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Conserved domains on  [gi|1227727900|gb|OXW70850|]
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2-hydroxyacid dehydrogenase [Shigella flexneri]

Protein Classification

2-hydroxyacid dehydrogenase( domain architecture ID 10187446)

NAD(+)-dependent 2-hydroxyacid dehydrogenase specific to D-isomers, similar to D-lactate dehydrogenase, which converts D-lactate to pyruvate

EC:  1.1.1.28
Gene Ontology:  GO:0070404|GO:0008720

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 1-328 0e+00

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: 629.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   1 MKLAVYSTKQYDKKYLQQVNESFGFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSHPVLEELKKHGVKYIALRCAGFN 80
Cdd:cd12183     1 MKIAVFSTKPYDREFFEAANEGYGHELTYFEERLTEETASLAKGFDAVCVFVNDDLDAPVLEKLAELGVKLIALRCAGFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  81 NVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGFTMYGKTAGVIGTGKIGVAML 160
Cdd:cd12183    81 NVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKIHRAYNRVREGNFSLDGLLGFDLHGKTVGVIGTGKIGQAFA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 161 RILKGFGMRLLAFDPYPSAAALELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDS 240
Cdd:cd12183   161 RILKGFGCRVLAYDPYPNPELAKLGVEYVDLDELLAESDIISLHCPLTPETHHLINAETIAKMKDGVMLINTSRGGLIDT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 241 QAAIEALKNQKIGSLGMDVYENERDLFFEDKSNDVIQDDVFRRLSACHNVLFTGHQAFLTAEALTSISQTTLQNLSNLEK 320
Cdd:cd12183   241 KALIEALKSGKIGGLGLDVYEEEAGLFFEDHSDEIIQDDVLARLLSFPNVLITGHQAFFTKEALTNIAETTLENLDDFEA 320


                  ....*...
gi 1227727900 321 GETCPNEL 328
Cdd:cd12183   321 GKPLKNEV 328
 
Name Accession Description Interval E-value
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 1-328 0e+00

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: 629.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   1 MKLAVYSTKQYDKKYLQQVNESFGFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSHPVLEELKKHGVKYIALRCAGFN 80
Cdd:cd12183     1 MKIAVFSTKPYDREFFEAANEGYGHELTYFEERLTEETASLAKGFDAVCVFVNDDLDAPVLEKLAELGVKLIALRCAGFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  81 NVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGFTMYGKTAGVIGTGKIGVAML 160
Cdd:cd12183    81 NVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKIHRAYNRVREGNFSLDGLLGFDLHGKTVGVIGTGKIGQAFA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 161 RILKGFGMRLLAFDPYPSAAALELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDS 240
Cdd:cd12183   161 RILKGFGCRVLAYDPYPNPELAKLGVEYVDLDELLAESDIISLHCPLTPETHHLINAETIAKMKDGVMLINTSRGGLIDT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 241 QAAIEALKNQKIGSLGMDVYENERDLFFEDKSNDVIQDDVFRRLSACHNVLFTGHQAFLTAEALTSISQTTLQNLSNLEK 320
Cdd:cd12183   241 KALIEALKSGKIGGLGLDVYEEEAGLFFEDHSDEIIQDDVLARLLSFPNVLITGHQAFFTKEALTNIAETTLENLDDFEA 320


                  ....*...
gi 1227727900 321 GETCPNEL 328
Cdd:cd12183   321 GKPLKNEV 328
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
 1-329 3.05e-132

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: 379.05  E-value: 3.05e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   1 MKLAVYSTKQYDKKYLQQVnESFGFELEFFDFLLT-EKTAKTANGCEAVCIFVNDDGSHPVLEELKkhGVKYIALRCAGF 79
Cdd:COG1052     1 KPILVLDPRTLPDEVLERL-EAEHFEVTVYEDETSpEELAERAAGADAVITNGKDPIDAEVLEALP--GLKLIANRGVGY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  80 NNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLE-GLTGFTMYGKTAGVIGTGKIGVA 158
Cdd:COG1052    78 DNIDLAAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSpGLLGRDLSGKTLGIIGLGRIGQA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 159 MLRILKGFGMRLLAFDPYPSAAALELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALI 238
Cdd:COG1052   158 VARRAKGFGMKVLYYDRSPKPEVAELGAEYVSLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARGGLV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 239 DSQAAIEALKNQKIGSLGMDVYENERDlffedksndvIQDDvfrRLSACHNVLFTGHQAFLTAEALTSISQTTLQNLSNL 318
Cdd:COG1052   238 DEAALIEALKSGRIAGAGLDVFEEEPP----------PPDH---PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAF 304

                         330
                  ....*....|.
gi 1227727900 319 EKGETCPNELV 329
Cdd:COG1052   305 LAGEPPPNPVN 315
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
 9-329 7.99e-103

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: 304.21  E-value: 7.99e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   9 KQYDKKYLQQvnesfgFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSHPVLEELKKhgVKYIALRCAGFNNVDLDAAK 88
Cdd:pfam00389   8 SPEALELLKE------GEVEVHDELLTEELLEKAKDADALIVRSRTKVTAEVLEAAPK--LKVIGRAGVGVDNVDLDAAT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  89 ELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGFTMYGKTAGVIGTGKIGVAMLRILKGFGM 168
Cdd:pfam00389  80 ERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLELYGKTLGVIGGGGIGGGVAAIAKAFGM 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 169 RLLAFDPYPSAAALELGVEYVDLPTLFSESdvislhcplTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALK 248
Cdd:pfam00389 160 GVVAYDPYPNPERAEAGGVEVLSLLLLLLD---------LPESDDVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAAG 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 249 NQKIGSLGMDVYENERDLFFEDKSNDVIQDDVFRRLSACHNVLFTGHQAFLTAEALTSISQTTLQNLSNLEKGETCPNEL 328
Cdd:pfam00389 231 GGVIDEAALDALLEEGIAAAADLDVEEEPPPVDSPLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPPANAV 310


                  .
gi 1227727900 329 V 329
Cdd:pfam00389 311 N 311
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
 1-304 1.70e-59

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 193.81  E-value: 1.70e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   1 MKLAVYSTKQYDKKYLQQVNESFGFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSHPVLEELKKHGVKYIALRCAGFN 80
Cdd:PRK08605    2 TKIKIMSVRDEDAPYIKAWAEKHHVEVDLTKEALTDDNVEEVEGFDGLSLSQQIPLSEAIYKLLNELGIKQIAQRSAGFD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  81 NVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLE-GLTGFTMYGKTAGVIGTGKIGVAM 159
Cdd:PRK08605   82 TYDLELATKYNLIISNVPSYSPESIAEFTVTQAINLVRHFNQIQTKVREHDFRWEpPILSRSIKDLKVAVIGTGRIGLAV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 160 LRIL-KGFGMRLLAFDPYPSAAALELgVEYVD-LPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGAL 237
Cdd:PRK08605  162 AKIFaKGYGSDVVAYDPFPNAKAATY-VDYKDtIEEAVEGADIVTLHMPATKYNHYLFNADLFKHFKKGAVFVNCARGSL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1227727900 238 IDSQAAIEALKNQKIGSLGMDVYENERDLFFEDKSNDVIQDDVFRRLSACHNVLFTGHQAFLTAEAL 304
Cdd:PRK08605  241 VDTKALLDALDNGLIKGAALDTYEFERPLFPSDQRGQTINDPLLESLINREDVILTPHIAFYTDAAV 307
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
 60-326 4.47e-58

