTPLFKDGPYKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPELN 241
Cdd:cd12158 161 EELLAEADIITLHVPLTRDGEHPTYHLLDEDFLAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVWENEPEID 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 242 VELLTKVDIGTPHIAGYTLEGKARGTTQVFEAYSKFIGHEQHVALDTLLPAPEFGRITLHGPLDQPTLKRLVHLVYDVRR 321
Cdd:cd12158 241 LELLDKVDIATPHIAGYSLEGKARGTEMIYEALCQFLGLKARKSLSDLLPAPALPSITLDGSLDEALLARLVRAVYDIRR 320
                       330       340
                ....*....|....*....|..
gi 15832458 322 DDAPLRKVAGIPGEFDKLRKNY 343
Cdd:cd12158 321 DDARLRKTLALPAGFDALRKNY 342
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
1-281 4.81e-69

Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; Phosphoglycerate dehydrogenase or related dehydrogenase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439881 [Multi-domain]  Cd Length: 314  Bit Score: 219.68  E-value: 4.81e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   1 MKILVDENMPY-ARDLFSRLG--EVIAVPGRPIP--VAQLADADALMVRSVTKVNESLL-AGKPIKFVGTATAGTDHVDE 74
Cdd:COG0111   1 MKILILDDLPPeALEALEAAPgiEVVYAPGLDEEelAEALADADALIVRSRTKVTAELLaAAPNLKLIGRAGAGVDNIDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  75 AWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAER-DGFSLHERTVGIVGVGNVGRRLQ-----------------ARLE 136
Cdd:COG0111  81 AAATERGIPVTNAPGANARAVAEYALALLLALARRlPEADRAQRAGRWDRSAFRGRELRgktvgivglgrigravaRRLR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 137 ALGIKTLLCDPPRADCGDE----GDFRSLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVV 212
Cdd:COG0111 161 AFGMRVLAYDPSPKPEEAAdlgvGLVDSLDELLAEADVVSLHLPLTPE----TRGLIGAEELAAMKPGAILINTARGGVV 236
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15832458 213 DNTALLTCLNEGQKLSVVLDVWEGEPELNVELLTKVD--IGTPHIAGYTLEGKARGTTQVFEAYSKFIGHE 281
Cdd:COG0111 237 DEDALLAALDSGRLAGAALDVFEPEPLPADSPLWDLPnvILTPHIAGSTEEAQERAARQVAENIRRFLAGE 307
DUF3410 pfam11890
Domain of unknown function (DUF3410); This domain is functionally uncharacterized. This domain ...
289-369 3.35e-36

Domain of unknown function (DUF3410); This domain is functionally uncharacterized. This domain is found in bacteria. This presumed domain is about 90 amino acids in length. This domain is found associated with pfam02826, pfam00389. This domain has a conserved RRE sequence motif.


Pssm-ID: 432166 [Multi-domain]  Cd Length: 81  Bit Score: 126.53  E-value: 3.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   289 LLPAPEFGRITLHGPLDQPTLKRLVHLVYDVRRDDAPLRKVAGIPGEFDKLRKNYLERREWSSLYVICDDASAASLLCKL 368
Cdd:pfam11890   1 LLPPPPLPELSLTGNLDEEALKNLVRLVYDPRRDDALFRRNLARPGGFDYLRKHYPERREFSALTVTSTDSALANLLSKL 80

                  .
gi 15832458   369 G 369
Cdd:pfam11890  81 G 81
 
Name Accession Description Interval E-value
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
1-378 0e+00

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 794.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458    1 MKILVDENMPYARDLFSRLGEVIAVPGRPIPVAQLADADALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQA 80
Cdd:PRK15438   1 MKILVDENMPYARELFSRLGEVKAVPGRPIPVAQLADADALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   81 GIGFSAAPGCNAIAVVEYVFSSLLMLAERDGFSLHERTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADCGDEGDFRS 160
Cdd:PRK15438  81 GIGFSAAPGCNAIAVVEYVFSSLLMLAERDGFSLHDRTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADRGDEGDFRS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  161 LDELVQRADILTFHTPLFKDGPYKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPEL 240
Cdd:PRK15438 161 LDELVQEADILTFHTPLFKDGPYKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPEL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  241 NVELLTKVDIGTPHIAGYTLEGKARGTTQVFEAYSKFIGHEQHVALDTLLPAPEFGRITLHGPLDQPTLKRLVHLVYDVR 320
Cdd:PRK15438 241 NVELLKKVDIGTPHIAGYTLEGKARGTTQVFEAYSKFIGHEQHVALDTLLPAPEFGRITLHGPLDQPTLKRLVHLVYDVR 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15832458  321 RDDAPLRKVAGIPGEFDKLRKNYLERREWSSLYVICDDASAASLLCKLGFNAVHHPAR 378
Cdd:PRK15438 321 RDDAPLRKVAGIPGEFDKLRKNYLERREWSSLYVICDDASAASLLCKLGFNAVHHPAR 378
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
2-343 0e+00

D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; D-Erythronate-4-phosphate Dehydrogenase (E. coli gene PdxB), a D-specific 2-hydroxyacid dehydrogenase family member, catalyzes the NAD-dependent oxidation of erythronate-4-phosphate, which is followed by transamination to form 4-hydroxy-L-threonine-4-phosphate within the de novo biosynthesis pathway of vitamin B6. D-Erythronate-4-phosphate dehydrogenase has the common architecture shared with D-isomer specific 2-hydroxyacid dehydrogenases but contains an additional C-terminal dimerization domain in addition to an NAD-binding domain and the "lid" domain. The lid domain corresponds to the catalytic domain of phosphoglycerate dehydrogenase and other proteins of the D-isomer specific 2-hydroxyacid dehydrogenase family, which include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240635 [Multi-domain]  Cd Length: 343  Bit Score: 525.17  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   2 KILVDENMPYARDLFSRLGEVIAVPGRPIPVAQLADADALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQAG 81
Cdd:cd12158   1 KILADENIPYAEELFSPLGEVTYLPGREITAEDLKDADVLLVRSVTKVNEALLEGSKVKFVGTATIGTDHIDTDYLKERG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  82 IGFSAAPGCNAIAVVEYVFSSLLMLAERDGFSLHERTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADCGDEGDFRSL 161
Cdd:cd12158  81 IGFANAPGCNANSVAEYVLSALLVLAQRQGFSLKGKTVGIVGVGNVGSRLARRLEALGMNVLLCDPPRAEAEGDPGFVSL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 162 DELVQRADILTFHTPLFKDGPYKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPELN 241
Cdd:cd12158 161 EELLAEADIITLHVPLTRDGEHPTYHLLDEDFLAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVWENEPEID 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 242 VELLTKVDIGTPHIAGYTLEGKARGTTQVFEAYSKFIGHEQHVALDTLLPAPEFGRITLHGPLDQPTLKRLVHLVYDVRR 321
Cdd:cd12158 241 LELLDKVDIATPHIAGYSLEGKARGTEMIYEALCQFLGLKARKSLSDLLPAPALPSITLDGSLDEALLARLVRAVYDIRR 320
                       330       340
                ....*....|....*....|..
gi 15832458 322 DDAPLRKVAGIPGEFDKLRKNY 343
Cdd:cd12158 321 DDARLRKTLALPAGFDALRKNY 342
PRK00257 PRK00257
4-phosphoerythronate dehydrogenase PdxB;
1-373 3.46e-152

4-phosphoerythronate dehydrogenase PdxB;


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 434.08  E-value: 3.46e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458    1 MKILVDENMPYARDLFSRLGEVIAVPGRPIPVAQLADADALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQA 80
Cdd:PRK00257   1 MKIVADENIPLLDAFFAGFGEIRRLPGRAFDRAAVRDADVLLVRSVTRVDRALLEGSRVRFVGTCTIGTDHLDLDYFAEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   81 GIGFSAAPGCNAIAVVEYVFSSLLMLAERDGFSLHERTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADCGDEGDFRS 160
Cdd:PRK00257  81 GITWSSAPGCNARGVVDYVLGSLLTLAEREGVDLAERTYGVVGAGHVGGRLVRVLRGLGWKVLVCDPPRQEAEGDGDFVS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  161 LDELVQRADILTFHTPLFKDGPYKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPEL 240
Cdd:PRK00257 161 LERILEECDVISLHTPLTKEGEHPTRHLLDEAFLASLRPGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWEGEPQI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  241 NVELLTKVDIGTPHIAGYTLEGKARGTTQVFEAYSKFIGHEQHVALDTLLPAPEFGRITLHGPLD-QPTLKRLVHLVYDV 319
Cdd:PRK00257 241 DLELADLCTIATPHIAGYSLDGKARGTAQIYQALCRFFGIPARVSLTDLLPPPWLAQIDLDASADpAWALATLCRAVYDP 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15832458  320 RRDDAPLRK-----VAGIPGEFDKLRKNYLERREWSSLYVICDDASA--ASLLCKLGFNAV 373
Cdd:PRK00257 321 RRDDAAFRRsltgdVAQQRAAFDALRKHYPLRREIEGLRVRLTGESPelAQLVRALGAQLV 381
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
1-281 4.81e-69

Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; Phosphoglycerate dehydrogenase or related dehydrogenase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439881 [Multi-domain]  Cd Length: 314  Bit Score: 219.68  E-value: 4.81e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   1 MKILVDENMPY-ARDLFSRLG--EVIAVPGRPIP--VAQLADADALMVRSVTKVNESLL-AGKPIKFVGTATAGTDHVDE 74
Cdd:COG0111   1 MKILILDDLPPeALEALEAAPgiEVVYAPGLDEEelAEALADADALIVRSRTKVTAELLaAAPNLKLIGRAGAGVDNIDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  75 AWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAER-DGFSLHERTVGIVGVGNVGRRLQ-----------------ARLE 136
Cdd:COG0111  81 AAATERGIPVTNAPGANARAVAEYALALLLALARRlPEADRAQRAGRWDRSAFRGRELRgktvgivglgrigravaRRLR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 137 ALGIKTLLCDPPRADCGDE----GDFRSLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVV 212
Cdd:COG0111 161 AFGMRVLAYDPSPKPEEAAdlgvGLVDSLDELLAEADVVSLHLPLTPE----TRGLIGAEELAAMKPGAILINTARGGVV 236
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15832458 213 DNTALLTCLNEGQKLSVVLDVWEGEPELNVELLTKVD--IGTPHIAGYTLEGKARGTTQVFEAYSKFIGHE 281
Cdd:COG0111 237 DEDALLAALDSGRLAGAALDVFEPEPLPADSPLWDLPnvILTPHIAGSTEEAQERAARQVAENIRRFLAGE 307
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
2-277 1.43e-57

Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240622 [Multi-domain]  Cd Length: 302  Bit Score: 189.76  E-value: 1.43e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   2 KILVDENM--PYARDLFSRLG-EVIAVPGRPIP--VAQLADADALMVRSVTKVNESLLAGKP-IKFVGTATAGTDHVDEA 75
Cdd:cd05198   1 KVLVLEPLfpPEALEALEATGfEVIVADDLLADelEALLADADALIVSSTTPVTAEVLAKAPkLKFIQVAGAGVDNIDLD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  76 WLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAERDGFSlHERTVGIVGVGNVG--------------------RRLQARL 135
Cdd:cd05198  81 AAKKRGITVTNVPGANAEAVAEHALGLLLALLRRLPRA-DAAVRRGWGWLWAGfpgyelegktvgivglgrigQRVAKRL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 136 EALGIKTLLCDP-PRADCGDEGDFR--SLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVV 212
Cdd:cd05198 160 QAFGMKVLYYDRtRKPEPEEDLGFRvvSLDELLAQSDVVVLHLPLTPE----TRHLINEEELALMKPGAVLVNTARGGLV 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15832458 213 DNTALLTCLNEGQKLSVVLDVWEGEPELNVELLTKVD--IGTPHIAGYTLEGKARGTTQVFEAYSKF 277
Cdd:cd05198 236 DEDALLRALKSGKIAGAALDVFEPEPLPADHPLLELPnvILTPHIAGYTEEARERMAEIAVENLERF 302
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
1-261 4.31e-44

Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, Coenzyme transport and metabolism, General function prediction only]; Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440672 [Multi-domain]  Cd Length: 316  Bit Score: 154.86  E-value: 4.31e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   1 MKILVDENMPYARDLFSRLG----EVIAVPGRPIP---VAQLADADALMVRSVTKVNESLLAGKP-IKFVGTATAGTDHV 72
Cdd:COG1052   1 KPILVLDPRTLPDEVLERLEaehfEVTVYEDETSPeelAERAAGADAVITNGKDPIDAEVLEALPgLKLIANRGVGYDNI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  73 DEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAER-------------------DGFSLHERTvgivgvgnvgrrL-- 131
Cdd:COG1052  81 DLAAAKERGITVTNTPGYLTEAVAEHAVALLLALARRiveadrrvragdwswspglLGRDLSGKT------------Lgi 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 132 -------QA---RLEALGIKTLLCDP-PRADCGDEGDFR-SLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKP 199
Cdd:COG1052 149 iglgrigQAvarRAKGFGMKVLYYDRsPKPEVAELGAEYvSLDELLAESDIVSLHCPLTPE----TRHLINAEELALMKP 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15832458 200 GAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPELNVELLTKVD--IGTPHIAGYTLE 261
Cdd:COG1052 225 GAILINTARGGLVDEAALIEALKSGRIAGAGLDVFEEEPPPPDHPLLSLPnvVLTPHIASATEE 288
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
2-265 4.37e-44

Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240650 [Multi-domain]  Cd Length: 304  Bit Score: 154.50  E-value: 4.37e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   2 KILVDENM-PYARDLFSRLG-EVIAVPGRPIP--VAQLADADALMVRSVTKVNESLL-AGKPIKFVGTATAGTDHVDEAW 76
Cdd:cd12173   1 KVLVTDPIdEEGLELLREAGiEVDVAPGLSEEelLAIIADADALIVRSATKVTAEVIeAAPRLKVIGRAGVGVDNIDVEA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  77 LKQAGIGFSAAPGCNAIAVVEYVFSSLLMLA---------------ERD---GFSLHERTVGIVGVGNVGRRLQARLEAL 138
Cdd:cd12173  81 ATARGILVVNAPGANTISVAEHTIALMLALArnipqadaslragkwDRKkfmGVELRGKTLGIVGLGRIGREVARRARAF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 139 GIKTLLCDP--PRADCGDEG-DFRSLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVVDNT 215
Cdd:cd12173 161 GMKVLAYDPyiSAERAAAGGvELVSLDELLAEADFISLHTPLTPE----TRGLINAEELAKMKPGAILINTARGGIVDEA 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15832458 216 ALLTCLNEGQKLSVVLDVWEGEPELNVELLTKVD--IGTPHIAGYTLEGKAR 265
Cdd:cd12173 237 ALADALKSGKIAGAALDVFEQEPPPADSPLLGLPnvILTPHLGASTEEAQER 288
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
1-265 5.81e-41

Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate dehydrogenase (PGDH) catalyzes the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDH comes in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240628 [Multi-domain]  Cd Length: 301  Bit Score: 146.14  E-value: 5.81e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   1 MKILVDENM-PYARDLFSRLG-EVIAVPGrpIPVAQLA----DADALMVRSVTKVNESLL-AGKPIKFVGTATAGTDHVD 73
Cdd:cd05303   1 MKILITDGIdEIAIEKLEEAGfEVDYEPL--IAKEELLekikDYDVLIVRSRTKVTKEVIdAAKNLKIIARAGVGLDNID 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  74 EAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLA------------------ERDGFSLHERTVGIVGVGNVGRRLQARL 135
Cdd:cd05303  79 VEYAKKKGIKVINTPGASSNSVAELVIGLMLSLArfihranremklgkwnkkKYKGIELRGKTLGIIGFGRIGREVAKIA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 136 EALGIKTLLCDP--PRADCGDEG-DFRSLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVV 212
Cdd:cd05303 159 RALGMNVIAYDPypKDEQAVELGvKTVSLEELLKNSDFISLHVPLTPE----TKHMINKKELELMKDGAIIINTSRGGVI 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15832458 213 DNTALLTCLNEGQKLSVVLDVWEGEPELNVELLT--KVdIGTPHIAGYTLEGKAR 265
Cdd:cd05303 235 DEEALLEALKSGKLAGAALDVFENEPPPGSKLLElpNV-SLTPHIGASTKEAQER 288
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
2-270 2.92e-37

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.


Pssm-ID: 240649 [Multi-domain]  Cd Length: 306  Bit Score: 136.46  E-value: 2.92e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   2 KILV-----DENMPYARDLFSRLG-EVIAVP-GRPIPVAQLA----DADALMVrSVTKVNESLLAGKP----IKFVGTat 66
Cdd:cd12172   1 KVLVtprsfSKYSEEAKELLEAAGfEVVLNPlGRPLTEEELIellkDADGVIA-GLDPITEEVLAAAPrlkvISRYGV-- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  67 aGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLA----ERD------------GFSLHERTVGIVGVGNVGRR 130
Cdd:cd12172  78 -GYDNIDLEAAKKRGIVVTNTPGANSNSVAELTIGLMLALArqipQADrevraggwdrpvGTELYGKTLGIIGLGRIGKA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 131 LQARLEALGIKTLLCDP-PRADCGDEGDFR--SLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINAC 207
Cdd:cd12172 157 VARRLSGFGMKVLAYDPyPDEEFAKEHGVEfvSLEELLKESDFISLHLPLTPE----TRHLINAAELALMKPGAILINTA 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15832458 208 RGAVVDNTALLTCLNEGQKLSVVLDVWEGEPELNVELLTKVD--IGTPHIAGYTLEGKARGTTQV 270
Cdd:cd12172 233 RGGLVDEEALYEALKSGRIAGAALDVFEEEPPPADSPLLELPnvILTPHIGASTKEAVLRMGTMA 297
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
2-261 8.29e-37

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240652 [Multi-domain]  Cd Length: 311  Bit Score: 135.39  E-value: 8.29e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   2 KILV-DENMPYARDLFSRLG------EVIAVPGRPIPVAQLADADALMVRSVTKVNESLLAGKP-IKFVGTATAGTDHVD 73
Cdd:cd12175   1 KVLFlGPEFPDAEELLRALLppapgvEVVTAAELDEEAALLADADVLVPGMRKVIDAELLAAAPrLRLIQQPGVGLDGVD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  74 EAWLKQAGIGFSAAPGCNAIAVVEyvFSSLLMLA---------------------ERDGFSLHERTVGIVGVGNVGRRLQ 132
Cdd:cd12175  81 LEAATARGIPVANIPGGNAESVAE--HAVMLMLAllrrlpeadrelragrwgrpeGRPSRELSGKTVGIVGLGNIGRAVA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 133 ARLEALGIKTLLCDPPRADCGDEGD----FRSLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACR 208
Cdd:cd12175 159 RRLRGFGVEVIYYDRFRDPEAEEKDlgvrYVELDELLAESDVVSLHVPLTPE----TRHLIGAEELAAMKPGAILINTAR 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15832458 209 GAVVDNTALLTCLNEGQKLSVVLDVWEGEP-ELNVELLTKVD-IGTPHIAGYTLE 261
Cdd:cd12175 235 GGLVDEEALLAALRSGHLAGAGLDVFWQEPlPPDDPLLRLDNvILTPHIAGVTDE 289
DUF3410 pfam11890
Domain of unknown function (DUF3410); This domain is functionally uncharacterized. This domain ...
289-369 3.35e-36

Domain of unknown function (DUF3410); This domain is functionally uncharacterized. This domain is found in bacteria. This presumed domain is about 90 amino acids in length. This domain is found associated with pfam02826, pfam00389. This domain has a conserved RRE sequence motif.


Pssm-ID: 432166 [Multi-domain]  Cd Length: 81  Bit Score: 126.53  E-value: 3.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   289 LLPAPEFGRITLHGPLDQPTLKRLVHLVYDVRRDDAPLRKVAGIPGEFDKLRKNYLERREWSSLYVICDDASAASLLCKL 368
Cdd:pfam11890   1 LLPPPPLPELSLTGNLDEEALKNLVRLVYDPRRDDALFRRNLARPGGFDYLRKHYPERREFSALTVTSTDSALANLLSKL 80

                  .
gi 15832458   369 G 369
Cdd:pfam11890  81 G 81
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
3-278 5.77e-35

D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the largest portion of the catalytic domain of 2-hydroxyacid dehydrogenases as the NAD binding domain is inserted within the structural domain.


