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Conserved domains on  [gi|149818447|gb|EDM77896|]
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erythronate-4-phosphate dehydrogenase [Plesiocystis pacifica SIR-1]

Protein Classification

Rossmann-fold NAD(P)-binding domain-containing protein( domain architecture ID 229380)

Rossmann-fold NAD(P)-binding domain-containing protein may function as an oxidoreductase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
5-355 2.44e-101

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd12158:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 343  Bit Score: 304.07  E-value: 2.44e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447   5 PIVVDDAVPLAGEVFTKLGEVHALPSGAIDAATLAriGARALVVRSVTTVDAALLDACPeLEFVGTATAGLDHLDLEALA 84
Cdd:cd12158    1 KILADENIPYAEELFSPLGEVTYLPGREITAEDLK--DADVLLVRSVTKVNEALLEGSK-VKFVGTATIGTDHIDTDYLK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  85 AREVAVADAAGCNSLAVAQWVAAALLTTRPRWPEALREA----------GdaptvgvvghghvgSKVARTLRALGFPVLV 154
Cdd:cd12158   78 ERGIGFANAPGCNANSVAEYVLSALLVLAQRQGFSLKGKtvgivgvgnvG--------------SRLARRLEALGMNVLL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 155 SDPF-APPSDPAVAVDFETLWRRSAIVSFHVPLTRGGLHPTAAMLapvgeGGPPLAGPK---LVVNTSRGPVVRDAALDR 230
Cdd:cd12158  144 CDPPrAEAEGDPGFVSLEELLAEADIITLHVPLTRDGEHPTYHLL-----DEDFLAALKpgqILINASRGAVIDNQALLA 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 231 P----DVRAAILDVWEGEPEPAAARLrdPKVLLASPHVAGYSLDAKIDASLAVARQLAARWGAErgAFERGRWLGPAGVV 306
Cdd:cd12158  219 LlqrgKDLRVVLDVWENEPEIDLELL--DKVDIATPHIAGYSLEGKARGTEMIYEALCQFLGLK--ARKSLSDLLPAPAL 294
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 149818447 307 EGGT---------SAEILRAVVALEADDRSVRALAELetggagasprARAFEALRRGY 355
Cdd:cd12158  295 PSITldgsldealLARLVRAVYDIRRDDARLRKTLAL----------PAGFDALRKNY 342
 
Name Accession Description Interval E-value
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
5-355 2.44e-101

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: 304.07  E-value: 2.44e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447   5 PIVVDDAVPLAGEVFTKLGEVHALPSGAIDAATLAriGARALVVRSVTTVDAALLDACPeLEFVGTATAGLDHLDLEALA 84
Cdd:cd12158    1 KILADENIPYAEELFSPLGEVTYLPGREITAEDLK--DADVLLVRSVTKVNEALLEGSK-VKFVGTATIGTDHIDTDYLK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  85 AREVAVADAAGCNSLAVAQWVAAALLTTRPRWPEALREA----------GdaptvgvvghghvgSKVARTLRALGFPVLV 154
Cdd:cd12158   78 ERGIGFANAPGCNANSVAEYVLSALLVLAQRQGFSLKGKtvgivgvgnvG--------------SRLARRLEALGMNVLL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 155 SDPF-APPSDPAVAVDFETLWRRSAIVSFHVPLTRGGLHPTAAMLapvgeGGPPLAGPK---LVVNTSRGPVVRDAALDR 230
Cdd:cd12158  144 CDPPrAEAEGDPGFVSLEELLAEADIITLHVPLTRDGEHPTYHLL-----DEDFLAALKpgqILINASRGAVIDNQALLA 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 231 P----DVRAAILDVWEGEPEPAAARLrdPKVLLASPHVAGYSLDAKIDASLAVARQLAARWGAErgAFERGRWLGPAGVV 306
Cdd:cd12158  219 LlqrgKDLRVVLDVWENEPEIDLELL--DKVDIATPHIAGYSLEGKARGTEMIYEALCQFLGLK--ARKSLSDLLPAPAL 294
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 149818447 307 EGGT---------SAEILRAVVALEADDRSVRALAELetggagasprARAFEALRRGY 355
Cdd:cd12158  295 PSITldgsldealLARLVRAVYDIRRDDARLRKTLAL----------PAGFDALRKNY 342
PRK00257 PRK00257
4-phosphoerythronate dehydrogenase PdxB;
6-368 2.81e-58

4-phosphoerythronate dehydrogenase PdxB;


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 194.48  E-value: 2.81e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447   6 IVVDDAVPLAGEVFTKLGEVHALPSGAIDAATLAriGARALVVRSVTTVDAALLDACPeLEFVGTATAGLDHLDLEALAA 85
Cdd:PRK00257   3 IVADENIPLLDAFFAGFGEIRRLPGRAFDRAAVR--DADVLLVRSVTRVDRALLEGSR-VRFVGTCTIGTDHLDLDYFAE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  86 REVAVADAAGCNSLAVAQWVAAALLTTRPRWPEALREAgdapTVGVVGHGHVGSKVARTLRALGFPVLVSDPfaPPSDPA 165
Cdd:PRK00257  80 AGITWSSAPGCNARGVVDYVLGSLLTLAEREGVDLAER----TYGVVGAGHVGGRLVRVLRGLGWKVLVCDP--PRQEAE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 166 VAVDF---ETLWRRSAIVSFHVPLTRGGLHPTAAMLapvgeGGPPLAGPK---LVVNTSRGPVV-----RDAALDRPDVR 234
Cdd:PRK00257 154 GDGDFvslERILEECDVISLHTPLTKEGEHPTRHLL-----DEAFLASLRpgaWLINASRGAVVdnqalREALLSGEDLD 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 235 aAILDVWEGEPEPAAARLRdpKVLLASPHVAGYSLDAKIDASlAVARQLAARWGAERGAFERGRWLGPAGVVEGGTSAE- 313
Cdd:PRK00257 229 -AVLDVWEGEPQIDLELAD--LCTIATPHIAGYSLDGKARGT-AQIYQALCRFFGIPARVSLTDLLPPPWLAQIDLDASa 304
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149818447 314 --------ILRAVVALEADDRSVRALAELETGGagaspRARAFEALRRGYALRREFGAWEAVG 368
Cdd:PRK00257 305 dpawalatLCRAVYDPRRDDAAFRRSLTGDVAQ-----QRAAFDALRKHYPLRREIEGLRVRL 362
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
6-285 7.86e-46

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: 159.97  E-value: 7.86e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447   6 IVVDDAVPLAG-EVFTKLGEVHALPSGAIDAATLARI--GARALVVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEA 82
Cdd:COG0111    3 ILILDDLPPEAlEALEAAPGIEVVYAPGLDEEELAEAlaDADALIVRSRTKVTAELLAAAPNLKLIGRAGAGVDNIDLAA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  83 LAAREVAVADAAGCNSLAVAQWVAAALLT-TR--PRWPEALREAGDAPTVGVVGHGHVG-----------SKVARTLRAL 148
Cdd:COG0111   83 ATERGIPVTNAPGANARAVAEYALALLLAlARrlPEADRAQRAGRWDRSAFRGRELRGKtvgivglgrigRAVARRLRAF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 149 GFPVLVSDPFAPPSDPA-----VAVDFETLWRRSAIVSFHVPL---TRGGLhpTAAMLAPVGEGGpplagpkLVVNTSRG 220
Cdd:COG0111  163 GMRVLAYDPSPKPEEAAdlgvgLVDSLDELLAEADVVSLHLPLtpeTRGLI--GAEELAAMKPGA-------ILINTARG 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149818447 221 PVVRD----AALDRPDVRAAILDVWEGEPEPAAARLRDPKVLLASPHVAGYSLDAKIDASLAVARQLAA 285
Cdd:COG0111  234 GVVDEdallAALDSGRLAGAALDVFEPEPLPADSPLWDLPNVILTPHIAGSTEEAQERAARQVAENIRR 302
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
32-285 2.17e-22

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: 96.59  E-value: 2.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447   32 AIDAATLARI--GARALVVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQWVAAAL 109
Cdd:pfam00389  25 ELLTEELLEKakDADALIVRSRTKVTAEVLEAAPKLKVIGRAGVGVDNVDLDAATERGILVTNAPGYNTESVAELTIGLI 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  110 LTTRPRWPEALRE--AGDAPTVGVVGHGHVGSK------------VARTLRALGFPVLVSDPFAPPSDPA---VAVDFET 172
Cdd:pfam00389 105 LALARRIPEADASvrEGKWKKSGLIGLELYGKTlgviggggigggVAAIAKAFGMGVVAYDPYPNPERAEaggVEVLSLL 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  173 LWRRSAIVSFHVPLTRGGLHPTAAMLAPVGEGGPPLAGpKLVVNTSRGPVVRDAALD---RPDVRAAILDVWEGEPEPAA 249
Cdd:pfam00389 185 LLLLDLPESDDVLTVNPLTTMKTGVIIINEARGMLKDA-VAIINAAGGGVIDEAALDallEEGIAAAADLDVEEEPPPVD 263
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 149818447  250 ARLRDPKVLLASPHVAGYSLDAKIDASLAVARQLAA 285
Cdd:pfam00389 264 SPLLDLPNVILTPHIGGATEEAQERIAEEAAENILA 299
 
Name Accession Description Interval E-value
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
5-355 2.44e-101