D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate dehydrogenase, the serA gene of one pathway of serine biosynthesis. Shorter forms, scoring between trusted and noise cutoff, include SerA from E. coli. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273556 [Multi-domain]  Cd Length: 525  Bit Score: 195.23  E-value: 4.47e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  60 VLEELKKhgVKYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTG 139
Cdd:TIGR01327  56 VIAAAPK--LKVIGRAGVGVDNIDIEAATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEGEWDRKAFMG 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 140 FTMYGKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPY-PSAAALELGVEYV-DLPTLFSESDVISLHCPLTPENYHLLNE 217
Cdd:TIGR01327 134 TELYGKTLGVIGLGRIGSIVAKRAKAFGMKVLAYDPYiSPERAEQLGVELVdDLDELLARADFITVHTPLTPETRGLIGA 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 218 AAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENErdlffEDKSNdviqddvfrRLSACHNVLFTGHQA 297
Cdd:TIGR01327 214 EELAKMKKGVIIVNCARGGIIDEAALYEALEEGHVRAAALDVFEKE-----PPTDN---------PLFDLDNVIATPHLG 279

                         250       260
                  ....*....|....*....|....*....
gi 1227727900 298 FLTAEALTSISQTTLQNLSNLEKGETCPN 326
Cdd:TIGR01327 280 ASTREAQENVATQVAEQVLDALKGLPVPN 308
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
133-231 3.15e-03

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 37.81  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  133 SLEGL---TGFTMYGKTAGVIGTGKIG--VAMLriLKGFGMRLLAFDPYPsAAALEL---GVEYVDLPTLFSESDVIslh 204
Cdd:smart00997   9 LLDGIlraTNVLLAGKNVVVAGYGDVGkgVAAR--LRGLGARVIVTEIDP-IRALEAamdGFEVMKMEEAAKRADIF--- 82

                           90       100
                   ....*....|....*....|....*...
gi 1227727900  205 cpLTPE-NYHLLNEAAFDQMKNGVMIVN 231
Cdd:smart00997  83 --VTATgNKDVITREHFRAMKDGAILAN 108
 
Name Accession Description Interval E-value
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 1-328 0e+00

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: 629.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   1 MKLAVYSTKQYDKKYLQQVNESFGFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSHPVLEELKKHGVKYIALRCAGFN 80
Cdd:cd12183     1 MKIAVFSTKPYDREFFEAANEGYGHELTYFEERLTEETASLAKGFDAVCVFVNDDLDAPVLEKLAELGVKLIALRCAGFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  81 NVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGFTMYGKTAGVIGTGKIGVAML 160
Cdd:cd12183    81 NVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKIHRAYNRVREGNFSLDGLLGFDLHGKTVGVIGTGKIGQAFA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 161 RILKGFGMRLLAFDPYPSAAALELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDS 240
Cdd:cd12183   161 RILKGFGCRVLAYDPYPNPELAKLGVEYVDLDELLAESDIISLHCPLTPETHHLINAETIAKMKDGVMLINTSRGGLIDT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 241 QAAIEALKNQKIGSLGMDVYENERDLFFEDKSNDVIQDDVFRRLSACHNVLFTGHQAFLTAEALTSISQTTLQNLSNLEK 320
Cdd:cd12183   241 KALIEALKSGKIGGLGLDVYEEEAGLFFEDHSDEIIQDDVLARLLSFPNVLITGHQAFFTKEALTNIAETTLENLDDFEA 320


                  ....*...
gi 1227727900 321 GETCPNEL 328
Cdd:cd12183   321 GKPLKNEV 328
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
 1-329 3.05e-132

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: 379.05  E-value: 3.05e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   1 MKLAVYSTKQYDKKYLQQVnESFGFELEFFDFLLT-EKTAKTANGCEAVCIFVNDDGSHPVLEELKkhGVKYIALRCAGF 79
Cdd:COG1052     1 KPILVLDPRTLPDEVLERL-EAEHFEVTVYEDETSpEELAERAAGADAVITNGKDPIDAEVLEALP--GLKLIANRGVGY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  80 NNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLE-GLTGFTMYGKTAGVIGTGKIGVA 158
Cdd:COG1052    78 DNIDLAAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSpGLLGRDLSGKTLGIIGLGRIGQA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 159 MLRILKGFGMRLLAFDPYPSAAALELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALI 238
Cdd:COG1052   158 VARRAKGFGMKVLYYDRSPKPEVAELGAEYVSLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARGGLV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 239 DSQAAIEALKNQKIGSLGMDVYENERDlffedksndvIQDDvfrRLSACHNVLFTGHQAFLTAEALTSISQTTLQNLSNL 318
Cdd:COG1052   238 DEAALIEALKSGRIAGAGLDVFEEEPP----------PPDH---PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAF 304

                         330
                  ....*....|.
gi 1227727900 319 EKGETCPNELV 329
Cdd:COG1052   305 LAGEPPPNPVN 315
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 1-324 1.90e-118

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: 344.28  E-value: 1.90e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   1 MKLAVYSTKQYDKKYLQQVNESFGFELEFFDFLLT-EKTAKTANGCEAVCIFVNDDGSHPVLEelKKHGVKYIALRCAGF 79
Cdd:cd01619     1 MKVLIYDYRDDELEIEKEILKAGGVDVEIVTYLLNdDETAELAKGADAILTAFTDKIDAELLD--KAPGLKFISLRATGY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  80 NNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGFTMYGKTAGVIGTGKIGVAM 159
Cdd:cd01619    79 DNIDLDYAKELGIGVTNVPEYSPNAVAEHTIALILALLRNRKYIDERDKNQDLQDAGVIGRELEDQTVGVVGTGKIGRAV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 160 LRILKGFGMRLLAFDPYPSAAALELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALID 239
Cdd:cd01619   159 AQRAKGFGMKVIAYDPFRNPELEDKGVKYVSLEELFKNSDIISLHVPLTPENHHMINEEAFKLMKKGVIIINTARGSLVD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 240 SQAAIEALKNQKIGSLGMDVYENERDLFFEDKSNDVIQDDVFRRLSACHNVLFTGHQAFLTAEALTSISQTTLQNLSNLE 319
Cdd:cd01619   239 TEALIEALDSGKIFGAGLDVLEDETPDLLKDLEGEIFKDALNALLGRRPNVIITPHTAFYTDDALKNMVEISCENIVDFL 318