Pssm-ID: 425656 [Multi-domain]  Cd Length: 311  Bit Score: 130.49  E-value: 5.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458     3 ILVDENM-PYARDLFSRlGEVIAVPGRPIP--VAQLADADALMVRSVTKVNESLL-AGKPIKFVGTATAGTDHVDEAWLK 78
Cdd:pfam00389   1 VLILDPLsPEALELLKE-GEVEVHDELLTEelLEKAKDADALIVRSRTKVTAEVLeAAPKLKVIGRAGVGVDNVDLDAAT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458    79 QAGIGFSAAPGCNAIAVVEYVFSSLLMLAERD------------------GFSLHERTVGIVGVGNVGRRLQARLEALGI 140
Cdd:pfam00389  80 ERGILVTNAPGYNTESVAELTIGLILALARRIpeadasvregkwkksgliGLELYGKTLGVIGGGGIGGGVAAIAKAFGM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   141 KTLLCDPPRAD-------CGDEGDFRSLDELVQRADILTfHTPLFKDgpyKTLHLADEKLIRSLKPGAILINACRGAVVD 213
Cdd:pfam00389 160 GVVAYDPYPNPeraeaggVEVLSLLLLLLDLPESDDVLT-VNPLTTM---KTGVIIINEARGMLKDAVAIINAAGGGVID 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15832458   214 NTALLTCLNEGqKLSVVLDVWEGEPELNVELLTKVD--IGTPHIAGYTLEGKARGTTQVFEAYSKFI 278
Cdd:pfam00389 236 EAALDALLEEG-IAAAADLDVEEEPPPVDSPLLDLPnvILTPHIGGATEEAQERIAEEAAENILAFL 301
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
1-261 4.27e-32

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. D-HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. Similar to the structurally distinct L-HicDH, D-HicDH exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240620 [Multi-domain]  Cd Length: 323  Bit Score: 123.18  E-value: 4.27e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   1 MKILV----DENMPYARDLFSRLG---EVIAVPGRPIPVAQLA-DADALMVRSVTKVNESLLAGKP-IKFVGTATAGTDH 71
Cdd:cd01619   1 MKVLIydyrDDELEIEKEILKAGGvdvEIVTYLLNDDETAELAkGADAILTAFTDKIDAELLDKAPgLKFISLRATGYDN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  72 VDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLA-------ERD-----------GFSLHERTVGIVGVGNVGRRLQA 133
Cdd:cd01619  81 IDLDYAKELGIGVTNVPEYSPNAVAEHTIALILALLrnrkyidERDknqdlqdagviGRELEDQTVGVVGTGKIGRAVAQ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 134 RLEALGIKTLLCDP-PRADCGDEG-DFRSLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAV 211
Cdd:cd01619 161 RAKGFGMKVIAYDPfRNPELEDKGvKYVSLEELFKNSDIISLHVPLTPE----NHHMINEEAFKLMKKGVIIINTARGSL 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15832458 212 VDNTALLTCLNEGQKLSVVLDVWEGE-PELNVELLTKVD--------------IGTPHIAGYTLE 261
Cdd:cd01619 237 VDTEALIEALDSGKIFGAGLDVLEDEtPDLLKDLEGEIFkdalnallgrrpnvIITPHTAFYTDD 301
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
1-259 5.88e-30

D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenases family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase(D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240662  Cd Length: 329  Bit Score: 117.25  E-value: 5.88e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   1 MKILV----DENMPYARDLFSRLG-EVIAVPG--RPIPVAQLADADALMVRSVTKVNESL---LAGKPIKFVGTATAGTD 70
Cdd:cd12186   1 MKILMynvrDDEKPYIEEWAKEHPvEVDTTTEllTPETVDLAKGYDGVVVQQTLPYDEEVyekLAEYGIKQIALRSAGVD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  71 HVDEAWLKQAGIGFSAAPGC--NAIAvvEYVFSSLLMLAERDGFsLHERTVGIVGVGNVGrrLQAR-------------- 134
Cdd:cd12186  81 MIDLDLAKENGLKITNVPAYspRAIA--EFAVTQALNLLRNTPE-IDRRVAKGDFRWAPG--LIGReirdltvgiigtgr 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 135 --------LEALGIKTLLCDP-PRADCGDEGDFR-SLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILI 204
Cdd:cd12186 156 igsaaakiFKGFGAKVIAYDPyPNPELEKFLLYYdSLEDLLKQADIISLHVPLTKE----NHHLINAEAFAKMKDGAILV 231
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 205 NACRGAVVDNTALLTCLNEGQKLSVVLDVWEGE-----------PELNVELLTKVD----IGTPHIAGYT 259
Cdd:cd12186 232 NAARGGLVDTKALIDALDSGKIAGAALDTYENEtgyfnkdwsgkEIEDEVLKELIAmpnvLITPHIAFYT 301
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
31-265 1.79e-29

D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase(D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-2-hydroxyisocaproate dehydrogenase-like (HicDH) proteins are NAD-dependent members of the hydroxycarboxylate dehydrogenase family, and share the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240663 [Multi-domain]  Cd Length: 329  Bit Score: 116.22  E-value: 1.79e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  31 PVAQLADADALMVRSVTKVNESLLAGKP-IKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAER 109
Cdd:cd12187  35 NVEEFKDAEVISVFVYSRLDAEVLEKLPrLKLIATRSTGFDHIDLEACRERGIAVCNVPDYGEATVAEHAFALLLALSRK 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 110 ------------------DGFSLHERTVGIVGVGNVGRRLQARLEALGIKTLLCDP-PRADCGDEGDFR--SLDELVQRA 168
Cdd:cd12187 115 lreaiertrrgdfsqaglRGFELAGKTLGVVGTGRIGRRVARIARGFGMKVLAYDVvPDEELAERLGFRyvSLEELLQES 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 169 DILTFHTPLFKdgpyKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPEL-------- 240
Cdd:cd12187 195 DIISLHVPYTP----QTHHLINRENFALMKPGAVLINTARGAVVDTEALVRALKEGKLAGAGLDVLEQEEVLreeaelfr 270
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15832458 241 -------------NVELLTKVD-IGTPHIAGYTLEGKAR 265
Cdd:cd12187 271 edvspedlkkllaDHALLRKPNvIITPHVAYNTKEALER 309
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
1-263 2.37e-29

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240655 [Multi-domain]  Cd Length: 317  Bit Score: 115.41  E-value: 2.37e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   1 MKILVDENMPyaRDLFSRLG---EVIAVPG-RPIPVAQL----ADADALMVRSVTKVNESLL-AGKPIKFVGTATAGTDH 71
Cdd:cd12178   1 AKVLVTGWIP--KEALEELEenfEVTYYDGlGLISKEELleriADYDALITPLSTPVDKEIIdAAKNLKIIANYGAGFDN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  72 VDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAER---------------------DGFSLHERTVGIVGVGNVGRR 130
Cdd:cd12178  79 IDVDYAKEKGIPVTNTPAVSTEPTAELTFGLILALARRiaegdrlmrrggflgwaplffLGHELAGKTLGIIGMGRIGQA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 131 LQARLEALGIKTLLCDPPRADCGDE----GDFRSLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINA 206
Cdd:cd12178 159 VARRAKAFGMKILYYNRHRLSEETEkelgATYVDLDELLKESDFVSLHAPYTPE----THHLIDAAAFKLMKPTAYLINA 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15832458 207 CRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPELNVELLtKVD--IGTPHIAGYTLEGK 263
Cdd:cd12178 235 ARGPLVDEKALVDALKTGEIAGAALDVFEFEPEVSPELK-KLDnvILTPHIGNATVEAR 292
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
1-261 4.47e-29

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.


Pssm-ID: 240651 [Multi-domain]  Cd Length: 305  Bit Score: 114.58  E-value: 4.47e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   1 MKILV-DENMPYARDLFSRLGEVIAVpgrpipvAQLADADALMVRSvtKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQ 79
Cdd:cd12174   1 MKILTaNKISKKGLERFKKDKYEVKE-------DALEDPDALIVRS--DKLHDMDFAPSLKAIARAGAGVNNIDVDAASK 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  80 AGIGFSAAPGCNAIAVVEYVFSSLLMLAER--DGFSLHERTVGIVGVGNVG-------------------------RRLQ 132
Cdd:cd12174  72 RGIVVFNTPGANANAVAELVIAMMLALSRNiiQAIKWVTNGDGDDISKGVEkgkkqfvgtelrgktlgviglgnigRLVA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 133 ARLEALGIKTLLCDPP----RADCGDEGDFR--SLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINA 206
Cdd:cd12174 152 NAALALGMKVIGYDPYlsveAAWKLSVEVQRvtSLEELLATADYITLHVPLTDE----TRGLINAELLAKMKPGAILLNF 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15832458 207 CRGAVVDNTALLTCLNEGQKLSVVLDVweGEPELNVELltKVDIGTPHIAGYTLE 261
Cdd:cd12174 228 ARGEIVDEEALLEALDEGKLGGYVTDF--PEPALLGHL--PNVIATPHLGASTEE 278
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
32-265 6.39e-29

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240639 [Multi-domain]  Cd Length: 307  Bit Score: 114.09  E-value: 6.39e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  32 VAQLADADALMVRSVtKVNESLLAGKP-IKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLA--- 107
Cdd:cd12162  39 VERIKDADIVITNKV-VLDAEVLAQLPnLKLIGVLATGYNNVDLAAAKERGITVTNVPGYSTDSVAQHTFALLLALArlv 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 108 ------ERDG-------FSLHE--------RTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADCGDEGdFRSLDELVQ 166
Cdd:cd12162 118 ayhndvVKAGewqkspdFCFWDypiielagKTLGIIGYGNIGQAVARIARAFGMKVLFAERKGAPPLREG-YVSLDELLA 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 167 RADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEP-ELNVELL 245
Cdd:cd12162 197 QSDVISLHCPLTPE----TRNLINAEELAKMKPGAILINTARGGLVDEQALADALNSGKIAGAGLDVLSQEPpRADNPLL 272
                       250       260
                ....*....|....*....|..
gi 15832458 246 TKVD--IGTPHIAGYTLEGKAR 265
Cdd:cd12162 273 KAAPnlIITPHIAWASREARQR 294
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
1-259 1.10e-27

C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related repressor; The transcriptional corepressor CtBP is a dehydrogenase with sequence and structural similarity to the d2-hydroxyacid dehydrogenase family. CtBP was initially identified as a protein that bound the PXDLS sequence at the adenovirus E1A C terminus, causing the loss of CR-1-mediated transactivation. CtBP binds NAD(H) within a deep cleft, undergoes a conformational change upon NAD binding, and has NAD-dependent dehydrogenase activity.