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: 304.07  E-value: 2.44e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447   5 PIVVDDAVPLAGEVFTKLGEVHALPSGAIDAATLAriGARALVVRSVTTVDAALLDACPeLEFVGTATAGLDHLDLEALA 84
Cdd:cd12158    1 KILADENIPYAEELFSPLGEVTYLPGREITAEDLK--DADVLLVRSVTKVNEALLEGSK-VKFVGTATIGTDHIDTDYLK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  85 AREVAVADAAGCNSLAVAQWVAAALLTTRPRWPEALREA----------GdaptvgvvghghvgSKVARTLRALGFPVLV 154
Cdd:cd12158   78 ERGIGFANAPGCNANSVAEYVLSALLVLAQRQGFSLKGKtvgivgvgnvG--------------SRLARRLEALGMNVLL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 155 SDPF-APPSDPAVAVDFETLWRRSAIVSFHVPLTRGGLHPTAAMLapvgeGGPPLAGPK---LVVNTSRGPVVRDAALDR 230
Cdd:cd12158  144 CDPPrAEAEGDPGFVSLEELLAEADIITLHVPLTRDGEHPTYHLL-----DEDFLAALKpgqILINASRGAVIDNQALLA 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 231 P----DVRAAILDVWEGEPEPAAARLrdPKVLLASPHVAGYSLDAKIDASLAVARQLAARWGAErgAFERGRWLGPAGVV 306
Cdd:cd12158  219 LlqrgKDLRVVLDVWENEPEIDLELL--DKVDIATPHIAGYSLEGKARGTEMIYEALCQFLGLK--ARKSLSDLLPAPAL 294
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 149818447 307 EGGT---------SAEILRAVVALEADDRSVRALAELetggagasprARAFEALRRGY 355
Cdd:cd12158  295 PSITldgsldealLARLVRAVYDIRRDDARLRKTLAL----------PAGFDALRKNY 342
PRK00257 PRK00257
4-phosphoerythronate dehydrogenase PdxB;
6-368 2.81e-58

4-phosphoerythronate dehydrogenase PdxB;


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 194.48  E-value: 2.81e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447   6 IVVDDAVPLAGEVFTKLGEVHALPSGAIDAATLAriGARALVVRSVTTVDAALLDACPeLEFVGTATAGLDHLDLEALAA 85
Cdd:PRK00257   3 IVADENIPLLDAFFAGFGEIRRLPGRAFDRAAVR--DADVLLVRSVTRVDRALLEGSR-VRFVGTCTIGTDHLDLDYFAE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  86 REVAVADAAGCNSLAVAQWVAAALLTTRPRWPEALREAgdapTVGVVGHGHVGSKVARTLRALGFPVLVSDPfaPPSDPA 165
Cdd:PRK00257  80 AGITWSSAPGCNARGVVDYVLGSLLTLAEREGVDLAER----TYGVVGAGHVGGRLVRVLRGLGWKVLVCDP--PRQEAE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 166 VAVDF---ETLWRRSAIVSFHVPLTRGGLHPTAAMLapvgeGGPPLAGPK---LVVNTSRGPVV-----RDAALDRPDVR 234
Cdd:PRK00257 154 GDGDFvslERILEECDVISLHTPLTKEGEHPTRHLL-----DEAFLASLRpgaWLINASRGAVVdnqalREALLSGEDLD 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 235 aAILDVWEGEPEPAAARLRdpKVLLASPHVAGYSLDAKIDASlAVARQLAARWGAERGAFERGRWLGPAGVVEGGTSAE- 313
Cdd:PRK00257 229 -AVLDVWEGEPQIDLELAD--LCTIATPHIAGYSLDGKARGT-AQIYQALCRFFGIPARVSLTDLLPPPWLAQIDLDASa 304
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149818447 314 --------ILRAVVALEADDRSVRALAELETGGagaspRARAFEALRRGYALRREFGAWEAVG 368
Cdd:PRK00257 305 dpawalatLCRAVYDPRRDDAAFRRSLTGDVAQ-----QRAAFDALRKHYPLRREIEGLRVRL 362
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
6-285 7.86e-46

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: 159.97  E-value: 7.86e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447   6 IVVDDAVPLAG-EVFTKLGEVHALPSGAIDAATLARI--GARALVVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEA 82
Cdd:COG0111    3 ILILDDLPPEAlEALEAAPGIEVVYAPGLDEEELAEAlaDADALIVRSRTKVTAELLAAAPNLKLIGRAGAGVDNIDLAA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  83 LAAREVAVADAAGCNSLAVAQWVAAALLT-TR--PRWPEALREAGDAPTVGVVGHGHVG-----------SKVARTLRAL 148
Cdd:COG0111   83 ATERGIPVTNAPGANARAVAEYALALLLAlARrlPEADRAQRAGRWDRSAFRGRELRGKtvgivglgrigRAVARRLRAF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 149 GFPVLVSDPFAPPSDPA-----VAVDFETLWRRSAIVSFHVPL---TRGGLhpTAAMLAPVGEGGpplagpkLVVNTSRG 220
Cdd:COG0111  163 GMRVLAYDPSPKPEEAAdlgvgLVDSLDELLAEADVVSLHLPLtpeTRGLI--GAEELAAMKPGA-------ILINTARG 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149818447 221 PVVRD----AALDRPDVRAAILDVWEGEPEPAAARLRDPKVLLASPHVAGYSLDAKIDASLAVARQLAA 285
Cdd:COG0111  234 GVVDEdallAALDSGRLAGAALDVFEPEPLPADSPLWDLPNVILTPHIAGSTEEAQERAARQVAENIRR 302
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
42-285 2.26e-42

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: 150.47  E-value: 2.26e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  42 GARALVVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQWVAAALLTTRPRWPEALR 121
Cdd:cd05198   41 DADALIVSSTTPVTAEVLAKAPKLKFIQVAGAGVDNIDLDAAKKRGITVTNVPGANAEAVAEHALGLLLALLRRLPRADA 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 122 EAGDAPTVGVVGHGHVG---------------SKVARTLRALGFPVLVSDPFAPPSDP----AVAVDFETLWRRSAIVSF 182
Cdd:cd05198  121 AVRRGWGWLWAGFPGYElegktvgivglgrigQRVAKRLQAFGMKVLYYDRTRKPEPEedlgFRVVSLDELLAQSDVVVL 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 183 HVPLTRGGLHP-TAAMLAPVGEGgpplagpKLVVNTSRGPVV-RDA---ALDRPDVRAAILDVWEGEPEPAAARLRDPKV 257
Cdd:cd05198  201 HLPLTPETRHLiNEEELALMKPG-------AVLVNTARGGLVdEDAllrALKSGKIAGAALDVFEPEPLPADHPLLELPN 273
                        250       260
                 ....*....|....*....|....*...
gi 149818447 258 LLASPHVAGYSLDAKIDASLAVARQLAA 285
Cdd:cd05198  274 VILTPHIAGYTEEARERMAEIAVENLER 301
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
6-378 3.47e-39

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 143.89  E-value: 3.47e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447   6 IVVDDAVPLAGEVFTKLGEVHALPSGAIDAATLARigARALVVRSVTTVDAALLDACPeLEFVGTATAGLDHLDLEALAA 85
Cdd:PRK15438   3 ILVDENMPYARELFSRLGEVKAVPGRPIPVAQLAD--ADALMVRSVTKVNESLLAGKP-IKFVGTATAGTDHVDEAWLKQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  86 REVAVADAAGCNSLAVAQWVAAALLTTRPRWPEALREAgdapTVGVVGHGHVGSKVARTLRALGFPVLVSDPfaPPSDPA 165
Cdd:PRK15438  80 AGIGFSAAPGCNAIAVVEYVFSSLLMLAERDGFSLHDR----TVGIVGVGNVGRRLQARLEALGIKTLLCDP--PRADRG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 166 VAVDFET---LWRRSAIVSFHVPLTRGGLHPT-----AAMLAPVGEGGpplagpkLVVNTSRGPVVRDAA----LDRPDV 233
Cdd:PRK15438 154 DEGDFRSldeLVQEADILTFHTPLFKDGPYKTlhladEKLIRSLKPGA-------ILINACRGAVVDNTAlltcLNEGQK 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 234 RAAILDVWEGEPEPAAARLRdpKVLLASPHVAGYSLDAKIDASLAVARQLAARWGAERG--------AFERGRwLGPAGV 305
Cdd:PRK15438 227 LSVVLDVWEGEPELNVELLK--KVDIGTPHIAGYTLEGKARGTTQVFEAYSKFIGHEQHvaldtllpAPEFGR-ITLHGP 303
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149818447 306 VEGGTSAEILRAVVALEADDRSVRALAeletGGAGasprarAFEALRRGYALRREFGAWEAVGGDSR----LDTLGF 378
Cdd:PRK15438 304 LDQPTLKRLVHLVYDVRRDDAPLRKVA----GIPG------EFDKLRKNYLERREWSSLYVICDDASaaslLCKLGF 370
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
5-285 1.92e-37