                  ....*
gi 1227727900 320 KGETC 324
Cdd:cd01619   319 EGEEE 323
HGDH_LDH_like cd12185
Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, ...
 1-324 2.04e-118

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


Pssm-ID: 240661  Cd Length: 322  Bit Score: 344.19  E-value: 2.04e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   1 MKLAVYSTKQYDKKYLQQVNESFGFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSHPVLEELKKHGVKYIALRCAGFN 80
Cdd:cd12185     1 MKIFAYGVRPDELEYFEKFAKEYNVEVTLTKEPLTLENAHLAEGYDGISILGKSKISAELLEKLKEAGVKYISTRSIGYD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  81 NVDLDAAKELGLKVVRVPaYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGFTMYGKTAGVIGTGKIGVAML 160
Cdd:cd12185    81 HIDLDAAKELGIKVSNVT-YSPNSVADYTVMLMLMALRKYKQIMKRAEVNDYSLGGLQGRELRNLTVGVIGTGRIGQAVI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 161 RILKGFGMRLLAFDPYPSAAaLELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDS 240
Cdd:cd12185   160 KNLSGFGCKILAYDPYPNEE-VKKYAEYVDLDTLYKESDIITLHTPLTEETYHLINKESIAKMKDGVIIINTARGELIDT 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 241 QAAIEALKNQKIGSLGMDVYENERDLFFEDKSNDVIQDDVFRRLSACHNVLFTGHQAFLTAEALTSISQTTLQNLSNLEK 320
Cdd:cd12185   239 EALIEGLESGKIGGAALDVIEGEDGIYYNDRKGDILSNRELAILRSFPNVILTPHMAFYTDQAVSDMVENSIESLVAFEK 318


                  ....
gi 1227727900 321 GETC 324
Cdd:cd12185   319 GGEN 322
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
 1-328 1.28e-115

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: 337.20  E-value: 1.28e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   1 MKLAVYSTKQYDKKYLQQVNESFGFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSHPVLEELKKHGVKYIALRCAGFN 80
Cdd:cd12186     1 MKILMYNVRDDEKPYIEEWAKEHPVEVDTTTELLTPETVDLAKGYDGVVVQQTLPYDEEVYEKLAEYGIKQIALRSAGVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  81 NVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLE-GLTGFTMYGKTAGVIGTGKIGVAM 159
Cdd:cd12186    81 MIDLDLAKENGLKITNVPAYSPRAIAEFAVTQALNLLRNTPEIDRRVAKGDFRWApGLIGREIRDLTVGIIGTGRIGSAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 160 LRILKGFGMRLLAFDPYPSAAALELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALID 239
Cdd:cd12186   161 AKIFKGFGAKVIAYDPYPNPELEKFLLYYDSLEDLLKQADIISLHVPLTKENHHLINAEAFAKMKDGAILVNAARGGLVD 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 240 SQAAIEALKNQKIGSLGMDVYENERDLFFEDKSNDVIQDDVFRRLSACHNVLFTGHQAFLTAEALTSISQTTLQNLSNLE 319
Cdd:cd12186   241 TKALIDALDSGKIAGAALDTYENETGYFNKDWSGKEIEDEVLKELIAMPNVLITPHIAFYTDTAVKNMVEISLDDALEII 320


                  ....*....
gi 1227727900 320 KGETCPNEL 328
Cdd:cd12186   321 EGGTSENEV 329
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
 2-315 6.24e-103

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: 304.97  E-value: 6.24e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   2 KLAVYSTKQYDKKYLQQVneSFGFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSHPVLEELKKhgVKYIALRCAGFNN 81
Cdd:cd12187     1 KIVFFETEEWEQEYFQEL--LPGHKVVFTSQELLDDNVEEFKDAEVISVFVYSRLDAEVLEKLPR--LKLIATRSTGFDH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  82 VDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGFTMYGKTAGVIGTGKIGVAMLR 161
Cdd:cd12187    77 IDLEACRERGIAVCNVPDYGEATVAEHAFALLLALSRKLREAIERTRRGDFSQAGLRGFELAGKTLGVVGTGRIGRRVAR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 162 ILKGFGMRLLAFDPYPSAAALE-LGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDS 240
Cdd:cd12187   157 IARGFGMKVLAYDVVPDEELAErLGFRYVSLEELLQESDIISLHVPYTPQTHHLINRENFALMKPGAVLINTARGAVVDT 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 241 QAAIEALKNQKIGSLGMDVYENERDLFFEDKS-NDVIQDDVFRRLSACH------NVLFTGHQAFLTAEALTSISQTTLQ 313
Cdd:cd12187   237 EALVRALKEGKLAGAGLDVLEQEEVLREEAELfREDVSPEDLKKLLADHallrkpNVIITPHVAYNTKEALERILDTTVE 316


                  ..
gi 1227727900 314 NL 315
Cdd:cd12187   317 NI 318
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
 9-329 7.99e-103

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: 304.21  E-value: 7.99e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   9 KQYDKKYLQQvnesfgFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSHPVLEELKKhgVKYIALRCAGFNNVDLDAAK 88
Cdd:pfam00389   8 SPEALELLKE------GEVEVHDELLTEELLEKAKDADALIVRSRTKVTAEVLEAAPK--LKVIGRAGVGVDNVDLDAAT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  89 ELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGFTMYGKTAGVIGTGKIGVAMLRILKGFGM 168
Cdd:pfam00389  80 ERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLELYGKTLGVIGGGGIGGGVAAIAKAFGM 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 169 RLLAFDPYPSAAALELGVEYVDLPTLFSESdvislhcplTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALK 248
Cdd:pfam00389 160 GVVAYDPYPNPERAEAGGVEVLSLLLLLLD---------LPESDDVLTVNPLTTMKTGVIIINEARGMLKDAVAIINAAG 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 249 NQKIGSLGMDVYENERDLFFEDKSNDVIQDDVFRRLSACHNVLFTGHQAFLTAEALTSISQTTLQNLSNLEKGETCPNEL 328
Cdd:pfam00389 231 GGVIDEAALDALLEEGIAAAADLDVEEEPPPVDSPLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPPANAV 310


                  .
gi 1227727900 329 V 329
Cdd:pfam00389 311 N 311
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
 1-328 1.95e-93