Pssm-ID: 240624 [Multi-domain]  Cd Length: 312  Bit Score: 110.68  E-value: 1.10e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   1 MKILV-DENMP---YARDLFSRLG-EVIAVPGRPIP--VAQLADADALMVRSvTKVNESLLAG-KPIKFVGTATAGTDHV 72
Cdd:cd05299   1 PKVVItDYDFPdldIEREVLEEAGvELVDAQSRTEDelIEAAADADALLVQY-APVTAEVIEAlPRLKVIVRYGVGVDNV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  73 DEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAeRDGFSLHERTVG---IVGVGNVGRRLQ----------------- 132
Cdd:cd05299  80 DVAAATERGIPVCNVPDYCTEEVADHALALILALA-RKLPFLDRAVRAggwDWTVGGPIRRLRgltlglvgfgrigrava 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 133 ARLEALGIKTLLCDPPRADCGDEGDFR---SLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRG 209
Cdd:cd05299 159 KRAKAFGFRVIAYDPYVPDGVAALGGVrvvSLDELLARSDVVSLHCPLTPE----TRHLIDAEALALMKPGAFLVNTARG 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15832458 210 AVVDNTALLTCLNEGQKLSVVLDVWEGEPELNVELLTKVD--IGTPHIAGYT 259
Cdd:cd05299 235 GLVDEAALARALKSGRIAGAALDVLEEEPPPADSPLLSAPnvILTPHAAWYS 286
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
2-263 4.07e-27

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240656 [Multi-domain]  Cd Length: 306  Bit Score: 109.30  E-value: 4.07e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   2 KIL-VDENMPYARDLFSRLG-EVIAVP--GRPIPVAQLADADALMVRSVTKVNESLL-AGKPIKFVGTATAGTDHVDEAW 76
Cdd:cd12179   1 KILiIDKNHPSLTELLEALGfEVDYDPtiSREEILAIIPQYDGLIIRSRFPIDKEFIeKATNLKFIARAGAGLENIDLEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  77 LKQAGIGFSAAPGCNAIAVVEYVFSSLLML------------------AERDGFSLHERTVGIVGVGNVGRRLQARLEAL 138
Cdd:cd12179  81 AKEKGIELFNAPEGNRDAVGEHALGMLLALfnklnradqevrngiwdrEGNRGVELMGKTVGIIGYGNMGKAFAKRLSGF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 139 GIKTLLCDPPRaDCGDEGDFR-SLDELVQRADILTFHTPLFKdgpyKTLHLADEKLIRSLKPGAILINACRGAVVDNTAL 217
Cdd:cd12179 161 GCKVIAYDKYK-NFGDAYAEQvSLETLFKEADILSLHIPLTP----ETRGMVNKEFISSFKKPFYFINTARGKVVVTKDL 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15832458 218 LTCLNEGQKLSVVLDVWEGE----------PElNVELLTKVD--IGTPHIAGYTLEGK 263
Cdd:cd12179 236 VKALKSGKILGACLDVLEYEkasfesifnqPE-AFEYLIKSPkvILTPHIAGWTFESY 292
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
1-261 5.67e-27

D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase, HPR) catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. In humans, HPR deficiency causes primary hyperoxaluria type 2, characterized by over-excretion of L-glycerate and oxalate in the urine, possibly due to an imbalance in competition with L-lactate dehydrogenase, another formate dehydrogenase (FDH)-like enzyme. GDH, like FDH and other members of the D-specific hydroxyacid dehydrogenase family that also includes L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase, typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form, despite often low sequence identity. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240626 [Multi-domain]  Cd Length: 309  Bit Score: 108.64  E-value: 5.67e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   1 MKILVDENMP-YARDLFSRLGEVIAVPG-RPIPVAQL----ADADALMVRSVTKVNESLL-AGKPIKFVGTATAGTDHVD 73
Cdd:cd05301   1 PKVLVTRRLPeEALALLREGFEVEVWDEdRPLPREELleaaKGADGLLCTLTDKIDAELLdAAPPLKVIANYSVGYDHID 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  74 EAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAER---------------------DGFSLHERTvgivgvgnvgrrL- 131
Cdd:cd05301  81 VDAAKARGIPVTNTPDVLTDATADLAFALLLAAARRvvegdrfvragewkgwsptllLGTDLHGKT------------Lg 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 132 --------QA---RLEALGIKTLLCDPPRADCGDEGD---FRSLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSL 197
Cdd:cd05301 149 ivgmgrigQAvarRAKGFGMKILYHNRSRKPEAEEELgarYVSLDELLAESDFVSLHCPLTPE----TRHLINAERLALM 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832458 198 KPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPELNVELLTKVD--IGTPHIAGYTLE 261
Cdd:cd05301 225 KPTAILINTARGGVVDEDALVEALKSGKIAGAGLDVFEPEPLPADHPLLTLPnvVLLPHIGSATVE 290
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
50-272 2.50e-26

D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified as an enzyme that interconverts benzoylformate and D-mandelate, is a D-2-hydroxyacid dehydrogenase family member that catalyzes the conversion of c3-branched 2-ketoacids. D-ManDH exhibits broad substrate specificities for 2-ketoacids with large hydrophobic side chains, particularly those with C3-branched side chains. 2-hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Glycerate dehydrogenase catalyzes the reaction (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240645 [Multi-domain]  Cd Length: 321  Bit Score: 107.25  E-value: 2.50e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  50 NESLLAGKP--IKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEY-VFsslLMLAERDGFSLHERTVGIVGVGN 126
Cdd:cd12168  66 DEELISPLPpsLKIIAHAGAGYDQIDVDALTKRGIQVSNTPGAVDEATADTaLF---LILGALRNFSRAERSARAGKWRG 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 127 VG----------------------RRLQARLEALGIKTLLCDPPRADCGDEGD----FRSLDELVQRADILTFHTPLFKD 180
Cdd:cd12168 143 FLdltlahdprgktlgilglggigKAIARKAAAFGMKIIYHNRSRLPEELEKAlatyYVSLDELLAQSDVVSLNCPLTAA 222
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 181 gpykTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPELNVELLT--KVdIGTPHIAGY 258
Cdd:cd12168 223 ----TRHLINKKEFAKMKDGVIIVNTARGAVIDEDALVDALESGKVASAGLDVFENEPEVNPGLLKmpNV-TLLPHMGTL 297
                       250
                ....*....|....
gi 15832458 259 TLEGKARGTTQVFE 272
Cdd:cd12168 298 TVETQEKMEELVLE 311
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
32-284 5.47e-26

Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy dehydrogenase family; This group contains a variety of proteins variously identified as glycerate dehydrogenase (GDH, aka Hydroxypyruvate Reductase) and other enzymes of the 2-hydroxyacid dehydrogenase family. GDH catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. 2-hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240638 [Multi-domain]  Cd Length: 315  Bit Score: 106.15  E-value: 5.47e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  32 VAQLADADALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLML----- 106
Cdd:cd12161  43 IERSKDADIVMIANMPLPGEVIEACKNLKMISVAFTGVDHVDLEACKERGITVSNAAGYSTEAVAELTIGLAIDLlrniv 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 107 ----AERD--------GFSLHERTVGIVGVGNVGRRLQARLEALGIKTLLCDP-PRADCGDEG-DFRSLDELVQRADILT 172
Cdd:cd12161 123 pcdaAVRAggtkagliGRELAGKTVGIVGTGAIGLRVARLFKAFGCKVLAYSRsEKEEAKALGiEYVSLDELLAESDIVS 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 173 FHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPEL--NVELL-TKVD 249
Cdd:cd12161 203 LHLPLNDE----TKGLIGKEKLALMKESAILINTARGPVVDNEALADALNEGKIAGAGIDVFDMEPPLpaDYPLLhAPNT 278
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15832458 250 IGTPHIAGYTLEGKARGTTQVFEAYSKFI-GHEQHV 284
Cdd:cd12161 279 ILTPHVAFATEEAMEKRAEIVFDNIEAWLaGKPQNV 314
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
1-265 1.00e-25

Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240653  Cd Length: 304  Bit Score: 105.35  E-value: 1.00e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   1 MKILVDENM-PYARDLFSRLG-EVIAVPGRPIP---VAQLADADALMVRSVTKVNESLL-AGKPIKFVGTATAGTDHVDE 74
Cdd:cd12176   1 IKILLLENIhPSADELFRAGGiEVERLKGALDEdelIEALKDVHLLGIRSKTQLTEEVLeAAPKLLAIGCFCIGTNQVDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  75 AWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAERdgfsLHERTVGIVGVG---NVGRRLQAR----------------- 134
Cdd:cd12176  81 DAAAKRGIPVFNAPFSNTRSVAELVIGEIIMLARR----LPDRNAAAHRGIwnkSATGSHEVRgktlgiigyghigsqls 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 135 --LEALGIKTLLCDP-PRADCGDEGDFRSLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAV 211
Cdd:cd12176 157 vlAEALGMRVIFYDIaEKLPLGNARQVSSLEELLAEADFVTLHVPATPS----TKNMIGAEEIAQMKKGAILINASRGTV 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 212 VDNTALLTCLNEGQKLSVVLDVWEGEPELNVEL----LTKVD--IGTPHIAGYTLEGKAR 265
Cdd:cd12176 233 VDIDALAEALRSGHLAGAAVDVFPEEPASNGEPfsspLQGLPnvILTPHIGGSTEEAQEN 292
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
129-256 1.08e-25

D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.


Pssm-ID: 427007 [Multi-domain]  Cd Length: 178  Bit Score: 101.80  E-value: 1.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   129 RRLQARLEALGIKTLLCDPPRADCGDEGD----FRSLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILI 204
Cdd:pfam02826  49 RAVAKRLKAFGMKVIAYDRYPKPEEEEEElgarYVSLDELLAESDVVSLHLPLTPE----TRHLINAERLALMKPGAILI 124
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15832458   205 NACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPELNVELLTKVD--IGTPHIA 256
Cdd:pfam02826 125 NTARGGLVDEDALIAALKSGRIAGAALDVFEPEPLPADHPLLDLPnvILTPHIA 178
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
12-272 1.10e-25

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240644 [Multi-domain]  Cd Length: 330  Bit Score: 105.72  E-value: 1.10e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  12 ARDLFSRLGEVIAVPGRPIP-----VAQLADADALmvrsVT-----KVNESLLAGKP-IKFVGTAtAGT--DHVDEAwLK 78
Cdd:cd12167  19 ALARLAALAEVLPPTPDADFaaeelRALLAGVEVL----VTgwgtpPLDAELLARAPrLRAVVHA-AGSvrGLVTDA-VW 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  79 QAGIGFSAAPGCNAIAVVEYVFSSLLMLAER--------------------DGFSLHERTVGIVGVGNVGRRLQARLEAL 138
Cdd:cd12167  93 ERGILVTSAADANAEPVAEFTLAAILLALRRiprfaaayragrdwgwptrrGGRGLYGRTVGIVGFGRIGRAVVELLRPF 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 139 GIKTLLCDP--PRADCGDEGDFR-SLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVVDNT 215
Cdd:cd12167 173 GLRVLVYDPylPAAEAAALGVELvSLDELLARSDVVSLHAPLTPE----TRGMIDARLLALMRDGATFINTARGALVDEA 248
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832458 216 ALLTCLNEGqKLSVVLDVWEGEP--------EL-NVELltkvdigTPHIAGYTLEGKARGTTQVFE 272
Cdd:cd12167 249 ALLAELRSG-RLRAALDVTDPEPlppdsplrTLpNVLL-------TPHIAGSTGDERRRLGDYALD 306
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
1-261 2.27e-25