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: 137.53  E-value: 1.92e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447   5 PIVVDDAVPLAGEVFTKLG----EVHALPSGAIDAATLARI-GARALVVRSVTTVDAALLDACPELEFVGTATAGLDHLD 79
Cdd:COG1052    2 PILVLDPRTLPDEVLERLEaehfEVTVYEDETSPEELAERAaGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNID 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  80 LEALAAREVAVADAAGCNSLAVAQWVAAALLTTRPRWPEALRE--AGDAPTVGVVGHGHVGSK-------------VART 144
Cdd:COG1052   82 LAAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRvrAGDWSWSPGLLGRDLSGKtlgiiglgrigqaVARR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 145 LRALGFPVLVSDPFAPPSDPAV---AVDFETLWRRSAIVSFHVPLTRGGLHP-TAAMLAPVGEGGpplagpkLVVNTSRG 220
Cdd:COG1052  162 AKGFGMKVLYYDRSPKPEVAELgaeYVSLDELLAESDIVSLHCPLTPETRHLiNAEELALMKPGA-------ILINTARG 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 221 PVVRDA----ALDRPDVRAAILDVWEGEPEPAAARLRD-PKVLLaSPHVAGYSLDAKIDASLAVARQLAA 285
Cdd:COG1052  235 GLVDEAalieALKSGRIAGAGLDVFEEEPPPPDHPLLSlPNVVL-TPHIASATEEAREAMAELALDNLLA 303
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
33-285 1.89e-34

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: 129.46  E-value: 1.89e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  33 IDAATLARI--GARALVVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQWVAAALL 110
Cdd:cd12173   29 LSEEELLAIiaDADALIVRSATKVTAEVIEAAPRLKVIGRAGVGVDNIDVEAATARGILVVNAPGANTISVAEHTIALML 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 111 TTRPRWPEALRE--AGDAPTVGVVGHGHVG------------SKVARTLRALGFPVLVSDPFAPPSDPAV----AVDFET 172
Cdd:cd12173  109 ALARNIPQADASlrAGKWDRKKFMGVELRGktlgivglgrigREVARRARAFGMKVLAYDPYISAERAAAggveLVSLDE 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 173 LWRRSAIVSFHVPLTRGglhpTAAMLapvgeGGPPLAGPK---LVVNTSRGPVVRDA----ALDRPDVRAAILDVWEGEP 245
Cdd:cd12173  189 LLAEADFISLHTPLTPE----TRGLI-----NAEELAKMKpgaILINTARGGIVDEAaladALKSGKIAGAALDVFEQEP 259
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 149818447 246 EPAAARLRD-PKVLLaSPHVAGYSLDAKIDASLAVARQLAA 285
Cdd:cd12173  260 PPADSPLLGlPNVIL-TPHLGASTEEAQERVAVDAAEQVLA 299
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
45-287 5.80e-30

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: 117.25  E-value: 5.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  45 ALVVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQWVAAALLTTRPRWPEALRE-- 122
Cdd:cd05303   44 VLIVRSRTKVTKEVIDAAKNLKIIARAGVGLDNIDVEYAKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHRANREmk 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 123 AGDAPTVGVVGHGHV------------GSKVARTLRALGFPVLVSDPFAPPS----DPAVAVDFETLWRRSAIVSFHVPL 186
Cdd:cd05303  124 LGKWNKKKYKGIELRgktlgiigfgriGREVAKIARALGMNVIAYDPYPKDEqaveLGVKTVSLEELLKNSDFISLHVPL 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 187 TRgglhPTAAMLapvgeGGPPLAGPK---LVVNTSRGPVVRDAAL----DRPDVRAAILDVWEGEPEPAAARLRDPKVLL 259
Cdd:cd05303  204 TP----ETKHMI-----NKKELELMKdgaIIINTSRGGVIDEEALlealKSGKLAGAALDVFENEPPPGSKLLELPNVSL 274
                        250       260
                 ....*....|....*....|....*...
gi 149818447 260 aSPHVAGYSLDAKIDASLAVARQLAARW 287
Cdd:cd05303  275 -TPHIGASTKEAQERIGEELANKIIEFL 301
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
24-271 9.70e-26

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: 105.73  E-value: 9.70e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  24 EVHALPSGAIDAATLAriGARALVVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQ 103
Cdd:cd12175   27 EVVTAAELDEEAALLA--DADVLVPGMRKVIDAELLAAAPRLRLIQQPGVGLDGVDLEAATARGIPVANIPGGNAESVAE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 104 WVAAALLTTRPRWPEALRE--AGDAPTVGVVGHGHVGSK-------------VARTLRALGFPVLVSDPFAPPSD----- 163
Cdd:cd12175  105 HAVMLMLALLRRLPEADRElrAGRWGRPEGRPSRELSGKtvgivglgnigraVARRLRGFGVEVIYYDRFRDPEAeekdl 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 164 PAVAVDFETLWRRSAIVSFHVPLTRGGLHP-TAAMLAPVGEGGpplagpkLVVNTSRGPVVRDAALDRP----DVRAAIL 238
Cdd:cd12175  185 GVRYVELDELLAESDVVSLHVPLTPETRHLiGAEELAAMKPGA-------ILINTARGGLVDEEALLAAlrsgHLAGAGL 257
                        250       260       270
                 ....*....|....*....|....*....|...
gi 149818447 239 DVWEGEPEPAAARLRDPKVLLASPHVAGYSLDA 271
Cdd:cd12175  258 DVFWQEPLPPDDPLLRLDNVILTPHIAGVTDES 290
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
32-285 2.17e-22

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: 96.59  E-value: 2.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447   32 AIDAATLARI--GARALVVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQWVAAAL 109
Cdd:pfam00389  25 ELLTEELLEKakDADALIVRSRTKVTAEVLEAAPKLKVIGRAGVGVDNVDLDAATERGILVTNAPGYNTESVAELTIGLI 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  110 LTTRPRWPEALRE--AGDAPTVGVVGHGHVGSK------------VARTLRALGFPVLVSDPFAPPSDPA---VAVDFET 172
Cdd:pfam00389 105 LALARRIPEADASvrEGKWKKSGLIGLELYGKTlgviggggigggVAAIAKAFGMGVVAYDPYPNPERAEaggVEVLSLL 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  173 LWRRSAIVSFHVPLTRGGLHPTAAMLAPVGEGGPPLAGpKLVVNTSRGPVVRDAALD---RPDVRAAILDVWEGEPEPAA 249
Cdd:pfam00389 185 LLLLDLPESDDVLTVNPLTTMKTGVIIINEARGMLKDA-VAIINAAGGGVIDEAALDallEEGIAAAADLDVEEEPPPVD 263
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 149818447  250 ARLRDPKVLLASPHVAGYSLDAKIDASLAVARQLAA 285
Cdd:pfam00389 264 SPLLDLPNVILTPHIGGATEEAQERIAEEAAENILA 299
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
16-285 1.23e-21

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: 94.14  E-value: 1.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  16 GEVFTKLGEVHALPSGAIDAATLariGARALVVrSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAG 95
Cdd:cd12171   23 ILVVEKSGPEAVEPEEELLEALK---DADILIT-HFAPVTKKVIEAAPKLKLIGVCRGGPENVDVEAATERGIPVLNTPG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  96 CNSLAVAQWVAAALLT-TR--PRWPEALRE---AGDAPTVGVVG------------HGHVGSKVARTLRALGFPVLVSDP 157
Cdd:cd12171   99 RNAEAVAEFTVGLMLAeTRniARAHAALKDgewRKDYYNYDGYGpelrgktvgivgFGAIGRRVAKRLKAFGAEVLVYDP 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 158 FAPPSDPAV----AVDFETLWRRSAIVSFHVPL---TRG--GLHPTAAMlapvgeggPPLAgpkLVVNTSRGPVV-RDA- 226
Cdd:cd12171  179 YVDPEKIEAdgvkKVSLEELLKRSDVVSLHARLtpeTRGmiGAEEFALM--------KPTA---YFINTARAGLVdEDAl 247
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149818447 227 --ALDRPDVRAAILDVWEGEPEPAAARLRD-PKVLLaSPHVAGYSLDAKIDASLAVARQLAA 285
Cdd:cd12171  248 ieALEEGKIGGAALDVFPEEPLPADHPLLKlDNVTL-TPHIAGATRDVAERSPEIIAEELKR 308
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
15-280 1.60e-21

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: 93.71  E-value: 1.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  15 AGEVFTKLG-EVHALPSG-AIDAATLARI--GARALVVrSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAV 90
Cdd:cd12172   16 AKELLEAAGfEVVLNPLGrPLTEEELIELlkDADGVIA-GLDPITEEVLAAAPRLKVISRYGVGYDNIDLEAAKKRGIVV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  91 ADAAGCNSLAVAQWVAAALLTTRPRWPEALRE--AGDAPtvgVVGHGHVGSK-------------VARTLRALGFPVLVS 155
Cdd:cd12172   95 TNTPGANSNSVAELTIGLMLALARQIPQADREvrAGGWD---RPVGTELYGKtlgiiglgrigkaVARRLSGFGMKVLAY 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 156 DPFaPPSDPAVA-----VDFETLWRRSAIVSFHVPLTrgglHPTAAMLapvgeGGPPLAGPK---LVVNTSRGPVVRD-- 225
Cdd:cd12172  172 DPY-PDEEFAKEhgvefVSLEELLKESDFISLHLPLT----PETRHLI-----NAAELALMKpgaILINTARGGLVDEea 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 149818447 226 --AALDRPDVRAAILDVWEGEPEPAAARLRDPKVLLASPHVAGYSLDAKIDASLAVA 280
Cdd:cd12172  242 lyEALKSGRIAGAALDVFEEEPPPADSPLLELPNVILTPHIGASTKEAVLRMGTMAA 298
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
46-278 1.79e-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: 240656 [Multi-domain]  Cd Length: 306  Bit Score: 90.82  E-value: 1.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  46 LVVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQWVAAALLTTRPRWPEA------ 119
Cdd:cd12179   44 LIIRSRFPIDKEFIEKATNLKFIARAGAGLENIDLEYAKEKGIELFNAPEGNRDAVGEHALGMLLALFNKLNRAdqevrn 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 120 ---LREAG-----DAPTVGVVGHGHVGSKVARTLRALGFPVLVSDPFAPPSDP-AVAVDFETLWRRSAIVSFHVPL---T 187
Cdd:cd12179  124 giwDREGNrgvelMGKTVGIIGYGNMGKAFAKRLSGFGCKVIAYDKYKNFGDAyAEQVSLETLFKEADILSLHIPLtpeT 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 188 RGGLhpTAAMLAPVgeggpplAGPKLVVNTSRGPVVRDA----ALDRPDVRAAILDVWEGE--------PEPAAAR--LR 253
Cdd:cd12179  204 RGMV--NKEFISSF-------KKPFYFINTARGKVVVTKdlvkALKSGKILGACLDVLEYEkasfesifNQPEAFEylIK 274
                        250       260
                 ....*....|....*....|....*..
gi 149818447 254 DPKVLLaSPHVAGYSLDA--KIDASLA 278
Cdd:cd12179  275 SPKVIL-TPHIAGWTFESyeKIAEVLV 300
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
17-286 3.83e-20