(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: 280.72  E-value: 1.95e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   1 MKLAVYSTKQYDKKYLQQVNESFGFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSHPVLEELKKHGVKYIALRCAGFN 80
Cdd:cd12184     1 MKIICYGVRPVEKPIFEKLNKKFGYDLTLVEEYLNDENVHLAKGHDAVIVRGNCFADKENLEIYKEYGIKYVFTRTVGFN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  81 NVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLtgftMYGK-----TAGVIGTGKI 155
Cdd:cd12184    81 HIDLEAAKELGFKMARVPSYSPNAIAELAFTLAMTLSRHTAYTASRTANKNFKVDPF----MFSKeirnsTVGIIGTGRI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 156 GVAMLRILKGFGMRLLAFDPYPSAAALELgVEYVDLPTLFSESDVISLHCPLTP-ENYHLLNEAAFDQMKNGVMIVNTSR 234
Cdd:cd12184   157 GLTAAKLFKGLGAKVIGYDIYPSDAAKDV-VTFVSLDELLKKSDIISLHVPYIKgKNDKLINKEFISKMKDGAILINTAR 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 235 GALIDSQAAIEALKNQKIGSLGMDVYENERDLFFEDKSNDVIQDDVFRRL-SACHNVLFTGHQAFLTAEALTSISQTTLQ 313
Cdd:cd12184   236 GELQDEEAILEALESGKLAGFGTDVLNNEKEIFFKDFDGDKIEDPVVEKLlDLYPRVLLTPHIGSYTDEALSNMIETSYE 315

                         330
                  ....*....|....*
gi 1227727900 314 NLSNLEKGETCPNEL 328
Cdd:cd12184   316 NLKEYLETGDCKNKI 330
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
 1-328 2.63e-90

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: 272.45  E-value: 2.63e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   1 MKLAVysTKQYDKKYLQQVNESFGFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSHPVLEELKKhgVKYIALRCAGFN 80
Cdd:COG0111     1 MKILI--LDDLPPEALEALEAAPGIEVVYAPGLDEEELAEALADADALIVRSRTKVTAELLAAAPN--LKLIGRAGAGVD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  81 NVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGFTMYGKTAGVIGTGKIGVAML 160
Cdd:COG0111    77 NIDLAAATERGIPVTNAPGANARAVAEYALALLLALARRLPEADRAQRAGRWDRSAFRGRELRGKTVGIVGLGRIGRAVA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 161 RILKGFGMRLLAFDPYPSAA-ALELGVEYV-DLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALI 238
Cdd:COG0111   157 RRLRAFGMRVLAYDPSPKPEeAADLGVGLVdSLDELLAEADVVSLHLPLTPETRGLIGAEELAAMKPGAILINTARGGVV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 239 DSQAAIEALKNQKIGSLGMDVYENErdlffedksnDVIQDDVFRRLSachNVLFTGHQAFLTAEALTSISQTTLQNLSNL 318
Cdd:COG0111   237 DEDALLAALDSGRLAGAALDVFEPE----------PLPADSPLWDLP---NVILTPHIAGSTEEAQERAARQVAENIRRF 303

                         330
                  ....*....|
gi 1227727900 319 EKGETCPNEL 328
Cdd:COG0111   304 LAGEPLRNLV 313
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
 2-315 1.26e-89

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: 270.27  E-value: 1.26e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   2 KLAVYSTkqYDKKYLQQVNESFGFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSHPVLEELKKhgVKYIALRCAGFNN 81
Cdd:cd05198     1 KVLVLEP--LFPPEALEALEATGFEVIVADDLLADELEALLADADALIVSSTTPVTAEVLAKAPK--LKFIQVAGAGVDN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  82 VDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSL-EGLTGFTMYGKTAGVIGTGKIGVAML 160
Cdd:cd05198    77 IDLDAAKKRGITVTNVPGANAEAVAEHALGLLLALLRRLPRADAAVRRGWGWLwAGFPGYELEGKTVGIVGLGRIGQRVA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 161 RILKGFGMRLLAFDPYPSAAALE-LGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALID 239
Cdd:cd05198   157 KRLQAFGMKVLYYDRTRKPEPEEdLGFRVVSLDELLAQSDVVVLHLPLTPETRHLINEEELALMKPGAVLVNTARGGLVD 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1227727900 240 SQAAIEALKNQKIGSLGMDVYENERDLFfedkSNDVIQDDvfrrlsachNVLFTGHQAFLTAEALTSISQTTLQNL 315
Cdd:cd05198   237 EDALLRALKSGKIAGAALDVFEPEPLPA----DHPLLELP---------NVILTPHIAGYTEEARERMAEIAVENL 299
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 6-315 2.53e-88

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: 267.05  E-value: 2.53e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   6 YSTKQYDKKYLQQVnESFGFELEFFDF--LLTEKT-AKTANGCEAVcIFVNDDGSHPVLEELK------KHGVkyialrc 76
Cdd:cd12172     7 RSFSKYSEEAKELL-EAAGFEVVLNPLgrPLTEEElIELLKDADGV-IAGLDPITEEVLAAAPrlkvisRYGV------- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  77 aGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSleGLTGFTMYGKTAGVIGTGKIG 156
Cdd:cd12172    78 -GYDNIDLEAAKKRGIVVTNTPGANSNSVAELTIGLMLALARQIPQADREVRAGGWD--RPVGTELYGKTLGIIGLGRIG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 157 VAMLRILKGFGMRLLAFDPYP-SAAALELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRG 235
Cdd:cd12172   155 KAVARRLSGFGMKVLAYDPYPdEEFAKEHGVEFVSLEELLKESDFISLHLPLTPETRHLINAAELALMKPGAILINTARG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 236 ALIDSQAAIEALKNQKIGSLGMDVYENERdlffedksndviqDDVFRRLSACHNVLFTGHQAFLTAEALTSISQTTLQNL 315
Cdd:cd12172   235 GLVDEEALYEALKSGRIAGAALDVFEEEP-------------PPADSPLLELPNVILTPHIGASTKEAVLRMGTMAAQNV 301
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 77-324 7.08e-80

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: 245.56  E-value: 7.08e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  77 AGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDAN-FSLEGLTGFTMYGKTAGVIGTGKI 155
Cdd:cd12175    74 VGLDGVDLEAATARGIPVANIPGGNAESVAEHAVMLMLALLRRLPEADRELRAGRwGRPEGRPSRELSGKTVGIVGLGNI 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 156 GVAMLRILKGFGMRLLAFDPYPSAAA--LELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTS 233
Cdd:cd12175   154 GRAVARRLRGFGVEVIYYDRFRDPEAeeKDLGVRYVELDELLAESDVVSLHVPLTPETRHLIGAEELAAMKPGAILINTA 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 234 RGALIDSQAAIEALKNQKIGSLGMDVYENErdlffedksnDVIQDDVFRRLsacHNVLFTGHQAFLTAEALTSISQTTLQ 313
Cdd:cd12175   234 RGGLVDEEALLAALRSGHLAGAGLDVFWQE----------PLPPDDPLLRL---DNVILTPHIAGVTDESYQRMAAIVAE 300