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240648 [Multi-domain]  Cd Length: 310  Bit Score: 104.54  E-value: 2.27e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   1 MKILVDENMPYARDLFSRLGEVIAV-----PGRPIPVAQLA----DADALMVR--SVTKvnESLLAGKPIKFVGTATAGT 69
Cdd:cd12171   1 MKELETAPIDWPDEPFEDLQEVILVveksgPEAVEPEEELLealkDADILITHfaPVTK--KVIEAAPKLKLIGVCRGGP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  70 DHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSslLMLAE------------------------RDGFSLHERTVGIVGVG 125
Cdd:cd12171  79 ENVDVEAATERGIPVLNTPGRNAEAVAEFTVG--LMLAEtrniarahaalkdgewrkdyynydGYGPELRGKTVGIVGFG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 126 NVGRRLQARLEALGIKTLLCDP-----PRADCGDEGDfrSLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPG 200
Cdd:cd12171 157 AIGRRVAKRLKAFGAEVLVYDPyvdpeKIEADGVKKV--SLEELLKRSDVVSLHARLTPE----TRGMIGAEEFALMKPT 230
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 201 AILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEP-----EL----NVELltkvdigTPHIAGYTLE 261
Cdd:cd12171 231 AYFINTARAGLVDEDALIEALEEGKIGGAALDVFPEEPlpadhPLlkldNVTL-------TPHIAGATRD 293
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
32-261 2.73e-25

(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic domains; (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. HGDH is a member of the D-2-hydroxyacid NAD(+)-dependent dehydrogenase family; these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240660  Cd Length: 330  Bit Score: 104.68  E-value: 2.73e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  32 VAQLADADALMVRSVTKVNESLL---AGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAE 108
Cdd:cd12184  39 VHLAKGHDAVIVRGNCFADKENLeiyKEYGIKYVFTRTVGFNHIDLEAAKELGFKMARVPSYSPNAIAELAFTLAMTLSR 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 109 RDGFSLHER-----TVGIVGVGNVGRRL-------------QARL-EALGIKTLLCDP-PRADCGDEGDFRSLDELVQRA 168
Cdd:cd12184 119 HTAYTASRTanknfKVDPFMFSKEIRNStvgiigtgrigltAAKLfKGLGAKVIGYDIyPSDAAKDVVTFVSLDELLKKS 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 169 DILTFHTPLFKDgpyKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGE----------- 237
Cdd:cd12184 199 DIISLHVPYIKG---KNDKLINKEFISKMKDGAILINTARGELQDEEAILEALESGKLAGFGTDVLNNEkeiffkdfdgd 275
                       250       260       270
                ....*....|....*....|....*....|
gi 15832458 238 ----PELN--VELLTKVDIgTPHIAGYTLE 261
Cdd:cd12184 276 kiedPVVEklLDLYPRVLL-TPHIGSYTDE 304
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
7-277 5.21e-25

Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related dehydrogenases; The formate/glycerate dehydrogenase like family contains a diverse group of enzymes such as formate dehydrogenase (FDH), glycerate dehydrogenase (GDH), D-lactate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine hydrolase, that share a common 2-domain structure. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar domains of the alpha/beta Rossmann fold NAD+ binding form. The NAD(P) binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD(P) is bound, primarily to the C-terminal portion of the 2nd (internal) domain. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of a hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases.


Pssm-ID: 240631 [Multi-domain]  Cd Length: 310  Bit Score: 103.46  E-value: 5.21e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   7 ENMPYARDLFSRLG-EVIAVPGRPIPV------------------AQLADADALMVRSVTKVNES--LLAGKPIKFVGTA 65
Cdd:cd12154  15 GLSPSVVATLVEAGhEVRVETGAGIGAgfadqayvqagaivvtlaKALWSLDVVLKVKEPLTNAEyaLIQKLGDRLLFTY 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  66 TAGTDHVD-EAWLKQAGIGFSAAPG-------CNAIAVVEYVFSSLLMLAERDG-------FSLHERTVGIVGVGNVGRR 130
Cdd:cd12154  95 TIGADHRDlTEALARAGLTAIAVEGvelplltSNSIGAGELSVQFIARFLEVQQpgrlggaPDVAGKTVVVVGAGVVGKE 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 131 LQARLEALGIKTLLCDPPRADCGDEG-----DFRSLDELVQRADILTFHTPLfkdgPYKTLH-LADEKLIRSLKPGAILI 204
Cdd:cd12154 175 AAQMLRGLGAQVLITDINVEALEQLEelggkNVEELEEALAEADVIVTTTLL----PGKRAGiLVPEELVEQMKPGSVIV 250
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15832458 205 NACRGAVVDNTALLT-CLNEGQKLSVVLDVWEGEPELnvelltkvdigtphIAGYTLEGKARGTTQVFEAYSKF 277
Cdd:cd12154 251 NVAVGAVGCVQALHTqLLEEGHGVVHYGDVNMPGPGC--------------AMGVPWDATLRLAANTLPALVKL 310
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
10-257 7.40e-25

Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the D-specific 2-hydroxyacid dehydrogenase family, catalyzes the NAD-dependent formation of phosphate from phosphite (hydrogen phosphonate). PTDH has been suggested as a potential enzyme for cofactor regeneration systems. The D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD-binding domain.


Pssm-ID: 240634 [Multi-domain]  Cd Length: 318  Bit Score: 103.14  E-value: 7.40e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  10 PYARDLFSRLGEVIAVPGR-PIPVAQL----ADADALMVRSVTKVNESLLAGKP-IKFVGTATAGTDHVDEAWLKQAGIG 83
Cdd:cd12157  12 PEVLELLKPHCEVISNQTDePLSREELlrrcKDADGLMAFMPDRIDADFLDACPrLKIIACALKGYDNFDVEACTARGIW 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  84 FSAAPGCNAIAVVEYVFSSLLMLAE---------RDGF-----------SLHERTVGIVGVGNVGRRLQARLEALGIKTL 143
Cdd:cd12157  92 VTIVPDLLTEPTAELTIGLLIGLGRhilagdrfvRSGKfggwrpkfygtGLDGKTVGILGMGALGRAIARRLSGFGATLL 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 144 LCDPPRADCGDEGDFR----SLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVVDNTALLT 219
Cdd:cd12157 172 YYDPHPLDQAEEQALNlrrvELDELLESSDFLVLALPLTPD----TLHLINAEALAKMKPGALLVNPCRGSVVDEAAVAE 247
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15832458 220 CLNEGQKLSVVLDVWEGEP--------ELNVELLTKVD--IGTPHIAG 257
Cdd:cd12157 248 ALKSGHLGGYAADVFEMEDwarpdrprSIPQELLDQHDrtVFTPHIGS 295
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
1-272 3.13e-24

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240642 [Multi-domain]  Cd Length: 314  Bit Score: 101.17  E-value: 3.13e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   1 MKILV---DENMPYARDLFSRLGEVIAVPGRPIPVAQLADADALMVrSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWL 77
Cdd:cd12165   1 MKVLVnfkAELREEFEAALEGLYAEVPELPDEAAEEALEDADVLVG-GRLTKEEALAALKRLKLIQVPSAGVDHLPLERL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  78 KqAGIGFSAAPGcNAIAVVEYVFSSLLMLAER-------------DGF--------SLHERTVGIVGVGNVGRRLQARLE 136
Cdd:cd12165  80 P-EGVVVANNHG-NSPAVAEHALALILALAKRiveydndlrrgiwHGRageepeskELRGKTVGILGYGHIGREIARLLK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 137 ALGIKTLLCD--PPRADCGDE-GDFRSLDELVQRADILTFHTPLFKdgpyKTLHLADEKLIRSLKPGAILINACRGAVVD 213
Cdd:cd12165 158 AFGMRVIGVSrsPKEDEGADFvGTLSDLDEALEQADVVVVALPLTK----QTRGLIGAAELAAMKPGAILVNVGRGPVVD 233
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15832458 214 NTALLTCLNEGQKLSVVLDVWEGEPE-----LNVEL-LTKVD--IGTPHIAGYTLEGKARGTTQVFE 272
Cdd:cd12165 234 EEALYEALKERPIAGAAIDVWWRYPSrgdpvAPSRYpFHELPnvIMSPHNAGWTEETFRRRIDEAAE 300
HGDH_LDH_like cd12185
Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, ...
1-259 6.80e-24

Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, NAD-binding and catalytic domains; This group contains various putative dehydrogenases related to D-lactate dehydrogenase (LDH), (R)-2-hydroxyglutarate dehydrogenase (HGDH), and related enzymes, members of the 2-hydroxyacid dehydrogenases family. LDH catalyzes the interconversion of pyruvate and lactate, and HGDH catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. Despite often low sequence identity within this 2-hydroxyacid dehydrogenase family, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240661  Cd Length: 322  Bit Score: 100.36  E-value: 6.80e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   1 MKILVDENMPYARDLFSRLG-----EVIAVPGRPIP-VAQLAD-ADALMVRSVTKVNESLL-----AGkpIKFVGTATAG 68
Cdd:cd12185   1 MKIFAYGVRPDELEYFEKFAkeynvEVTLTKEPLTLeNAHLAEgYDGISILGKSKISAELLeklkeAG--VKYISTRSIG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  69 TDHVDEAWLKQAGIGFSAA---PGCnaiaVVEYVFSSLLML----------AERDGFSL--------HERTVGIVGVGNV 127
Cdd:cd12185  79 YDHIDLDAAKELGIKVSNVtysPNS----VADYTVMLMLMAlrkykqimkrAEVNDYSLgglqgrelRNLTVGVIGTGRI 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 128 GRRLQARLEALGIKTLLCDP-PRADCGDEGDFRSLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINA 206
Cdd:cd12185 155 GQAVIKNLSGFGCKILAYDPyPNEEVKKYAEYVDLDTLYKESDIITLHTPLTEE----TYHLINKESIAKMKDGVIIINT 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832458 207 CRGAVVDNTALLTCLNEGQKLSVVLDVWEGE---------------PELNVELLTKVDIGTPHIAGYT 259
Cdd:cd12185 231 ARGELIDTEALIEGLESGKIGGAALDVIEGEdgiyyndrkgdilsnRELAILRSFPNVILTPHMAFYT 298
PRK13243 PRK13243
glyoxylate reductase; Reviewed
26-265 2.75e-22