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: 89.88  E-value: 3.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  17 EVFTKLG-EVHALPSGAIDAATLARIGARALVVRSvTTVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAG 95
Cdd:cd05299   18 EVLEEAGvELVDAQSRTEDELIEAAADADALLVQY-APVTAEVIEALPRLKVIVRYGVGVDNVDVAAATERGIPVCNVPD 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  96 CNSLAVAQWVAAALLT-TR--PRWPEALREAGDAPTVGVVG------------HGHVGSKVARTLRALGFPVLVSDPFAP 160
Cdd:cd05299   97 YCTEEVADHALALILAlARklPFLDRAVRAGGWDWTVGGPIrrlrgltlglvgFGRIGRAVAKRAKAFGFRVIAYDPYVP 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 161 PSDPAVA----VDFETLWRRSAIVSFHVPLTRGGLHP-TAAMLAPVGEGGpplagpkLVVNTSRGPVVRDA----ALDRP 231
Cdd:cd05299  177 DGVAALGgvrvVSLDELLARSDVVSLHCPLTPETRHLiDAEALALMKPGA-------FLVNTARGGLVDEAalarALKSG 249
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 149818447 232 DVRAAILDVWEGEPEPAAARLRD-PKVLLaSPHVAGYSldakiDASLAVARQLAAR 286
Cdd:cd05299  250 RIAGAALDVLEEEPPPADSPLLSaPNVIL-TPHAAWYS-----EESLAELRRKAAE 299
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
54-271 5.61e-18

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: 83.66  E-value: 5.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  54 VDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQWVAAALL--TTRPRWPEALREAG------- 124
Cdd:cd12162   55 LDAEVLAQLPNLKLIGVLATGYNNVDLAAAKERGITVTNVPGYSTDSVAQHTFALLLalARLVAYHNDVVKAGewqkspd 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 125 ----DAP-------TVGVVGHGHVGSKVARTLRALGFPVLVSDPFAPPSDPAVAVDFETLWRRSAIVSFHVPL---TRGG 190
Cdd:cd12162  135 fcfwDYPiielagkTLGIIGYGNIGQAVARIARAFGMKVLFAERKGAPPLREGYVSLDELLAQSDVISLHCPLtpeTRNL 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 191 L-HPTAAMLAPvgegGPplagpkLVVNTSRGPVVRDA----ALDRPDVRAAILDVWEGEPEPAAARLRD--PKVLLaSPH 263
Cdd:cd12162  215 InAEELAKMKP----GA------ILINTARGGLVDEQaladALNSGKIAGAGLDVLSQEPPRADNPLLKaaPNLII-TPH 283

                 ....*...
gi 149818447 264 VAGYSLDA 271
Cdd:cd12162  284 IAWASREA 291
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
53-266 1.46e-17

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: 82.99  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  53 TVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQW-VAAALLTTR--PRWPEALREAGDAPTV 129
Cdd:cd12167   61 PLDAELLARAPRLRAVVHAAGSVRGLVTDAVWERGILVTSAADANAEPVAEFtLAAILLALRriPRFAAAYRAGRDWGWP 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 130 GVVGHGHVGSK-------------VARTLRALGFPVLVSDPFAPPSDPA----VAVDFETLWRRSAIVSFHVPL---TRG 189
Cdd:cd12167  141 TRRGGRGLYGRtvgivgfgrigraVVELLRPFGLRVLVYDPYLPAAEAAalgvELVSLDELLARSDVVSLHAPLtpeTRG 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 190 GLhpTAAMLAPVGEGGpplagpkLVVNTSRGPVVRDAAL----DRPDVRAAiLDVWEGEPEPAAARLRD-PKVLLaSPHV 264
Cdd:cd12167  221 MI--DARLLALMRDGA-------TFINTARGALVDEAALlaelRSGRLRAA-LDVTDPEPLPPDSPLRTlPNVLL-TPHI 289

                 ..
gi 149818447 265 AG 266
Cdd:cd12167  290 AG 291
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
56-265 2.69e-17

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: 81.88  E-value: 2.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  56 AALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQWV---AAALLTTRPRWPEALREAGDA------ 126
Cdd:cd12161   61 GEVIEACKNLKMISVAFTGVDHVDLEACKERGITVSNAAGYSTEAVAELTiglAIDLLRNIVPCDAAVRAGGTKagligr 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 127 ----PTVGVVGHGHVGSKVARTLRALGFPVLVSDPFapPSDPAVA-----VDFETLWRRSAIVSFHVPL---TRGGLhpT 194
Cdd:cd12161  141 elagKTVGIVGTGAIGLRVARLFKAFGCKVLAYSRS--EKEEAKAlgieyVSLDELLAESDIVSLHLPLndeTKGLI--G 216
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149818447 195 AAMLAPVGEGGpplagpkLVVNTSRGPVVRD----AALDRPDVRAAILDVWEGEPE-PAAARLRDPKVLLASPHVA 265
Cdd:cd12161  217 KEKLALMKESA-------ILINTARGPVVDNealaDALNEGKIAGAGIDVFDMEPPlPADYPLLHAPNTILTPHVA 285
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
134-265 6.05e-17

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: 77.92  E-value: 6.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  134 HGHVGSKVARTLRALGFPVLVSDPFAPPSDPA-----VAVDFETLWRRSAIVSFHVPL---TRGGLhpTAAMLAPVGEGG 205
Cdd:pfam02826  44 LGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEeelgaRYVSLDELLAESDVVSLHLPLtpeTRHLI--NAERLALMKPGA 121
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149818447  206 pplagpkLVVNTSRGPVV-RDA---ALDRPDVRAAILDVWEGEPEPAAARLRDPKVLLASPHVA 265
Cdd:pfam02826 122 -------ILINTARGGLVdEDAliaALKSGRIAGAALDVFEPEPLPADHPLLDLPNVILTPHIA 178
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
42-285 1.22e-16

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: 79.75  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  42 GARALVVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQwVAAALL--TTRpRWPEA 119
Cdd:cd05301   43 GADGLLCTLTDKIDAELLDAAPPLKVIANYSVGYDHIDVDAAKARGIPVTNTPDVLTDATAD-LAFALLlaAAR-RVVEG 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 120 LREA------GDAPTVGVVGHGHVG-----------SKVARTLRALGFPVLVSDPFAPPSD----PAVAVDFETLWRRSA 178
Cdd:cd05301  121 DRFVragewkGWSPTLLLGTDLHGKtlgivgmgrigQAVARRAKGFGMKILYHNRSRKPEAeeelGARYVSLDELLAESD 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 179 IVSFHVPL---TRGGLhpTAAMLAPVgeggPPLAgpkLVVNTSRGPVVRDA----ALDRPDVRAAILDVWEGEPEPAAAR 251
Cdd:cd05301  201 FVSLHCPLtpeTRHLI--NAERLALM----KPTA---ILINTARGGVVDEDalveALKSGKIAGAGLDVFEPEPLPADHP 271
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 149818447 252 LRD-PKVLLAsPHVAGYSLDAKIDASLAVARQLAA 285
Cdd:cd05301  272 LLTlPNVVLL-PHIGSATVETRTAMAELAADNLLA 305
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
55-274 1.48e-16

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: 79.90  E-value: 1.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  55 DAALLDACPE-LEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQwVAAALL--TTR--PRWPEALReAGDAPTV 129
Cdd:cd12168   66 DEELISPLPPsLKIIAHAGAGYDQIDVDALTKRGIQVSNTPGAVDEATAD-TALFLIlgALRnfSRAERSAR-AGKWRGF 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 130 GVVGHGHVG--------------SKVARTLRALGFPVLVSDPFAPPSDPAVA-----VDFETLWRRSAIVSFHVPLTRGG 190
Cdd:cd12168  144 LDLTLAHDPrgktlgilglggigKAIARKAAAFGMKIIYHNRSRLPEELEKAlatyyVSLDELLAQSDVVSLNCPLTAAT 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 191 LHP-TAAMLAPVGEGGpplagpkLVVNTSRGPVVRDA----ALDRPDVRAAILDVWEGEPEPAAARLRDPKVLLaSPHVA 265
Cdd:cd12168  224 RHLiNKKEFAKMKDGV-------IIVNTARGAVIDEDalvdALESGKVASAGLDVFENEPEVNPGLLKMPNVTL-LPHMG 295

                 ....*....
gi 149818447 266 GYSLDAKID 274
Cdd:cd12168  296 TLTVETQEK 304
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
45-283 2.94e-16