                         250
                  ....*....|.
gi 1227727900 314 NLSNLEKGETC 324
Cdd:cd12175   301 NIARLLRGEPP 311
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
 66-322 1.45e-77

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: 239.24  E-value: 1.45e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  66 KHGVkyialrcaGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGFTMYGK 145
Cdd:cd12173    68 RAGV--------GVDNIDVEAATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGKWDRKKFMGVELRGK 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 146 TAGVIGTGKIGVAMLRILKGFGMRLLAFDPYPSAA-ALELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMK 224
Cdd:cd12173   140 TLGIVGLGRIGREVARRARAFGMKVLAYDPYISAErAAAGGVELVSLDELLAEADFISLHTPLTPETRGLINAEELAKMK 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 225 NGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENErdlffedksnDVIQDDVFRRLSachNVLFTGHQAFLTAEAL 304
Cdd:cd12173   220 PGAILINTARGGIVDEAALADALKSGKIAGAALDVFEQE----------PPPADSPLLGLP---NVILTPHLGASTEEAQ 286

                         250
                  ....*....|....*...
gi 1227727900 305 TSISQTTLQNLSNLEKGE 322
Cdd:cd12173   287 ERVAVDAAEQVLAVLAGE 304
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
 1-326 1.74e-76

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: 237.03  E-value: 1.74e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   1 MKLAVYSTKQYDKKYLQQVNESFGFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGShPVLEELKKHGVkyIALRCAGFN 80
Cdd:cd05299     1 PKVVITDYDFPDLDIEREVLEEAGVELVDAQSRTEDELIEAAADADALLVQYAPVTA-EVIEALPRLKV--IVRYGVGVD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  81 NVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGftMY---GKTAGVIGTGKIGV 157
Cdd:cd05299    78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTVGGP--IRrlrGLTLGLVGFGRIGR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 158 AMLRILKGFGMRLLAFDPYPSAAALEL-GVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGA 236
Cdd:cd05299   156 AVAKRAKAFGFRVIAYDPYVPDGVAALgGVRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVNTARGG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 237 LIDSQAAIEALKNQKIGSLGMDVYENErdlffedksnDVIQDDVFRRLSachNVLFTGHQAFLTAEALTSISQTTLQNLS 316
Cdd:cd05299   236 LVDEAALARALKSGRIAGAALDVLEEE----------PPPADSPLLSAP---NVILTPHAAWYSEESLAELRRKAAEEVV 302

                         330
                  ....*....|
gi 1227727900 317 NLEKGETCPN 326
Cdd:cd05299   303 RVLRGEPPRN 312
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 21-317 2.13e-73

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: 228.88  E-value: 2.13e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  21 ESFGfELEFFDFLLTEKTAKTANGCEAVciFVND---DGSHpvLEELKKhgVKYIALRCAGFNNVDLDAAKELGLKVVRV 97
Cdd:cd12162    22 EFLG-ELTVYDRTSPEEVVERIKDADIV--ITNKvvlDAEV--LAQLPN--LKLIGVLATGYNNVDLAAAKERGITVTNV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  98 PAYDPEAVAEHAIGMMMTLNRRI--HRAYQR----TRDANFSLeglTGFTMY---GKTAGVIGTGKIGVAMLRILKGFGM 168
Cdd:cd12162    95 PGYSTDSVAQHTFALLLALARLVayHNDVVKagewQKSPDFCF---WDYPIIelaGKTLGIIGYGNIGQAVARIARAFGM 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 169 RLLAFDPYPSAaalELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALK 248
Cdd:cd12162   172 KVLFAERKGAP---PLREGYVSLDELLAQSDVISLHCPLTPETRNLINAEELAKMKPGAILINTARGGLVDEQALADALN 248

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1227727900 249 NQKIGSLGMDVYENE--RDlffedksndviqDDVFrrLSACHNVLFTGHQAFLTAEALTSISQTTLQNLSN 317
Cdd:cd12162   249 SGKIAGAGLDVLSQEppRA------------DNPL--LKAAPNLIITPHIAWASREARQRLMDILVDNIKA 305
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
 24-263 6.93e-70

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: 219.96  E-value: 6.93e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  24 GFELEFFD---FLLTEKTAKTANGCEAVCIFVNDDGSHPVLEELKKhgVKYIALRCAGFNNVDLDAAKELGLKVvrvpAY 100
Cdd:cd05301    20 GFEVEVWDedrPLPREELLEAAKGADGLLCTLTDKIDAELLDAAPP--LKVIANYSVGYDHIDVDAAKARGIPV----TN 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 101 DP----EAVAEHAIGMMMTLNRRIHRAYQRTRDANF---SLEGLTGFTMYGKTAGVIGTGKIGVAMLRILKGFGMRLLAF 173
Cdd:cd05301    94 TPdvltDATADLAFALLLAAARRVVEGDRFVRAGEWkgwSPTLLLGTDLHGKTLGIVGMGRIGQAVARRAKGFGMKILYH 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 174 DPYPSAAALE-LGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKI 252
Cdd:cd05301   174 NRSRKPEAEEeLGARYVSLDELLAESDFVSLHCPLTPETRHLINAERLALMKPTAILINTARGGVVDEDALVEALKSGKI 253

                         250
                  ....*....|.
gi 1227727900 253 GSLGMDVYENE 263
Cdd:cd05301   254 AGAGLDVFEPE 264
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 68-322 3.63e-68

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: 216.03  E-value: 3.63e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  68 GVKYIALRCAGFNNVDLDAAKELGLKVVRVP-AYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEG-LTGFTMYGK 145
Cdd:cd12177    69 GLKLIARHGIGYDNVDLKAATEHGVIVTRVPgAVERDAVAEHAVALILTVLRKINQASEAVKEGKWTERAnFVGHELSGK 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 146 TAGVIGTGKIGVAMLRILK-GFGMRLLAFDPYPSAAALE-LGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQM 223
Cdd:cd12177   149 TVGIIGYGNIGSRVAEILKeGFNAKVLAYDPYVSEEVIKkKGAKPVSLEELLAESDIISLHAPLTEETYHMINEKAFSKM 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 224 KNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENERdlffEDKSNDVIQDDvfrrlsachNVLFTGHQAFLTAEA 303
Cdd:cd12177   229 KKGVILVNTARGELIDEEALIEALKSGKIAGAGLDVLEEEP----IKADHPLLHYE---------NVVITPHIGAYTYES 295

                         250
                  ....*....|....*....
gi 1227727900 304 LTSISQTTLQNLSNLEKGE 322
Cdd:cd12177   296 LYGMGEKVVDDIEDFLAGK 314
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 57-323 2.88e-66