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 96.40  E-value: 2.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   26 PGRPIPVAQLADADALMVRSVTKVNESLLAGKP-IKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLL 104
Cdd:PRK13243  34 IPREVLLEKVRDVDALVTMLSERIDCEVFEAAPrLRIVANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADFAWALLL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  105 MLAER----D---------------------GFSLHERTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADCGDE---G 156
Cdd:PRK13243 114 ATARRlveaDhfvrsgewkrrgvawhplmflGYDVYGKTIGIIGFGRIGQAVARRAKGFGMRILYYSRTRKPEAEKelgA 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  157 DFRSLDELVQRADILTFHTPLFKdgpyKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEG 236
Cdd:PRK13243 194 EYRPLEELLRESDFVSLHVPLTK----ETYHMINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDVFEE 269
                        250       260       270
                 ....*....|....*....|....*....|
gi 15832458  237 EPELNVELLT-KVDIGTPHIAGYTLEGKAR 265
Cdd:PRK13243 270 EPYYNEELFSlKNVVLAPHIGSATFEAREG 299
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
136-281 1.29e-20

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240654 [Multi-domain]  Cd Length: 321  Bit Score: 91.23  E-value: 1.29e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 136 EALGIKTLLCDP--PRADCGDEGDFR-SLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVV 212
Cdd:cd12177 168 EGFNAKVLAYDPyvSEEVIKKKGAKPvSLEELLAESDIISLHAPLTEE----TYHMINEKAFSKMKKGVILVNTARGELI 243
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15832458 213 DNTALLTCLNEGQKLSVVLDVWEGEP-ELNVELLT--KVDIgTPHIAGYTLEGKARGTTQVFEAYSKFIGHE 281
Cdd:cd12177 244 DEEALIEALKSGKIAGAGLDVLEEEPiKADHPLLHyeNVVI-TPHIGAYTYESLYGMGEKVVDDIEDFLAGK 314
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
35-274 1.03e-18

NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of a formate anion to carbon dioxide coupled with the reduction of NAD+ to NADH. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family have 2 highly similar subdomains of the alpha/beta form, with NAD binding occurring in the cleft between subdomains. NAD contacts are primarily to the Rossmann-fold NAD-binding domain which is inserted within the linear sequence of the more diverse flavodoxin-like catalytic subdomain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production from C1 compounds such as methanol, and in the stress responses of plants. NAD-dependent FDH is useful in cofactor regeneration in asymmetrical biocatalytic reduction processes, where FDH irreversibly oxidizes formate to carbon dioxide, while reducing the oxidized form of the cofactor to the reduced form.


Pssm-ID: 240627  Cd Length: 348  Bit Score: 86.23  E-value: 1.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  35 LADADALMVRS-----VTKvnESLLAGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLML--- 106
Cdd:cd05302  58 LPDADVVISTPfhpayMTA--ERIAKAKNLKLALTAGIGSDHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILvrn 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 107 -----------------AERDGFSLHERTVGIVGVGNVGRRLQARLEALGIKTLLCDPPR--ADCGDEGD---FRSLDEL 164
Cdd:cd05302 136 yvpgheqaieggwnvadVVKRAYDLEGKTVGTVGAGRIGLRVLRRLKPFDVHLLYYDRHRlpEEVEKELGltrHADLEDM 215
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 165 VQRADILTFHTPLFKdgpyKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPE-LNVE 243
Cdd:cd05302 216 VSKCDVVTINCPLHP----ETEGLFNKELLSKMKKGAYLVNTARGKICDREAVAEALESGHLAGYAGDVWFPQPApKDHP 291
                       250       260       270
                ....*....|....*....|....*....|....*
gi 15832458 244 LLTKVDIG-TPHIAGYTLEGKAR---GTTQVFEAY 274
Cdd:cd05302 292 WRTMPNNAmTPHISGTTLDAQARyaaGTKEILERF 326
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
3-261 3.22e-18

Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; Hydroxy(phenyl)pyruvate reductase (HPPR) catalyzes the NADP-dependent reduction of hydroxyphenylpyruvates, hydroxypyruvate, or pyruvate to its respective lactate. HPPR acts as a dimer and is related to D-isomer-specific 2-hydroxyacid dehydrogenases, a superfamily that includes groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240633 [Multi-domain]  Cd Length: 301  Bit Score: 84.06  E-value: 3.22e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   3 ILVDENMPYARDLFSRLGEVIAVPGRPIPVAQLA----DADALMVRSVTKVNESLLAGKP-IKFVGTATAGTDHVDEAWL 77
Cdd:cd12156   4 LQLGPLPPELLAELEARFTVHRLWEAADPAALLAehggRIRAVVTNGETGLSAALIAALPaLELIASFGVGYDGIDLDAA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  78 KQAGIGFSAAPGCNAIAVVEYVFSSLLMLAE---------RDG------FSLHERTVGivgvgnvgRRL---------QA 133
Cdd:cd12156  84 RARGIRVTNTPGVLTDDVADLAVGLLLAVLRripaadrfvRAGrwpkgaFPLTRKVSG--------KRVgivglgrigRA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 134 ---RLEALGIKTLLCDPPRADCGDEGDFRSLDELVQRADILTFHTPLfkdGPyKTLHLADEKLIRSLKPGAILINACRGA 210
Cdd:cd12156 156 iarRLEAFGMEIAYHGRRPKPDVPYRYYASLLELAAESDVLVVACPG---GP-ATRHLVNAEVLEALGPDGVLVNVARGS 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 15832458 211 VVDNTALLTCLNEGQKLSVVLDVWEGEPELNVELLTkVD--IGTPHIAGYTLE 261
Cdd:cd12156 232 VVDEAALIAALQEGRIAGAGLDVFENEPNVPAALLD-LDnvVLTPHIASATVE 283
PRK07574 PRK07574
NAD-dependent formate dehydrogenase;
57-274 4.46e-18

NAD-dependent formate dehydrogenase;


Pssm-ID: 181041  Cd Length: 385  Bit Score: 84.73  E-value: 4.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   57 KPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAE---------RDG-----------FSLHE 116
Cdd:PRK07574 113 PNLKLAITAGIGSDHVDLQAASEHGITVAEVTGSNSISVAEHVVMMILALVRnyepshrqaVEGgwniadcvsrsYDLEG 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  117 RTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADCGDEGD-----FRSLDELVQRADILTFHTPLFKDgpykTLHLADE 191
Cdd:PRK07574 193 MTVGIVGAGRIGLAVLRRLKPFDVKLHYTDRHRLPEEVEQElgltyHVSFDSLVSVCDVVTIHCPLHPE----TEHLFDA 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  192 KLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEP--------ELNVELLtkvdigTPHIAGYTLEGK 263
Cdd:PRK07574 269 DVLSRMKRGSYLVNTARGKIVDRDAVVRALESGHLAGYAGDVWFPQPapadhpwrTMPRNGM------TPHISGTTLSAQ 342
                        250
                 ....*....|....
gi 15832458  264 AR---GTTQVFEAY 274
Cdd:PRK07574 343 ARyaaGTREILECF 356
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
1-259 5.21e-18

Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomains but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants.


Pssm-ID: 240625 [Multi-domain]  Cd Length: 313  Bit Score: 83.73  E-value: 5.21e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   1 MKILV-----DENMPYARDLFSRLGEVIAVPGRPIpvAQLADADALMVRSVTKvnESLLAGKPIKFVGTATAGTDHVDEA 75
Cdd:cd05300   1 MKILVlspldDEHLERLRAAAPGAELRVVTAEELT--EELADADVLLGNPPLP--ELLPAAPRLRWIQSTSAGVDALLFP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  76 WLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLA-----------------ERDGFSLHERTVGIVGVGNVGRRLQARLEAL 138
Cdd:cd05300  77 ELLERDVVLTNARGIFGPPIAEYVLGYMLAFArklpryarnqaerrwqrRGPVRELAGKTVLIVGLGDIGREIARRAKAF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 139 GIKTLLCD---PPRADCGDE-GDFRSLDELVQRADIL---TFHTPlfkdgpyKTLHLADEKLIRSLKPGAILINACRGAV 211
Cdd:cd05300 157 GMRVIGVRrsgRPAPPVVDEvYTPDELDELLPEADYVvnaLPLTP-------ETRGLFNAERFAAMKPGAVLINVGRGSV 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15832458 212 VDNTALLTCLNEGQKLSVVLDVWEGEPeL----------NVelltkvdIGTPHIAGYT 259
Cdd:cd05300 230 VDEDALIEALESGRIAGAALDVFEEEP-LpadsplwdlpNV-------IITPHISGDS 279
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
139-240 7.23e-17

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2-domain structure of formate dehydrogenase. D-2-hydroxyisocaproate dehydrogenase-like (HicDH) proteins are NAD-dependent members of the hydroxycarboxylate dehydrogenase family, and share the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240659  Cd Length: 328  Bit Score: 80.57  E-value: 7.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 139 GIKTLLCDP-PRADCGDEG-DFRSLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVVDNTA 216
Cdd:cd12183 167 GCRVLAYDPyPNPELAKLGvEYVDLDELLAESDIISLHCPLTPE----THHLINAETIAKMKDGVMLINTSRGGLIDTKA 242
                        90       100
                ....*....|....*....|....
gi 15832458 217 LLTCLNEGQKLSVVLDVWEGEPEL 240
Cdd:cd12183 243 LIEALKSGKIGGLGLDVYEEEAGL 266
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
1-273 7.89e-17

Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate Dehydrogenase (PGDH) catalyzes the NAD-dependent conversion of 3-phosphoglycerate into 3-phosphohydroxypyruvate, which is the first step in serine biosynthesis. Over-expression of PGDH has been implicated as supporting proliferation of certain breast cancers, while PGDH deficiency is linked to defects in mammalian central nervous system development. PGDH is a member of the 2-hydroxyacid dehydrogenase family, enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240632 [Multi-domain]  Cd Length: 314  Bit Score: 80.32  E-value: 7.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   1 MKIL----VDENMPYARDLFSRLgEVIaVPGRPIPVAQLADADALMVRSvTKVNESLLAGKP-IKFVGTATAGTDHVDEA 75
Cdd:cd12155   1 KKLLtldyGDEKEEQIEDLGYDV-DVV-FEDELSDEEDLEDIEILYGYN-PDFDELDLAKMKnLKWIQLYSAGVDYLPLE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  76 WLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAERDGFSLHERTVGIVGVGNVGRRLQ-----------------ARLEAL 138
Cdd:cd12155  78 YIKKKGILLTNNSGIHSIPIAEWIVGYILEIYKGLKKAYKNQKEKKWKMDSSLLELYgktilflgtgsigqeiaKRLKAF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 139 GIKTLlcdppradcgdeGDFRS---------------LDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAIL 203
Cdd:cd12155 158 GMKVI------------GVNTSgrdveyfdkcypleeLDEVLKEADIVVNVLPLTEE----THHLFDEAFFEQMKKGALF 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15832458 204 INACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEP-ELNVEL--LTKVDIgTPHIAGYTlEGKARGTTQVFEA 273
Cdd:cd12155 222 INVGRGPSVDEDALIEALKNKQIRGAALDVFEEEPlPKDSPLwdLDNVLI-TPHISGVS-EHFNERLFDIFYE 292
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
32-278 1.62e-16