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: 78.76  E-value: 2.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  45 ALVVRSVttvDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQWVAAALLTTRPRWPEALREAG 124
Cdd:cd12174   34 ALIVRSD---KLHDMDFAPSLKAIARAGAGVNNIDVDAASKRGIVVFNTPGANANAVAELVIAMMLALSRNIIQAIKWVT 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 125 DAPTVGVVG-----------------------HGHVGSKVARTLRALGFPVLVSDPFAPP-------SDPAVAVDFETLW 174
Cdd:cd12174  111 NGDGDDISKgvekgkkqfvgtelrgktlgvigLGNIGRLVANAALALGMKVIGYDPYLSVeaawklsVEVQRVTSLEELL 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 175 RRSAIVSFHVPL---TRGGLhpTAAMLAPVGEGGpplagpkLVVNTSRGPVVRDAAL----DRPDVRAAILDVwegePEP 247
Cdd:cd12174  191 ATADYITLHVPLtdeTRGLI--NAELLAKMKPGA-------ILLNFARGEIVDEEALlealDEGKLGGYVTDF----PEP 257
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 149818447 248 AAARlRDPKVlLASPHVAGYSLDAKIDASLAVARQL 283
Cdd:cd12174  258 ALLG-HLPNV-IATPHLGASTEEAEENCAVMAARQI 291
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
11-285 3.11e-16

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: 78.66  E-value: 3.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  11 AVPLAGEVFTKLGE---VHALPSGAIDAATLARIGA--RALVVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAA 85
Cdd:cd12156    6 LGPLPPELLAELEArftVHRLWEAADPAALLAEHGGriRAVVTNGETGLSAALIAALPALELIASFGVGYDGIDLDAARA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  86 REVAVADAAGCNSLAVAQWVAAALLTTRPRWPEALR--EAGDAPTVGVVGHGHVGSK-------------VARTLRALGF 150
Cdd:cd12156   86 RGIRVTNTPGVLTDDVADLAVGLLLAVLRRIPAADRfvRAGRWPKGAFPLTRKVSGKrvgivglgrigraIARRLEAFGM 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 151 PVLVSDP----------FAPPSDPAVAVDFetlwrrsAIVSfhVPLTRGGLH-PTAAMLAPVGEGGpplagpkLVVNTSR 219
Cdd:cd12156  166 EIAYHGRrpkpdvpyryYASLLELAAESDV-------LVVA--CPGGPATRHlVNAEVLEALGPDG-------VLVNVAR 229
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149818447 220 GPVVRDAALdrpdVRA--------AILDVWEGEPEPAAARLRDPKVLLaSPHVAGYSLDAKIDASLAVARQLAA 285
Cdd:cd12156  230 GSVVDEAAL----IAAlqegriagAGLDVFENEPNVPAALLDLDNVVL-TPHIASATVETRRAMGDLVLANLEA 298
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
42-271 2.21e-15

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: 76.19  E-value: 2.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  42 GARALVVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQWVAA---ALLTTRPRWPE 118
Cdd:cd01619   45 GADAILTAFTDKIDAELLDKAPGLKFISLRATGYDNIDLDYAKELGIGVTNVPEYSPNAVAEHTIAlilALLRNRKYIDE 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 119 ------------ALREAGDApTVGVVGHGHVGSKVARTLRALGFPVLVSDPFAPPSDPAVAVDF---ETLWRRSAIVSFH 183
Cdd:cd01619  125 rdknqdlqdagvIGRELEDQ-TVGVVGTGKIGRAVAQRAKGFGMKVIAYDPFRNPELEDKGVKYvslEELFKNSDIISLH 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 184 VPLTRGGLHP-TAAMLAPVGEGgpplagpKLVVNTSRGPVV-RDA---ALDRPDVRAAILDVWEGE-------------P 245
Cdd:cd01619  204 VPLTPENHHMiNEEAFKLMKKG-------VIIINTARGSLVdTEAlieALDSGKIFGAGLDVLEDEtpdllkdlegeifK 276
                        250       260
                 ....*....|....*....|....*..
gi 149818447 246 EPAAARL-RDPKVLLaSPHVAGYSLDA 271
Cdd:cd01619  277 DALNALLgRRPNVII-TPHTAFYTDDA 302
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
19-267 1.06e-14

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: 74.09  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  19 FTKLGEVHAL-----PSGAIDAATLARIGARALVV-RSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVAD 92
Cdd:cd12169   18 WSKLDDRAEVtvfndHLLDEDALAERLAPFDAIVLmRERTPFPAALLERLPNLKLLVTTGMRNASIDLAAAKERGIVVCG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  93 AAGcNSLAVAQWVAAALLTTRPRWPE---ALREAGDAPTVGVVGHGHV---------GSKVARTLRALGFPVLVSDPFAP 160
Cdd:cd12169   98 TGG-GPTATAELTWALILALARNLPEedaALRAGGWQTTLGTGLAGKTlgivglgriGARVARIGQAFGMRVIAWSSNLT 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 161 PSDPA-----VAVDFETLWRRSAIVSFHVPL---TRGGLhpTAAMLAPVGEGGpplagpkLVVNTSRGPVVRDAA----L 228
Cdd:cd12169  177 AERAAaagveAAVSKEELFATSDVVSLHLVLsdrTRGLV--GAEDLALMKPTA-------LLVNTSRGPLVDEGAllaaL 247
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 149818447 229 DRPDVRAAILDVWEGEPEPAAARLRDPKVLLASPHVaGY 267
Cdd:cd12169  248 RAGRIAGAALDVFDVEPLPADHPLRGLPNVLLTPHI-GY 285
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
54-271 1.27e-14

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: 74.23  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  54 VDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQWVAAALLTTRPRwpeaLREAGDAP------ 127
Cdd:cd12187   53 LDAEVLEKLPRLKLIATRSTGFDHIDLEACRERGIAVCNVPDYGEATVAEHAFALLLALSRK----LREAIERTrrgdfs 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 128 ------------TVGVVGHGHVGSKVARTLRALGFPVLVSDPFAPPSDPAVA----VDFETLWRRSAIVSFHVPLTRGGL 191
Cdd:cd12187  129 qaglrgfelagkTLGVVGTGRIGRRVARIARGFGMKVLAYDVVPDEELAERLgfryVSLEELLQESDIISLHVPYTPQTH 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 192 H----PTAAMLAPvgeggpplagPKLVVNTSRGPVVRDAA----LDRPDVRAAILDVWEGEPE--------PAAARLRDP 255
Cdd:cd12187  209 HlinrENFALMKP----------GAVLINTARGAVVDTEAlvraLKEGKLAGAGLDVLEQEEVlreeaelfREDVSPEDL 278
                        250       260
                 ....*....|....*....|....*...
gi 149818447 256 KVLLA------------SPHVAGYSLDA 271
Cdd:cd12187  279 KKLLAdhallrkpnviiTPHVAYNTKEA 306
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
19-271 5.70e-14

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: 71.97  E-value: 5.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  19 FTKLGEV-HALPSGAIDAATLA-RIGARALVVRSVT-TVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAG 95
Cdd:cd12177   21 LKKIGYVdRFEVPPDISGKALAeKLKGYDIIIASVTpNFDKEFFEYNDGLKLIARHGIGYDNVDLKAATEHGVIVTRVPG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  96 -CNSLAVAQWVAAALLTTRPRWPEA-LREAGDAPTVGVVG--------------HGHVGSKVARTLRAlGF--PVLVSDP 157
Cdd:cd12177  101 aVERDAVAEHAVALILTVLRKINQAsEAVKEGKWTERANFvghelsgktvgiigYGNIGSRVAEILKE-GFnaKVLAYDP 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 158 FAPPSDP----AVAVDFETLWRRSAIVSFHVPLTRGglhpTAAMLapvgeGGPPLAGPK---LVVNTSRGPVVRDAA--- 227
Cdd:cd12177  180 YVSEEVIkkkgAKPVSLEELLAESDIISLHAPLTEE----TYHMI-----NEKAFSKMKkgvILVNTARGELIDEEAlie 250
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 149818447 228 -LDRPDVRAAILDVWEGEPEPAAAR-LRDPKVLLaSPHVAGYSLDA 271
Cdd:cd12177  251 aLKSGKIAGAGLDVLEEEPIKADHPlLHYENVVI-TPHIGAYTYES 295
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
38-284 2.69e-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: 240655 [Multi-domain]  Cd Length: 317  Bit Score: 67.26  E-value: 2.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  38 LARIG-ARALVVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQwVAAALL--TTR- 113
Cdd:cd12178   38 LERIAdYDALITPLSTPVDKEIIDAAKNLKIIANYGAGFDNIDVDYAKEKGIPVTNTPAVSTEPTAE-LTFGLIlaLARr 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 114 -PRWPEALREAGD---APTVGVVGHGHVG-----------SKVARTLRALGFPVLVSDPFAPPSDP-----AVAVDFETL 173
Cdd:cd12178  117 iAEGDRLMRRGGFlgwAPLFFLGHELAGKtlgiigmgrigQAVARRAKAFGMKILYYNRHRLSEETekelgATYVDLDEL 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 174 WRRSAIVSFHVPLTRGGLH-----------PTAamlapvgeggpplagpkLVVNTSRGPVVRDAALDRP----DVRAAIL 238
Cdd:cd12178  197 LKESDFVSLHAPYTPETHHlidaaafklmkPTA-----------------YLINAARGPLVDEKALVDAlktgEIAGAAL 259
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 149818447 239 DVWEGEPEPAAARLRDPKVLLaSPHVAgyslDAKIDASLAVARQLA 284
Cdd:cd12178  260 DVFEFEPEVSPELKKLDNVIL-TPHIG----NATVEARDAMAKEAA 300
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
26-268 3.68e-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: 240642 [Multi-domain]  Cd Length: 314  Bit Score: 66.50  E-value: 3.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  26 HALPSGAIDAATLARIGARAL-----VVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAArEVAVADAAGcNSLA 100
Cdd:cd12165   17 AALEGLYAEVPELPDEAAEEAledadVLVGGRLTKEEALAALKRLKLIQVPSAGVDHLPLERLPE-GVVVANNHG-NSPA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 101 VAQWVAAALLTTRPRWPEALRE--AGDAPTVGVVG---------------HGHVGSKVARTLRALGFPVLV---SDPFAP 160
Cdd:cd12165   95 VAEHALALILALAKRIVEYDNDlrRGIWHGRAGEEpeskelrgktvgilgYGHIGREIARLLKAFGMRVIGvsrSPKEDE 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 161 PSDPAVAV-DFETLWRRSAIVSFHVPL---TRGGLhpTAAMLAPVGEGgpplagpKLVVNTSRGPVVRDAAL-----DRP 231
Cdd:cd12165  175 GADFVGTLsDLDEALEQADVVVVALPLtkqTRGLI--GAAELAAMKPG-------AILVNVGRGPVVDEEALyealkERP 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 149818447 232 DVRAAIlDVWEGEPEPAAARL--RDP----KVLLASPHVAGYS 268
Cdd:cd12165  246 IAGAAI-DVWWRYPSRGDPVApsRYPfhelPNVIMSPHNAGWT 287
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
6-272 1.02e-11