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: 210.94  E-value: 2.88e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  57 SHPVLEELKKHGV--KYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSL 134
Cdd:cd12178    52 STPVDKEIIDAAKnlKIIANYGAGFDNIDVDYAKEKGIPVTNTPAVSTEPTAELTFGLILALARRIAEGDRLMRRGGFLG 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 135 EGLT---GFTMYGKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPY--PSAAALELGVEYVDLPTLFSESDVISLHCPLTP 209
Cdd:cd12178   132 WAPLfflGHELAGKTLGIIGMGRIGQAVARRAKAFGMKILYYNRHrlSEETEKELGATYVDLDELLKESDFVSLHAPYTP 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 210 ENYHLLNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENErdlffedksndviqDDVFRRLSACHN 289
Cdd:cd12178   212 ETHHLIDAAAFKLMKPTAYLINAARGPLVDEKALVDALKTGEIAGAALDVFEFE--------------PEVSPELKKLDN 277

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1227727900 290 VLFTGHQAFLTAEALTSISQTTLQNLSNLEKGET 323
Cdd:cd12178   278 VILTPHIGNATVEARDAMAKEAADNIISFLEGKR 311
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 25-305 3.63e-66

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: 210.47  E-value: 3.63e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  25 FELEFFDFLLTEKTAKTANGCEA----------VCIFVNDDGSHPVLEELKKhgVKYIA-LRcAGFNNVDLDAAKELGLK 93
Cdd:cd12171    16 FEDLQEVILVVEKSGPEAVEPEEellealkdadILITHFAPVTKKVIEAAPK--LKLIGvCR-GGPENVDVEAATERGIP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  94 VVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRD----ANFSLEGLTGFTMYGKTAGVIGTGKIGVAMLRILKGFGMR 169
Cdd:cd12171    93 VLNTPGRNAEAVAEFTVGLMLAETRNIARAHAALKDgewrKDYYNYDGYGPELRGKTVGIVGFGAIGRRVAKRLKAFGAE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 170 LLAFDPYPSAAALE-LGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALK 248
Cdd:cd12171   173 VLVYDPYVDPEKIEaDGVKKVSLEELLKRSDVVSLHARLTPETRGMIGAEEFALMKPTAYFINTARAGLVDEDALIEALE 252

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1227727900 249 NQKIGSLGMDVYENErdlffedksnDVIQDDVFRRLSachNVLFTGHQAFLTAEALT 305
Cdd:cd12171   253 EGKIGGAALDVFPEE----------PLPADHPLLKLD---NVTLTPHIAGATRDVAE 296
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
 70-263 8.94e-66

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: 208.93  E-value: 8.94e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  70 KYIAlRCA-GFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGFTMYGKTAG 148
Cdd:cd05303    65 KIIA-RAGvGLDNIDVEYAKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHRANREMKLGKWNKKKYKGIELRGKTLG 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 149 VIGTGKIGVAMLRILKGFGMRLLAFDPYP-SAAALELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGV 227
Cdd:cd05303   144 IIGFGRIGREVAKIARALGMNVIAYDPYPkDEQAVELGVKTVSLEELLKNSDFISLHVPLTPETKHMINKKELELMKDGA 223

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1227727900 228 MIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENE 263
Cdd:cd05303   224 IIINTSRGGVIDEEALLEALKSGKLAGAALDVFENE 259
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
 24-315 2.02e-65

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: 208.61  E-value: 2.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  24 GFELEFFDFLLT--EKTAKTANGCEAVCIfvnddGSHP----VLEELKKhgVKYIALRCAGFNNVDLDAAKELGLKVVRV 97
Cdd:cd12161    26 GHEFVYYDTKTTdtAELIERSKDADIVMI-----ANMPlpgeVIEACKN--LKMISVAFTGVDHVDLEACKERGITVSNA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  98 PAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSlEGLTGFTMYGKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPYP 177
Cdd:cd12161    99 AGYSTEAVAELTIGLAIDLLRNIVPCDAAVRAGGTK-AGLIGRELAGKTVGIVGTGAIGLRVARLFKAFGCKVLAYSRSE 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 178 SAAALELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGM 257
Cdd:cd12161   178 KEEAKALGIEYVSLDELLAESDIVSLHLPLNDETKGLIGKEKLALMKESAILINTARGPVVDNEALADALNEGKIAGAGI 257

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1227727900 258 DVYENERDLffedksndviqdDVFRRLSACHNVLFTGHQAFLTAEALTSISQTTLQNL 315
Cdd:cd12161   258 DVFDMEPPL------------PADYPLLHAPNTILTPHVAFATEEAMEKRAEIVFDNI 303
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 110-297 5.78e-65

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: 202.73  E-value: 5.78e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 110 IGMMMTLNRRIHRAYQRTRDANFSLE-GLTGFTMYGKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPYPSA--AALELGV 186
Cdd:pfam02826   1 LALLLALARRIPEADRQVRAGRWASPdALLGRELSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPeeEEEELGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 187 EYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENErdl 266
Cdd:pfam02826  81 RYVSLDELLAESDVVSLHLPLTPETRHLINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDVFEPE--- 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1227727900 267 ffedksnDVIQDDvfrRLSACHNVLFTGHQA 297
Cdd:pfam02826 158 -------PLPADH---PLLDLPNVILTPHIA 178
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
 1-304 1.70e-59

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 193.81  E-value: 1.70e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   1 MKLAVYSTKQYDKKYLQQVNESFGFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSHPVLEELKKHGVKYIALRCAGFN 80
Cdd:PRK08605    2 TKIKIMSVRDEDAPYIKAWAEKHHVEVDLTKEALTDDNVEEVEGFDGLSLSQQIPLSEAIYKLLNELGIKQIAQRSAGFD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  81 NVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLE-GLTGFTMYGKTAGVIGTGKIGVAM 159
Cdd:PRK08605   82 TYDLELATKYNLIISNVPSYSPESIAEFTVTQAINLVRHFNQIQTKVREHDFRWEpPILSRSIKDLKVAVIGTGRIGLAV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 160 LRIL-KGFGMRLLAFDPYPSAAALELgVEYVD-LPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGAL 237
Cdd:PRK08605  162 AKIFaKGYGSDVVAYDPFPNAKAATY-VDYKDtIEEAVEGADIVTLHMPATKYNHYLFNADLFKHFKKGAVFVNCARGSL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1227727900 238 IDSQAAIEALKNQKIGSLGMDVYENERDLFFEDKSNDVIQDDVFRRLSACHNVLFTGHQAFLTAEAL 304
Cdd:PRK08605  241 VDTKALLDALDNGLIKGAALDTYEFERPLFPSDQRGQTINDPLLESLINREDVILTPHIAFYTDAAV 307
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
 60-326 4.47e-58