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 79.26  E-value: 1.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   32 VAQLADADALMVRSVtKVNESLLAGKP-IKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLML---- 106
Cdd:PRK08410  37 IERIKDANIIITNKV-VIDKEVLSQLPnLKLICITATGTNNVDIEYAKKKGIAVKNVAGYSTESVAQHTFAMLLSLlgri 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  107 ------------AERDGFSLHERTVGIVGVG--------NVGRRLqARL-EALGIKTLLCDPPRADCGDEGDFRSLDELV 165
Cdd:PRK08410 116 nyydryvksgeySESPIFTHISRPLGEIKGKkwgiiglgTIGKRV-AKIaQAFGAKVVYYSTSGKNKNEEYERVSLEELL 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  166 QRADILTFHTPLFKdgpyKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGqKLSVVLDVWEGEP-ELNVEL 244
Cdd:PRK08410 195 KTSDIISIHAPLNE----KTKNLIAYKELKLLKDGAILINVGRGGIVNEKDLAKALDEK-DIYAGLDVLEKEPmEKNHPL 269
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 15832458  245 LTKVD----IGTPHIAGYTLEGKARGTTQVFEAYSKFI 278
Cdd:PRK08410 270 LSIKNkeklLITPHIAWASKEARKTLIEKVKENIKDFL 307
PRK06487 PRK06487
2-hydroxyacid dehydrogenase;
28-280 1.84e-16

2-hydroxyacid dehydrogenase;


Pssm-ID: 180588 [Multi-domain]  Cd Length: 317  Bit Score: 79.36  E-value: 1.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   28 RPIPVAQ-LADADALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLML 106
Cdd:PRK06487  35 TPEQVAErLRGAQVAISNKVALDAAALAAAPQLKLILVAATGTNNVDLAAARERGITVCNCQGYGTPSVAQHTLALLLAL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  107 AER---------DG------------FSLHE---RTVGIVGVGNVGRRLqARL-EALGIKTLLCD----PPRADcgdegd 157
Cdd:PRK06487 115 ATRlpdyqqavaAGrwqqssqfclldFPIVElegKTLGLLGHGELGGAV-ARLaEAFGMRVLIGQlpgrPARPD------ 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  158 fR-SLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEG 236
Cdd:PRK06487 188 -RlPLDELLPQVDALTLHCPLTEH----TRHLIGARELALMKPGALLINTARGGLVDEQALADALRSGHLGGAATDVLSV 262
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 15832458  237 EPELNVELLTKVDIG----TPHIAGYTLEGKARGTTQVFE-AYSKFIGH 280
Cdd:PRK06487 263 EPPVNGNPLLAPDIPrlivTPHSAWGSREARQRIVGQLAEnARAFFAGK 311
PRK11790 PRK11790
phosphoglycerate dehydrogenase;
1-261 5.67e-16

phosphoglycerate dehydrogenase;


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 78.68  E-value: 5.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458    1 MKILVDENM-PYARDLFSRLG--EVIAVPGRPIP---VAQLADADALMVRSVTKVNESLLAGKPiKF--VGTATAGTDHV 72
Cdd:PRK11790  11 IKFLLLEGVhQSAVEVLRAAGytNIEYHKGALDEeelIEAIKDAHFIGIRSRTQLTEEVLAAAE-KLvaIGCFCIGTNQV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   73 DEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAerdgfslhertvgivgvgnvgRRLQAR------------------ 134
Cdd:PRK11790  90 DLDAAAKRGIPVFNAPFSNTRSVAELVIGEIILLL---------------------RGIPEKnakahrggwnksaagsfe 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  135 ---------------------LEALGIKTLLCDP-PRADCGDEGDFRSLDELVQRADILTFHTPlfkDGPyKTLHLADEK 192
Cdd:PRK11790 149 vrgktlgivgyghigtqlsvlAESLGMRVYFYDIeDKLPLGNARQVGSLEELLAQSDVVSLHVP---ETP-STKNMIGAE 224
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15832458  193 LIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPELNVEL----LTKVD--IGTPHIAGYTLE 261
Cdd:PRK11790 225 ELALMKPGAILINASRGTVVDIDALADALKSGHLAGAAIDVFPVEPKSNGDPfespLRGLDnvILTPHIGGSTQE 299
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
32-273 6.17e-16

Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.


Pssm-ID: 240646 [Multi-domain]  Cd Length: 308  Bit Score: 77.55  E-value: 6.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  32 VAQLADADALMV-RSVTKVNESLLAGKP-IKFVGTATAGTDHVDEAWLKQAGIGFSAAPGcNAIAVVEYVFSSLLMLAER 109
Cdd:cd12169  41 AERLAPFDAIVLmRERTPFPAALLERLPnLKLLVTTGMRNASIDLAAAKERGIVVCGTGG-GPTATAELTWALILALARN 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 110 ----------------DGFSLHERTVGIVGVGNVGRRLQARLEALGIKTLL----CDPPRADCGDEGDFRSLDELVQRAD 169
Cdd:cd12169 120 lpeedaalraggwqttLGTGLAGKTLGIVGLGRIGARVARIGQAFGMRVIAwssnLTAERAAAAGVEAAVSKEELFATSD 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 170 ILTFHTPLFKdgpyKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPELNVELLTKVD 249
Cdd:cd12169 200 VVSLHLVLSD----RTRGLVGAEDLALMKPTALLVNTSRGPLVDEGALLAALRAGRIAGAALDVFDVEPLPADHPLRGLP 275
                       250       260
                ....*....|....*....|....*..
gi 15832458 250 --IGTPHIaGYTLEGKARG-TTQVFEA 273
Cdd:cd12169 276 nvLLTPHI-GYVTEEAYEGfYGQAVEN 301
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
160-259 1.62e-15

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 76.71  E-value: 1.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  160 SLDELVQRADILTFHTPLFKDGPyktlHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGE-- 237
Cdd:PRK08605 193 TIEEAVEGADIVTLHMPATKYNH----YLFNADLFKHFKKGAVFVNCARGSLVDTKALLDALDNGLIKGAALDTYEFErp 268
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15832458  238 --------PELN----VELLTKVD-IGTPHIAGYT 259
Cdd:PRK08605 269 lfpsdqrgQTINdpllESLINREDvILTPHIAFYT 303
PRK06932 PRK06932
2-hydroxyacid dehydrogenase;
32-256 1.22e-13

2-hydroxyacid dehydrogenase;


Pssm-ID: 235890 [Multi-domain]  Cd Length: 314  Bit Score: 70.98  E-value: 1.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   32 VAQLADADALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSL------LM 105
Cdd:PRK06932  39 IERAKDADIVITSKVLFTRETLAQLPKLKLIAITATGTNNVDLVAAKELGIAVKNVTGYSSTTVPEHVLGMIfalkhsLM 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  106 LAERDGFS------------------LHERTVGIVGVGNVGRRLqARL-EALGIKTLLCDPPRADCGDEGdFRSLDELVQ 166
Cdd:PRK06932 119 GWYRDQLSdrwatckqfcyfdypitdVRGSTLGVFGKGCLGTEV-GRLaQALGMKVLYAEHKGASVCREG-YTPFEEVLK 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  167 RADILTFHTPLFKdgpyKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGE-PELNVELL 245
Cdd:PRK06932 197 QADIVTLHCPLTE----TTQNLINAETLALMKPTAFLINTGRGPLVDEQALLDALENGKIAGAALDVLVKEpPEKDNPLI 272
                        250
                 ....*....|....*.
gi 15832458  246 TKVD-----IGTPHIA 256
Cdd:PRK06932 273 QAAKrlpnlLITPHIA 288
2-Hacid_dh_15 cd12180
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
21-238 2.55e-12

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240657  Cd Length: 308  Bit Score: 66.98  E-value: 2.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  21 EVIAVPGRPiPVAQLADADALMVRSvTKVNESLLAGKP------IKFVGTATAGTDHVdEAWLKQAGIgFSAAPGCNAIA 94
Cdd:cd12180  23 EVIEVPPGP-AWDLPADADVLLARP-TNGRGAAPAVPPpgwpgrLRWVQLVSSGIDYY-PDWLFEGPV-VTCARGVAAEA 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  95 VVEYVFSSLLMLAER--------DGF-------SLHERTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADCGDEG--D 157
Cdd:cd12180  99 IAEFVLAAILAAAKRlpeiwvkgAEQwrreplgSLAGSTLGIVGFGAIGQALARRALALGMRVLALRRSGRPSDVPGveA 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 158 FRSLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGE 237
Cdd:cd12180 179 AADLAELFARSDHLVLAAPLTPE----TRHLINADVLAQAKPGLHLINIARGGLVDQEALLEALDSGRISLASLDVTDPE 254

                .
gi 15832458 238 P 238
Cdd:cd12180 255 P 255
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
32-261 2.66e-12

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 67.25  E-value: 2.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   32 VAQLADADALMVRSVTKVNESL---LAGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAE 108
Cdd:PRK12480  40 VDQLKDYDGVTTMQFGKLENDVypkLESYGIKQIAQRTAGFDMYDLDLAKKHNIVISNVPSYSPETIAEYSVSIALQLVR 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  109 RdgFSLHERtvgivgvgnvgrRLQA-------------------------RLEAL--------GIKTLLCDPPRADCGDE 155
Cdd:PRK12480 120 R--FPDIER------------RVQAhdftwqaeimskpvknmtvaiigtgRIGAAtakiyagfGATITAYDAYPNKDLDF 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  156 GDFR-SLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVW 234
Cdd:PRK12480 186 LTYKdSVKEAIKDADIISLHVPANKE----SYHLFDKAMFDHVKKGAILVNAARGAVINTPDLIAAVNDGTLLGAAIDTY 261
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 15832458  235 EGEP--------------ELNVELLTKVDIG-TPHIAGYTLE 261
Cdd:PRK12480 262 ENEAayftndwtnkdiddKTLLELIEHERILvTPHIAFFSDE 303
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
21-259 3.50e-12