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 65.39  E-value: 1.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447   6 IVVDDAVPLAG---EVFTKLGEVHALPSGAIDAaTLARIGARALVVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEA 82
Cdd:PRK08410   3 IVILDAKTLGDkdlSVFEEFGDFQIYPTTSPEE-VIERIKDANIIITNKVVIDKEVLSQLPNLKLICITATGTNNVDIEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  83 LAAREVAVADAAGCNSLAVAQWVAAAL--LTTRPRWPEALREAG-----DAPTVGVVGHGHVGSK-------------VA 142
Cdd:PRK08410  82 AKKKGIAVKNVAGYSTESVAQHTFAMLlsLLGRINYYDRYVKSGeysesPIFTHISRPLGEIKGKkwgiiglgtigkrVA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 143 RTLRALGFPVLVSDPFAPPSDPAV-AVDFETLWRRSAIVSFHVPL---TRGGLHPTAAMLapvgeggppLAGPKLVVNTS 218
Cdd:PRK08410 162 KIAQAFGAKVVYYSTSGKNKNEEYeRVSLEELLKTSDIISIHAPLnekTKNLIAYKELKL---------LKDGAILINVG 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149818447 219 RGPVVRDA----ALDRPDVRAAiLDVWEGEPEPAAARLRDPKV---LLASPHVAGYSLDAK 272
Cdd:PRK08410 233 RGGIVNEKdlakALDEKDIYAG-LDVLEKEPMEKNHPLLSIKNkekLLITPHIAWASKEAR 292
PRK06487 PRK06487
2-hydroxyacid dehydrogenase;
42-272 3.28e-11

2-hydroxyacid dehydrogenase;


Pssm-ID: 180588 [Multi-domain]  Cd Length: 317  Bit Score: 63.95  E-value: 3.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  42 GARALVVRSVTtVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQWVAAALL--TTR-PRWPE 118
Cdd:PRK06487  45 GAQVAISNKVA-LDAAALAAAPQLKLILVAATGTNNVDLAAARERGITVCNCQGYGTPSVAQHTLALLLalATRlPDYQQ 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 119 ALREAG----------DAP-------TVGVVGHGHVGSKVARTLRALGFPVLVSDPFAPPSDPAvAVDFETLWRRSAIVS 181
Cdd:PRK06487 124 AVAAGRwqqssqfcllDFPivelegkTLGLLGHGELGGAVARLAEAFGMRVLIGQLPGRPARPD-RLPLDELLPQVDALT 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 182 FHVPL---TRG--GLHPTAAMlapvgeggPPLAgpkLVVNTSRGPVVRDA----ALDRPDVRAAILDVWEGEPEPAAARL 252
Cdd:PRK06487 203 LHCPLtehTRHliGARELALM--------KPGA---LLINTARGGLVDEQaladALRSGHLGGAATDVLSVEPPVNGNPL 271
                        250       260
                 ....*....|....*....|..
gi 149818447 253 RDPKV--LLASPHVAGYSLDAK 272
Cdd:PRK06487 272 LAPDIprLIVTPHSAWGSREAR 293
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
13-284 3.93e-11

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: 63.37  E-value: 3.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  13 PLAGEVFTKLG-EVHALPSGAIDAATLARI-GARALVVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAV 90
Cdd:cd12176   11 PSADELFRAGGiEVERLKGALDEDELIEALkDVHLLGIRSKTQLTEEVLEAAPKLLAIGCFCIGTNQVDLDAAAKRGIPV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  91 ADAAGCNSLAVAQWVAAALLTTRPRWPEALREAGDA--------------PTVGVVGHGHVGSKVARTLRALGFPVLVSD 156
Cdd:cd12176   91 FNAPFSNTRSVAELVIGEIIMLARRLPDRNAAAHRGiwnksatgshevrgKTLGIIGYGHIGSQLSVLAEALGMRVIFYD 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 157 PfAP--PSDPAVAVD-FETLWRRSAIVSFHVP---LTRGGLhpTAAMLAPVGEGGpplagpkLVVNTSRGPVVR-DA--- 226
Cdd:cd12176  171 I-AEklPLGNARQVSsLEELLAEADFVTLHVPatpSTKNMI--GAEEIAQMKKGA-------ILINASRGTVVDiDAlae 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149818447 227 ALDRPDVRAAILDVWEGEP----EPAAARLR-DPKVLLaSPHVAGYSLDAKIDASLAVARQLA 284
Cdd:cd12176  241 ALRSGHLAGAAVDVFPEEPasngEPFSSPLQgLPNVIL-TPHIGGSTEEAQENIGLEVAGKLV 302
PRK13243 PRK13243
glyoxylate reductase; Reviewed
45-298 9.87e-11

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 62.50  E-value: 9.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  45 ALVVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQWVAAALLTTRPRWPEA----- 119
Cdd:PRK13243  48 ALVTMLSERIDCEVFEAAPRLRIVANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADFAWALLLATARRLVEAdhfvr 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 120 -----LREAGDAP-----------TVGVVGHGHVGSKVARTLRALGFPVL----VSDPFAPPSDPAVAVDFETLWRRSAI 179
Cdd:PRK13243 128 sgewkRRGVAWHPlmflgydvygkTIGIIGFGRIGQAVARRAKGFGMRILyysrTRKPEAEKELGAEYRPLEELLRESDF 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 180 VSFHVPLTRGGLHptaamlaPVGEGGPPLAGPK-LVVNTSRGPVVRDAALDRPD----VRAAILDVWEGEPEPAAARLRD 254
Cdd:PRK13243 208 VSLHVPLTKETYH-------MINEERLKLMKPTaILVNTARGKVVDTKALVKALkegwIAGAGLDVFEEEPYYNEELFSL 280
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 149818447 255 PKVLLAsPHVAGYSLDAKIDASLAVARQLAarwgaergAFERGR 298
Cdd:PRK13243 281 KNVVLA-PHIGSATFEAREGMAELVAENLI--------AFKRGE 315
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
63-273 3.01e-10

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: 61.19  E-value: 3.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  63 PELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQWVAAALLT-TR---PRWPEALREAGDAP----------- 127
Cdd:cd05302   83 KNLKLALTAGIGSDHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILIlVRnyvPGHEQAIEGGWNVAdvvkraydleg 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 128 -TVGVVGHGHVGSKVARTLRALGFPVLVSDPFAPPSDPAVA------VDFETLWRRSAIVSFHVPLTRGGLHP-TAAMLA 199
Cdd:cd05302  163 kTVGTVGAGRIGLRVLRRLKPFDVHLLYYDRHRLPEEVEKElgltrhADLEDMVSKCDVVTINCPLHPETEGLfNKELLS 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 200 PVGEGGpplagpkLVVNTSRGPVVrdaalDRPDVRAAIL---------DVWEGEPEPAAARLRDPKVLLASPHVAGYSLD 270
Cdd:cd05302  243 KMKKGA-------YLVNTARGKIC-----DREAVAEALEsghlagyagDVWFPQPAPKDHPWRTMPNNAMTPHISGTTLD 310

                 ...
gi 149818447 271 AKI 273
Cdd:cd05302  311 AQA 313
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
134-267 5.76e-10

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: 60.24  E-value: 5.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 134 HGHVGSKVARTLRALGFPVLVSDPFAPPSDPAVA---VDFETLWRRSAIVSFHVPLTRGGLHP-TAAMLAPVGEGGppla 209
Cdd:cd12186  153 TGRIGSAAAKIFKGFGAKVIAYDPYPNPELEKFLlyyDSLEDLLKQADIISLHVPLTKENHHLiNAEAFAKMKDGA---- 228
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149818447 210 gpkLVVNTSRGPVVrD-----AALDRPDVRAAILDVWEGE-------------PEPAAARLRD-PKVLLaSPHVAGY 267
Cdd:cd12186  229 ---ILVNAARGGLV-DtkaliDALDSGKIAGAALDTYENEtgyfnkdwsgkeiEDEVLKELIAmPNVLI-TPHIAFY 300
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
55-268 7.90e-10