D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate dehydrogenase, the serA gene of one pathway of serine biosynthesis. Shorter forms, scoring between trusted and noise cutoff, include SerA from E. coli. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273556 [Multi-domain]  Cd Length: 525  Bit Score: 195.23  E-value: 4.47e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  60 VLEELKKhgVKYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTG 139
Cdd:TIGR01327  56 VIAAAPK--LKVIGRAGVGVDNIDIEAATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEGEWDRKAFMG 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 140 FTMYGKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPY-PSAAALELGVEYV-DLPTLFSESDVISLHCPLTPENYHLLNE 217
Cdd:TIGR01327 134 TELYGKTLGVIGLGRIGSIVAKRAKAFGMKVLAYDPYiSPERAEQLGVELVdDLDELLARADFITVHTPLTPETRGLIGA 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 218 AAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENErdlffEDKSNdviqddvfrRLSACHNVLFTGHQA 297
Cdd:TIGR01327 214 EELAKMKKGVIIVNCARGGIIDEAALYEALEEGHVRAAALDVFEKE-----PPTDN---------PLFDLDNVIATPHLG 279

                         250       260
                  ....*....|....*....|....*....
gi 1227727900 298 FLTAEALTSISQTTLQNLSNLEKGETCPN 326
Cdd:TIGR01327 280 ASTREAQENVATQVAEQVLDALKGLPVPN 308
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
 2-328 1.18e-57

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 189.35  E-value: 1.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   2 KLAVYSTKQYDKKYLQQVNESFGFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSHPVLEELKKHGVKYIALRCAGFNN 81
Cdd:PRK12480    3 KIMFFGTRDYEKEMALNWGKKNNVEVTTSKELLSSATVDQLKDYDGVTTMQFGKLENDVYPKLESYGIKQIAQRTAGFDM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  82 VDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEG-LTGFTMYGKTAGVIGTGKIGVAML 160
Cdd:PRK12480   83 YDLDLAKKHNIVISNVPSYSPETIAEYSVSIALQLVRRFPDIERRVQAHDFTWQAeIMSKPVKNMTVAIIGTGRIGAATA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 161 RILKGFGMRLLAFDPYPSAAaLELgVEYVD-LPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALID 239
Cdd:PRK12480  163 KIYAGFGATITAYDAYPNKD-LDF-LTYKDsVKEAIKDADIISLHVPANKESYHLFDKAMFDHVKKGAILVNAARGAVIN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 240 SQAAIEALKNQKIGSLGMDVYENERDLFFEDKSNDVIQDDVFRRLSACHNVLFTGHQAFLTAEALTSISQTTLQNLSNLE 319
Cdd:PRK12480  241 TPDLIAAVNDGTLLGAAIDTYENEAAYFTNDWTNKDIDDKTLLELIEHERILVTPHIAFFSDEAVQNLVEGGLNAALSVI 320


                  ....*....
gi 1227727900 320 KGETCPNEL 328
Cdd:PRK12480  321 NTGTCETRL 329
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
 42-321 1.16e-55

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: 183.64  E-value: 1.16e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  42 ANGCEAVCIFVNDDGSHPVLEELKKhgVKYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIH 121
Cdd:cd12157    42 CKDADGLMAFMPDRIDADFLDACPR--LKIIACALKGYDNFDVEACTARGIWVTIVPDLLTEPTAELTIGLLIGLGRHIL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 122 RA--YQRTRDANFSLEGLTGFTMYGKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPYP--SAAALELGVEYVDLPTLFSE 197
Cdd:cd12157   120 AGdrFVRSGKFGGWRPKFYGTGLDGKTVGILGMGALGRAIARRLSGFGATLLYYDPHPldQAEEQALNLRRVELDELLES 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 198 SDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENErDLFFEDKSNDVIQ 277
Cdd:cd12157   200 SDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRGSVVDEAAVAEALKSGHLGGYAADVFEME-DWARPDRPRSIPQ 278

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1227727900 278 DdvfrRLSACHNVLFTGHQAFLTAEALTSISQTTLQNLSNLEKG 321
Cdd:cd12157   279 E----LLDQHDRTVFTPHIGSAVDEVRLEIELEAALNILQALQG 318
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
 62-322 1.48e-55

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: 183.52  E-value: 1.48e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  62 EELKKH---GVKYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFS--LEG 136
Cdd:cd12168    67 EELISPlppSLKIIAHAGAGYDQIDVDALTKRGIQVSNTPGAVDEATADTALFLILGALRNFSRAERSARAGKWRgfLDL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 137 LTGFTMYGKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPYPSAAALE--LGVEYVDLPTLFSESDVISLHCPLTPENYHL 214
Cdd:cd12168   147 TLAHDPRGKTLGILGLGGIGKAIARKAAAFGMKIIYHNRSRLPEELEkaLATYYVSLDELLAQSDVVSLNCPLTAATRHL 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 215 LNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENErdlffedksndviqDDVFRRLSACHNVLFTG 294
Cdd:cd12168   227 INKKEFAKMKDGVIIVNTARGAVIDEDALVDALESGKVASAGLDVFENE--------------PEVNPGLLKMPNVTLLP 292

                         250       260
                  ....*....|....*....|....*....
gi 1227727900 295 HQAFLTAEALTSISQTTLQNLSN-LEKGE 322
Cdd:cd12168   293 HMGTLTVETQEKMEELVLENIEAfLETGK 321
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
 60-315 5.72e-55

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: 181.56  E-value: 5.72e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  60 VLEELKKhgVKYIALRCAGFNNVDLDAAKELGLkVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSleGLTG 139
Cdd:cd12169    63 LLERLPN--LKLLVTTGMRNASIDLAAAKERGI-VVCGTGGGPTATAELTWALILALARNLPEEDAALRAGGWQ--TTLG 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 140 FTMYGKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPYPSAA-ALELGVEY-VDLPTLFSESDVISLHCPLTPENYHLLNE 217
Cdd:cd12169   138 TGLAGKTLGIVGLGRIGARVARIGQAFGMRVIAWSSNLTAErAAAAGVEAaVSKEELFATSDVVSLHLVLSDRTRGLVGA 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 218 AAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENErdlffedksnDVIQDDVFRRLSachNVLFTGHQA 297
Cdd:cd12169   218 EDLALMKPTALLVNTSRGPLVDEGALLAALRAGRIAGAALDVFDVE----------PLPADHPLRGLP---NVLLTPHIG 284

                         250
                  ....*....|....*...
gi 1227727900 298 FLTAEALTSISQTTLQNL 315
Cdd:cd12169   285 YVTEEAYEGFYGQAVENI 302
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 68-323 7.90e-55