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240643 [Multi-domain]  Cd Length: 300  Bit Score: 66.46  E-value: 3.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  21 EVIAVPGRPIPVAQLADADALMVR--SVTKVNESLLAGKPIKFVGTATAGTDHVDEaWLKqAGIGFSAAPGCNAIAVVEY 98
Cdd:cd12166  21 EVVVWDGEGPPPDAAADVEFVVPPymAAPPVLEALRALPRLRVVQTLSAGYDGVLP-LLP-EGVTLCNARGVHDASTAEL 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  99 VFSslLMLAERDGF------------------SLHERTVGIVGVGNVGRRLQARLEALGIK-TLLCDPPRADCGDEGdFR 159
Cdd:cd12166  99 AVA--LILASLRGLprfvraqargrweprrtpSLADRRVLIVGYGSIGRAIERRLAPFEVRvTRVARTARPGEQVHG-ID 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 160 SLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQkLSVVLDVWEGEPe 239
Cdd:cd12166 176 ELPALLPEADVVVLIVPLTDE----TRGLVDAEFLARMPDGALLVNVARGPVVDTDALVAELASGR-LRAALDVTDPEP- 249
                       250       260
                ....*....|....*....|....
gi 15832458 240 LNVE----LLTKVDIgTPHIAGYT 259
Cdd:cd12166 250 LPPGhplwSAPGVLI-TPHVGGAT 272
PLN03139 PLN03139
formate dehydrogenase; Provisional
51-276 5.91e-12

formate dehydrogenase; Provisional


Pssm-ID: 178684  Cd Length: 386  Bit Score: 66.41  E-value: 5.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   51 ESLLAGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLML---------------------AER 109
Cdd:PLN03139 114 ERIKKAKNLELLLTAGIGSDHIDLPAAAAAGLTVAEVTGSNVVSVAEDELMRILILlrnflpgyhqvvsgewnvagiAYR 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  110 dGFSLHERTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRAD--------CGDEGDfrsLDELVQRADILTFHTPLFKdg 181
Cdd:PLN03139 194 -AYDLEGKTVGTVGAGRIGRLLLQRLKPFNCNLLYHDRLKMDpeleketgAKFEED---LDAMLPKCDVVVINTPLTE-- 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  182 pyKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPE---------LNVELltkvdigT 252
Cdd:PLN03139 268 --KTRGMFNKERIAKMKKGVLIVNNARGAIMDTQAVADACSSGHIGGYGGDVWYPQPApkdhpwrymPNHAM-------T 338
                        250       260
                 ....*....|....*....|....*..
gi 15832458  253 PHIAGYTLEGKAR---GTTQVFEAYSK 276
Cdd:PLN03139 339 PHISGTTIDAQLRyaaGVKDMLDRYFK 365
PRK06436 PRK06436
2-hydroxyacid dehydrogenase;
8-257 1.16e-11

2-hydroxyacid dehydrogenase;


Pssm-ID: 235800 [Multi-domain]  Cd Length: 303  Bit Score: 64.90  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458    8 NMPyARDLFSRLGEVI----AVPGRPipvaQLADADALMVRSvtkvneSLLAGKPIKFVGTATAGTDHVDEAWLKQAGIG 83
Cdd:PRK06436   6 NFP-MSKKLLEICRDIldldDVHWYP----DYYDAEAILIKG------RYVPGKKTKMIQSLSAGVDHIDVSGIPENVVL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   84 FSAApGCNAIAVVEYVFSSLLMLAER----------------DGFSLHERTVGIVGVGNVGRRLQARLEALGIKTLLCDP 147
Cdd:PRK06436  75 CSNA-GAYSISVAEHAFALLLAWAKNicennynmkngnfkqsPTKLLYNKSLGILGYGGIGRRVALLAKAFGMNIYAYTR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  148 PRADCGDEGDFRSLDELVQRADILTFHTPLFKdgpyKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKL 227
Cdd:PRK06436 154 SYVNDGISSIYMEPEDIMKKSDFVLISLPLTD----ETRGMINSKMLSLFRKGLAIINVARADVVDKNDMLNFLRNHNDK 229
                        250       260       270
                 ....*....|....*....|....*....|
gi 15832458  228 SVVLDVWEGEPELNvELLTKVDIGTPHIAG 257
Cdd:PRK06436 230 YYLSDVWWNEPIIT-ETNPDNVILSPHVAG 258
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
153-260 1.34e-10

Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy dehydrogenase family; This group contains a variety of proteins variously identified as glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase) and other enzymes of the 2-hydroxyacid dehydrogenase family. GDH catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. 2-hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240641 [Multi-domain]  Cd Length: 306  Bit Score: 61.74  E-value: 1.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 153 GDEGdfrsLDELVQRADILTF---HTPlfkdgpyKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQkLS- 228
Cdd:cd12164 176 GEEG----LDAFLAQTDILVCllpLTP-------ETRGILNAELLARLPRGAALINVGRGPHLVEADLLAALDSGH-LSg 243
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15832458 229 VVLDVWEGEPelnveLLT--------KVDIgTPHIAGYTL 260
Cdd:cd12164 244 AVLDVFEQEP-----LPAdhplwrhpRVTV-TPHIAAITD 277
PLN02306 PLN02306
hydroxypyruvate reductase
160-264 1.47e-10

hydroxypyruvate reductase


Pssm-ID: 177941  Cd Length: 386  Bit Score: 62.18  E-value: 1.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  160 SLDELVQRADILTFHTPLFKdgpyKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPE 239
Cdd:PLN02306 229 SMEEVLREADVISLHPVLDK----TTYHLINKERLALMKKEAVLVNASRGPVIDEVALVEHLKANPMFRVGLDVFEDEPY 304
                         90       100
                 ....*....|....*....|....*....
gi 15832458  240 LNVELL-TKVDIGTPHIAG---YTLEGKA 264
Cdd:PLN02306 305 MKPGLAdMKNAVVVPHIASaskWTREGMA 333
PRK15409 PRK15409
glyoxylate/hydroxypyruvate reductase GhrB;
14-261 1.76e-10

glyoxylate/hydroxypyruvate reductase GhrB;


Pssm-ID: 185307  Cd Length: 323  Bit Score: 61.69  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   14 DLFSRLGE---VIAVPG-RPIPVAQLADADAL---MVRSVTKVNESLLAGKP-IKFVGTATAGTDHVDEAWLKQAGIGFS 85
Cdd:PRK15409  14 DLLQRLEEhftVTQVANlSPETVEQHAAAFAEaegLLGSGEKVDAALLEKMPkLRAASTISVGYDNFDVDALTARKILLM 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458   86 AAPGCNAIAVVEYVFSSLLMLAERD---------------------GFSLHERTvgivgvgnvgrrlqarleaLGIKTL- 143
Cdd:PRK15409  94 HTPTVLTETVADTLMALVLSTARRVvevaervkagewtasigpdwfGTDVHHKT-------------------LGIVGMg 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  144 ---LCDPPRADCG-------------DEGDFR------SLDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGA 201
Cdd:PRK15409 155 rigMALAQRAHFGfnmpilynarrhhKEAEERfnarycDLDTLLQESDFVCIILPLTDE----THHLFGAEQFAKMKSSA 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15832458  202 ILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPeLNVE--LLTKVD-IGTPHIAGYTLE 261
Cdd:PRK15409 231 IFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQEP-LSVDspLLSLPNvVAVPHIGSATHE 292
2-Hacid_dh_2 cd12159
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
30-256 9.99e-10

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240636  Cd Length: 303  Bit Score: 59.20  E-value: 9.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  30 IPVAQLADADALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEA-WLKQAGIGFSAAPGCNAIAVVEYVFSSLL---- 104
Cdd:cd12159  21 ERVELDEDADALVWTGSAREPERLPASPGVRWVQLPFAGVEAFVEAgVITDPGRRWTNAAGAYAETVAEHALALLLaglr 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 105 MLAERDGFSLHERTVGIVGVGNVG-------------RRLQARLEALGIKTLLCD--PPRADCGDEG-DFRSLDELVQRA 168
Cdd:cd12159 101 QLPARARATTWDPAEEDDLVTLLRgstvaivgaggigRALIPLLAPFGAKVIAVNrsGRPVEGADETvPADRLDEVWPDA 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 169 DILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEP---------E 239
Cdd:cd12159 181 DHVVLAAPLTPE----TRHLVDAAALAAMKPHAWLVNVARGPLVDTDALVDALRSGEIAGAALDVTDPEPlpdghplwsL 256
                       250
                ....*....|....*..
gi 15832458 240 LNVelltkvdIGTPHIA 256
Cdd:cd12159 257 PNA-------LITPHVA 266
PLN02928 PLN02928
oxidoreductase family protein
129-259 2.30e-08

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 55.07  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  129 RRLQARLEALGIKTL-------------LCDPPRADCG---DEGDFRSLDELVQRADILTFHTPLFKDgpykTLHLADEK 192
Cdd:PLN02928 172 IELAKRLRPFGVKLLatrrswtsepedgLLIPNGDVDDlvdEKGGHEDIYEFAGEADIVVLCCTLTKE----TAGIVNDE 247
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15832458  193 LIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPELNVELLTKVD--IGTPHIAGYT 259
Cdd:PLN02928 248 FLSSMKKGALLVNIARGGLLDYDAVLAALESGHLGGLAIDVAWSEPFDPDDPILKHPnvIITPHVAGVT 316
2-Hacid_dh_3 cd12160
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
161-257 1.18e-07

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240637  Cd Length: 310  Bit Score: 52.76  E-value: 1.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 161 LDELVQRADILTFHTPLFKDgpykTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPEL 240
Cdd:cd12160 190 LPELLPETDVLVMILPATPS----TAHALDAEVLAALPKHAWVVNVGRGATVDEDALVAALESGRLGGAALDVTATEPLP 265
                        90
                ....*....|....*....
gi 15832458 241 NVELLTKVD--IGTPHIAG 257
Cdd:cd12160 266 ASSPLWDAPnlILTPHAAG 284
2-Hacid_dh_5 cd12163
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
59-259 3.38e-04

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240640  Cd Length: 334  Bit Score: 42.26  E-value: 3.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458  59 IKFVGTATAGTDH-VDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAER--------------------DGFSLHER 117
Cdd:cd12163  55 LRLVQLFSAGADHwLGHPLYKDPEVPLCTASGIHGPQIAEWVIGTWLVLSHHflqyielqkeqtwgrrqeaySVEDSVGK 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 118 TVGIVGVGNVGRRLqARL-EALGIK----TLLCDPPRADCGDEG---------------------DFRSLDE-LVQRADI 170
Cdd:cd12163 135 RVGILGYGSIGRQT-ARLaQALGMEvyayTRSPRPTPESRKDDGyivpgtgdpdgsipsawfsgtDKASLHEfLRQDLDL 213
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832458 171 LTFHTPLfkdgPYKTLHLADEKLIRSL-KPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPeL--NVELLT- 246
Cdd:cd12163 214 LVVSLPL----TPATKHLLGAEEFEILaKRKTFVSNIARGSLVDTDALVAALESGQIRGAALDVTDPEP-LpaDHPLWSa 288
                       250
                ....*....|....
gi 15832458 247 -KVDIgTPHIAGYT 259
Cdd:cd12163 289 pNVII-TPHVSWQT 301
 
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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