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: 59.46  E-value: 7.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  55 DAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQWVAAALLT------------TRPRW--PEAL 120
Cdd:cd05300   50 LPELLPAAPRLRWIQSTSAGVDALLFPELLERDVVLTNARGIFGPPIAEYVLGYMLAfarklpryarnqAERRWqrRGPV 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 121 RE----------AGDaptvgvvghghVGSKVARTLRALGFPVLVSDPFAPPSDPAVAVDF------ETLWRRSAIVSFhV 184
Cdd:cd05300  130 RElagktvlivgLGD-----------IGREIARRAKAFGMRVIGVRRSGRPAPPVVDEVYtpdeldELLPEADYVVNA-L 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 185 PL---TRGGLHP--TAAMlapvgeggPPLAgpkLVVNTSRGPVVRD----AALDRPDVRAAILDVWEGEPEPAAARLRD- 254
Cdd:cd05300  198 PLtpeTRGLFNAerFAAM--------KPGA---VLINVGRGSVVDEdaliEALESGRIAGAALDVFEEEPLPADSPLWDl 266
                        250
                 ....*....|....
gi 149818447 255 PKVLLaSPHVAGYS 268
Cdd:cd05300  267 PNVII-TPHISGDS 279
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
43-227 4.31e-09

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: 57.30  E-value: 4.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  43 ARALVVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQwVAAALLTTRPR------- 115
Cdd:cd12157   45 ADGLMAFMPDRIDADFLDACPRLKIIACALKGYDNFDVEACTARGIWVTIVPDLLTEPTAE-LTIGLLIGLGRhilagdr 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 116 ---------WPEALREAG-DAPTVGVVGHGHVGSKVARTLRALGFPVLVSDPFAPPSDPAVA-----VDFETLWRRSAIV 180
Cdd:cd12157  124 fvrsgkfggWRPKFYGTGlDGKTVGILGMGALGRAIARRLSGFGATLLYYDPHPLDQAEEQAlnlrrVELDELLESSDFL 203
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 149818447 181 SFHVPLTRGGLH-PTAAMLAPVGEGgpplagpKLVVNTSRGPVVRDAA 227
Cdd:cd12157  204 VLALPLTPDTLHlINAEALAKMKPG-------ALLVNPCRGSVVDEAA 244
PRK06932 PRK06932
2-hydroxyacid dehydrogenase;
26-265 5.03e-09

2-hydroxyacid dehydrogenase;


Pssm-ID: 235890 [Multi-domain]  Cd Length: 314  Bit Score: 57.12  E-value: 5.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  26 HALPSGAIDAATLARIgaralVVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQWV 105
Cdd:PRK06932  32 HTSAEQTIERAKDADI-----VITSKVLFTRETLAQLPKLKLIAITATGTNNVDLVAAKELGIAVKNVTGYSSTTVPEHV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 106 AAALLTTR------------PRWPEALREA-GDAP-------TVGVVGHGHVGSKVARTLRALGFPVLVSDPFAPPSDPA 165
Cdd:PRK06932 107 LGMIFALKhslmgwyrdqlsDRWATCKQFCyFDYPitdvrgsTLGVFGKGCLGTEVGRLAQALGMKVLYAEHKGASVCRE 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 166 VAVDFETLWRRSAIVSFHVPLTRGGLH----PTAAMLAPVGeggpplagpkLVVNTSRGPVVRD----AALDRPDVRAAI 237
Cdd:PRK06932 187 GYTPFEEVLKQADIVTLHCPLTETTQNlinaETLALMKPTA----------FLINTGRGPLVDEqallDALENGKIAGAA 256
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 149818447 238 LDVWEGEPEP-------AAARLRDpkvLLASPHVA 265
Cdd:PRK06932 257 LDVLVKEPPEkdnpliqAAKRLPN---LLITPHIA 288
PRK07574 PRK07574
NAD-dependent formate dehydrogenase;
63-271 1.61e-08

NAD-dependent formate dehydrogenase;


Pssm-ID: 181041  Cd Length: 385  Bit Score: 55.84  E-value: 1.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  63 PELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQWVAAALLTTRPRWPEALREAGD----------------A 126
Cdd:PRK07574 113 PNLKLAITAGIGSDHVDLQAASEHGITVAEVTGSNSISVAEHVVMMILALVRNYEPSHRQAVEggwniadcvsrsydleG 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 127 PTVGVVGHGHVGSKVARTLRALGFPVLVSDPFAPPSDP------AVAVDFETLWRRSAIVSFHVPLTRGGLHP-TAAMLA 199
Cdd:PRK07574 193 MTVGIVGAGRIGLAVLRRLKPFDVKLHYTDRHRLPEEVeqelglTYHVSFDSLVSVCDVVTIHCPLHPETEHLfDADVLS 272
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149818447 200 PVGEGGpplagpkLVVNTSRGPVV-RDA---ALDRPDVRAAILDVWEGEPEPAAARLRDPKVLLASPHVAGYSLDA 271
Cdd:PRK07574 273 RMKRGS-------YLVNTARGKIVdRDAvvrALESGHLAGYAGDVWFPQPAPADHPWRTMPRNGMTPHISGTTLSA 341
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
42-271 5.17e-08

(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: 54.22  E-value: 5.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  42 GARALVVRSVTTVDAALLDACPEL--EFVGTATAGLDHLDLEAlaAREV-------------AVADAAGCNSLAVAQWVA 106
Cdd:cd12184   44 GHDAVIVRGNCFADKENLEIYKEYgiKYVFTRTVGFNHIDLEA--AKELgfkmarvpsyspnAIAELAFTLAMTLSRHTA 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 107 AALLTTRPR--------WPEALREAgdapTVGVVGHGHVGSKVARTLRALGFPVLVSDPFapPSDPA----VAVDFETLW 174
Cdd:cd12184  122 YTASRTANKnfkvdpfmFSKEIRNS----TVGIIGTGRIGLTAAKLFKGLGAKVIGYDIY--PSDAAkdvvTFVSLDELL 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 175 RRSAIVSFHVPLTRG--GLHPTAAMLAPVGEGGpplagpkLVVNTSRGPVVRDAA----LDRPDVRAAILDVWEGE---- 244
Cdd:cd12184  196 KKSDIISLHVPYIKGknDKLINKEFISKMKDGA-------ILINTARGELQDEEAileaLESGKLAGFGTDVLNNEkeif 268
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 149818447 245 ---------PEPAAARLRD--PKVLLaSPHVAGYSLDA 271
Cdd:cd12184  269 fkdfdgdkiEDPVVEKLLDlyPRVLL-TPHIGSYTDEA 305
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
53-285 1.84e-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: 240643 [Multi-domain]  Cd Length: 300  Bit Score: 52.21  E-value: 1.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  53 TVDAALLDACPELEFVGTATAGLDHLDleALAAREVAVADAAGCNSLAVAQWVAAALLTTRPRWPEALREAGDAPTVGVV 132
Cdd:cd12166   49 PPVLEALRALPRLRVVQTLSAGYDGVL--PLLPEGVTLCNARGVHDASTAELAVALILASLRGLPRFVRAQARGRWEPRR 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 133 GHGHVGSKV------------ARTLRALGFPVLVSDPFAPPSDPAVAVD-FETLWRRSAIVSFHVPLTRGGLHPT-AAML 198
Cdd:cd12166  127 TPSLADRRVlivgygsigraiERRLAPFEVRVTRVARTARPGEQVHGIDeLPALLPEADVVVLIVPLTDETRGLVdAEFL 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 199 APVGEGGpplagpkLVVNTSRGPVVRDAAL----DRPDVRAAiLDVWEGEPEPAAARL-RDPKVLLaSPHVAGYSLDAKI 273
Cdd:cd12166  207 ARMPDGA-------LLVNVARGPVVDTDALvaelASGRLRAA-LDVTDPEPLPPGHPLwSAPGVLI-TPHVGGATPAFLP 277
                        250
                 ....*....|..
gi 149818447 274 DASLAVARQLAA 285
Cdd:cd12166  278 RAYALVRRQLRR 289
2-Hacid_dh_5 cd12163
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
63-266 1.19e-06

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: 49.96  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  63 PELEFVGTATAGLDH-LDLEALAAREVAVADAAGCNSLAVAQWVAAALLTTR---PRWPEALREAGDAPTVGVVGHGHVG 138
Cdd:cd12163   53 PNLRLVQLFSAGADHwLGHPLYKDPEVPLCTASGIHGPQIAEWVIGTWLVLShhfLQYIELQKEQTWGRRQEAYSVEDSV 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 139 SK-------------VARTLRALGFPVL-------------VSDPFAPP----------------SDPAVAVDFetLWRR 176
Cdd:cd12163  133 GKrvgilgygsigrqTARLAQALGMEVYaytrsprptpesrKDDGYIVPgtgdpdgsipsawfsgTDKASLHEF--LRQD 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 177 SAIVSFHVPLTRGGLHP-TAAMLAPVGEGGPplagpkLVVNTSRGPVVRD----AALDRPDVRAAILDVWEGEPEPAAAR 251
Cdd:cd12163  211 LDLLVVSLPLTPATKHLlGAEEFEILAKRKT------FVSNIARGSLVDTdalvAALESGQIRGAALDVTDPEPLPADHP 284
                        250
                 ....*....|....*
gi 149818447 252 LRDPKVLLASPHVAG 266
Cdd:cd12163  285 LWSAPNVIITPHVSW 299
2-Hacid_dh_15 cd12180
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
41-307 1.80e-06

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: 49.26  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  41 IGARALVVRSVTTVDAALLDACP----ELEFVGTATAGLDHLDLEALAAREVAVAdaAGCNSLAVAQWVAAALLTTRPRW 116
Cdd:cd12180   37 ADADVLLARPTNGRGAAPAVPPPgwpgRLRWVQLVSSGIDYYPDWLFEGPVVTCA--RGVAAEAIAEFVLAAILAAAKRL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 117 PEaLREAGDAP------------TVGVVGHGHVGSKVARTLRALGFPVLV---SDPFAPPSDPAVAVDFETLWRRSAIVS 181
Cdd:cd12180  115 PE-IWVKGAEQwrreplgslagsTLGIVGFGAIGQALARRALALGMRVLAlrrSGRPSDVPGVEAAADLAELFARSDHLV 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 182 FHVPLTRGGLH-PTAAMLApvgeggppLAGPKL-VVNTSRGPVVRD----AALDRPDVRAAILDVWEGEPEPAAARL-RD 254
Cdd:cd12180  194 LAAPLTPETRHlINADVLA--------QAKPGLhLINIARGGLVDQeallEALDSGRISLASLDVTDPEPLPEGHPLyTH 265
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 149818447 255 PKVLLaSPHVAGYSLDAKidaslavaRQLAARWGAERGAFERGRWLgpAGVVE 307
Cdd:cd12180  266 PRVRL-SPHTSAIAPDGR--------RNLADRFLENLARYRAGQPL--HDLVD 307
PRK11790 PRK11790
phosphoglycerate dehydrogenase;
13-284 3.88e-06

phosphoglycerate dehydrogenase;


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 48.64  E-value: 3.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  13 PLAGEVFTKLG----EVHalpSGAIDAATL-ARI-GARALVVRSVTTVDAALLDACPELEFVGTATAGLDHLDLEALAAR 86
Cdd:PRK11790  21 QSAVEVLRAAGytniEYH---KGALDEEELiEAIkDAHFIGIRSRTQLTEEVLAAAEKLVAIGCFCIGTNQVDLDAAAKR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  87 EVAVADAAGCNSLAVAQWV-AAALLTTRpRWPEALREAGDAptvgvvghghVGSKVA--------RTL------------ 145
Cdd:PRK11790  98 GIPVFNAPFSNTRSVAELViGEIILLLR-GIPEKNAKAHRG----------GWNKSAagsfevrgKTLgivgyghigtql 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 146 ----RALGFPVLVSDPFAP-PSDPAVAVD-FETLWRRSAIVSFHVPltrgGLHPTAAMLapvgeGGPPLAGPK---LVVN 216
Cdd:PRK11790 167 svlaESLGMRVYFYDIEDKlPLGNARQVGsLEELLAQSDVVSLHVP----ETPSTKNMI-----GAEELALMKpgaILIN 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149818447 217 TSRGPVVR----DAALDRPDVRAAILDVWEGEP----EPAAARLRD-PKVLLaSPHVAGYSLDAKIDASLAVARQLA 284
Cdd:PRK11790 238 ASRGTVVDidalADALKSGHLAGAAIDVFPVEPksngDPFESPLRGlDNVIL-TPHIGGSTQEAQENIGLEVAGKLV 313
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
134-244 7.22e-06

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: 47.44  E-value: 7.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 134 HGHVGSKVARTLRALGFPVLVSDPFapPSDPAVA-----VDFETLWRRSAIVSFHVPLTRGGLH----------PTAAML 198
Cdd:cd12183  152 TGKIGQAFARILKGFGCRVLAYDPY--PNPELAKlgveyVDLDELLAESDIISLHCPLTPETHHlinaetiakmKDGVML 229
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 149818447 199 apvgeggpplagpklvVNTSRGPVV--RDA--ALDRPDVRAAILDVWEGE 244
Cdd:cd12183  230 ----------------INTSRGGLIdtKALieALKSGKIGGLGLDVYEEE 263
PRK15409 PRK15409
glyoxylate/hydroxypyruvate reductase GhrB;
53-264 1.32e-05

glyoxylate/hydroxypyruvate reductase GhrB;


Pssm-ID: 185307  Cd Length: 323  Bit Score: 46.67  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  53 TVDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQWVAAALLTTRPRWPE-ALR-EAG------ 124
Cdd:PRK15409  55 KVDAALLEKMPKLRAASTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLSTARRVVEvAERvKAGewtasi 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 125 -------DAPTVGVVGHGHVGSKVARTLRA-LGF--PVLVS----DPFAPPSDPAVAVDFETLWRRSAIVSFHVPLTRGG 190
Cdd:PRK15409 135 gpdwfgtDVHHKTLGIVGMGRIGMALAQRAhFGFnmPILYNarrhHKEAEERFNARYCDLDTLLQESDFVCIILPLTDET 214
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149818447 191 LHPT-AAMLAPVGEGGpplagpkLVVNTSRGPVVRD----AALDRPDVRAAILDVWEGEPEPAAARLRDPKVLLASPHV 264
Cdd:PRK15409 215 HHLFgAEQFAKMKSSA-------IFINAGRGPVVDEnaliAALQKGEIHAAGLDVFEQEPLSVDSPLLSLPNVVAVPHI 286
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
54-268 2.23e-05

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: 46.04  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  54 VDAALLDACPELEFVGTATAGLDHLDLEALAAREVAVADAAGCNSLAVAQWVAAALLTTRPRWPEALRE------AGDAP 127
Cdd:cd12155   50 FDELDLAKMKNLKWIQLYSAGVDYLPLEYIKKKGILLTNNSGIHSIPIAEWIVGYILEIYKGLKKAYKNqkekkwKMDSS 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 128 TVGVVGHGHV-------GSKVARTLRALGFPVL-VS------DPFappsDPAVAVD--FETLWRRSAIVSF--HVPLTRG 189
Cdd:cd12155  130 LLELYGKTILflgtgsiGQEIAKRLKAFGMKVIgVNtsgrdvEYF----DKCYPLEelDEVLKEADIVVNVlpLTEETHH 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 190 GLhpTAAMLAPVGEGGpplagpkLVVNTSRGPVVRDA----ALDRPDVRAAILDVWEGEPEPAAARLRD-PKVLLaSPHV 264
Cdd:cd12155  206 LF--DEAFFEQMKKGA-------LFINVGRGPSVDEDalieALKNKQIRGAALDVFEEEPLPKDSPLWDlDNVLI-TPHI 275

                 ....
gi 149818447 265 AGYS 268
Cdd:cd12155  276 SGVS 279
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
139-285 5.98e-05

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: 44.41  E-value: 5.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 139 SKVARTLRALGFPVLVsdpfappsdpavavdfetlWRRSA-----IVSFH------------------VPL---TRGGL- 191
Cdd:cd12164  145 AAVARRLAALGFPVSG-------------------WSRSPkdiegVTCFHgeegldaflaqtdilvclLPLtpeTRGILn 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 192 HPTAAMLAPvgeggpplaGPKLvVNTSRGPVVRD----AALDRPDVRAAILDVWEGEPEPAAARL-RDPKVLLaSPHVAG 266
Cdd:cd12164  206 AELLARLPR---------GAAL-INVGRGPHLVEadllAALDSGHLSGAVLDVFEQEPLPADHPLwRHPRVTV-TPHIAA 274
                        170
                 ....*....|....*....
gi 149818447 267 YSLDAkiDASLAVARQLAA 285
Cdd:cd12164  275 ITDPD--SAAAQVAENIRR 291
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
5-249 3.32e-04

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: 42.22  E-value: 3.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447   5 PIVVDDAVPLAGEVFTKLG-------EVHALPSGAIDAATLARIGARALVVRSV----TTVDAALLDACPeLEFVGTATA 73
Cdd:cd12154   18 PSVVATLVEAGHEVRVETGagigagfADQAYVQAGAIVVTLAKALWSLDVVLKVkeplTNAEYALIQKLG-DRLLFTYTI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447  74 GLDHLDL-EALAAREVAVADAAG-------CNSLAVAQWVAAALLT-TRPRWPEALREAGDAP--TVGVVGHGHVGSKVA 142
Cdd:cd12154   97 GADHRDLtEALARAGLTAIAVEGvelplltSNSIGAGELSVQFIARfLEVQQPGRLGGAPDVAgkTVVVVGAGVVGKEAA 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149818447 143 RTLRALGFPVLVSDPFAPPSDPA------VAVDFETLWRRSAIVSFHVPLTRGGLHP--TAAMLAPVGEGgpplagpKLV 214
Cdd:cd12154  177 QMLRGLGAQVLITDINVEALEQLeelggkNVEELEEALAEADVIVTTTLLPGKRAGIlvPEELVEQMKPG-------SVI 249
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 149818447 215 VNTSRGPVVRDAALDRPDVRAA-----ILDVWEGEPEPAA 249
Cdd:cd12154  250 VNVAVGAVGCVQALHTQLLEEGhgvvhYGDVNMPGPGCAM 289
2-Hacid_dh_3 cd12160
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
213-266 6.33e-03

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: 38.13  E-value: 6.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 149818447 213 LVVNTSRGPVVR----DAALDRPDVRAAILDVWEGEPEPAAARLRDPKVLLASPHVAG 266
Cdd:cd12160  227 WVVNVGRGATVDedalVAALESGRLGGAALDVTATEPLPASSPLWDAPNLILTPHAAG 284
 
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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