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: 180.83  E-value: 7.90e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  68 GVKYIAlRC-AGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQ---RTRDANFSLEGLTGFTMY 143
Cdd:cd12174    50 SLKAIA-RAgAGVNNIDVDAASKRGIVVFNTPGANANAVAELVIAMMLALSRNIIQAIKwvtNGDGDDISKGVEKGKKQF 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 144 ------GKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPYPS---AAALELGVEYV-DLPTLFSESDVISLHCPLTPENYH 213
Cdd:cd12174   129 vgtelrGKTLGVIGLGNIGRLVANAALALGMKVIGYDPYLSveaAWKLSVEVQRVtSLEELLATADYITLHVPLTDETRG 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 214 LLNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSlGMDVYENERDLFFEDksndviqddvfrrlsachNVLFT 293
Cdd:cd12174   209 LINAELLAKMKPGAILLNFARGEIVDEEALLEALDEGKLGG-YVTDFPEPALLGHLP------------------NVIAT 269

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1227727900 294 GHQAFLTAEALTSISQTTLQNLSN-LEKGET 323
Cdd:cd12174   270 PHLGASTEEAEENCAVMAARQIMDfLETGNI 300
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 70-310 3.28e-54

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: 179.41  E-value: 3.28e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  70 KYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGFTMYGKTAGV 149
Cdd:cd12179    64 KFIARAGAGLENIDLEYAKEKGIELFNAPEGNRDAVGEHALGMLLALFNKLNRADQEVRNGIWDREGNRGVELMGKTVGI 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 150 IGTGKIGVAMLRILKGFGMRLLAFDPYPSAAalELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMI 229
Cdd:cd12179   144 IGYGNMGKAFAKRLSGFGCKVIAYDKYKNFG--DAYAEQVSLETLFKEADILSLHIPLTPETRGMVNKEFISSFKKPFYF 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 230 VNTSRGALIDSQAAIEALKNQKIGSLGMDVYENERDLFFEDKSndviQDDVFRRLSACHNVLFTGHQAFLTAEALTSISQ 309
Cdd:cd12179   222 INTARGKVVVTKDLVKALKSGKILGACLDVLEYEKASFESIFN----QPEAFEYLIKSPKVILTPHIAGWTFESYEKIAE 297


                  .
gi 1227727900 310 T 310
Cdd:cd12179   298 V 298
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 68-322 9.58e-53

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: 176.21  E-value: 9.58e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  68 GVKYIAlRCAG--FNNVDlDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHR---AYQRTRDANFSlEGLTGFTM 142
Cdd:cd12167    72 RLRAVV-HAAGsvRGLVT-DAVWERGILVTSAADANAEPVAEFTLAAILLALRRIPRfaaAYRAGRDWGWP-TRRGGRGL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 143 YGKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPYPSAAALE-LGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFD 221
Cdd:cd12167   149 YGRTVGIVGFGRIGRAVVELLRPFGLRVLVYDPYLPAAEAAaLGVELVSLDELLARSDVVSLHAPLTPETRGMIDARLLA 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 222 QMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLgMDVYENErdlffedksnDVIQDDVFRRLSachNVLFTGHQAFLTA 301
Cdd:cd12167   229 LMRDGATFINTARGALVDEAALLAELRSGRLRAA-LDVTDPE----------PLPPDSPLRTLP---NVLLTPHIAGSTG 294

                         250       260
                  ....*....|....*....|.
gi 1227727900 302 EALTSISQTTLQNLSNLEKGE 322
Cdd:cd12167   295 DERRRLGDYALDELERFLAGE 315
PRK13243 PRK13243
glyoxylate reductase; Reviewed
 1-326 8.50e-50

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 168.82  E-value: 8.50e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   1 MKLAVYSTKQYDKKYLQQVNESFGFEL-EFFDFLLTEKTAKTANGCEAVCIFVNDDGSHPVLEELKKhgVKYIALRCAGF 79
Cdd:PRK13243    1 MKPKVFITREIPENGIEMLEEHFEVEVwEDEREIPREVLLEKVRDVDALVTMLSERIDCEVFEAAPR--LRIVANYAVGY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  80 NNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLT-------GFTMYGKTAGVIGT 152
Cdd:PRK13243   79 DNIDVEEATRRGIYVTNTPGVLTEATADFAWALLLATARRLVEADHFVRSGEWKRRGVAwhplmflGYDVYGKTIGIIGF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 153 GKIGVAMLRILKGFGMRLLAFD-PYPSAAALELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVN 231
Cdd:PRK13243  159 GRIGQAVARRAKGFGMRILYYSrTRKPEAEKELGAEYRPLEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAILVN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 232 TSRGALIDSQAAIEALKNQKIGSLGMDVYEnerdlffEDKSNDviqddvfRRLSACHNVLFTGHQAFLTAEALTSISQTT 311
Cdd:PRK13243  239 TARGKVVDTKALVKALKEGWIAGAGLDVFE-------EEPYYN-------EELFSLKNVVLAPHIGSATFEAREGMAELV 304

                         330
                  ....*....|....*
gi 1227727900 312 LQNLSNLEKGETCPN 326
Cdd:PRK13243  305 AENLIAFKRGEVPPT 319
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 77-327 1.57e-47

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: 162.41  E-value: 1.57e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  77 AGFNNVDLDAAKElGLKVVRVPAYDPeAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGF---TMYGKTAGVIGTG 153
Cdd:cd12165    69 AGVDHLPLERLPE-GVVVANNHGNSP-AVAEHALALILALAKRIVEYDNDLRRGIWHGRAGEEPeskELRGKTVGILGYG 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 154 KIGVAMLRILKGFGMRLLAFDPYPSAAALELGVEYV-DLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNT 232
Cdd:cd12165   147 HIGREIARLLKAFGMRVIGVSRSPKEDEGADFVGTLsDLDEALEQADVVVVALPLTKQTRGLIGAAELAAMKPGAILVNV 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 233 SRGALIDSQAAIEALKNQKIGSLGMDVYENERdlffEDKSNDVIQDDVFRRLsacHNVLFTGHQAFLTAEALTSISQTTL 312
Cdd:cd12165   227 GRGPVVDEEALYEALKERPIAGAAIDVWWRYP----SRGDPVAPSRYPFHEL---PNVIMSPHNAGWTEETFRRRIDEAA 299

                         250
                  ....*....|....*
gi 1227727900 313 QNLSNLEKGETCPNE 327
Cdd:cd12165   300 ENIRRYLRGEPLLNL 314
PRK06932 PRK06932
2-hydroxyacid dehydrogenase;
60-315 1.81e-43

2-hydroxyacid dehydrogenase;


Pssm-ID: 235890 [Multi-domain]  Cd Length: 314  Bit Score: 151.88  E-value: 1.81e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  60 VLEELKKhgVKYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTG 139
Cdd:PRK06932   59 TLAQLPK--LKLIAITATGTNNVDLVAAKELGIAVKNVTGYSSTTVPEHVLGMIFALKHSLMGWYRDQLSDRWATCKQFC 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 140 FTMY------GKTAGVIGTGKIGVAMLRILKGFGMRLLaFDPYPSAAALELGveYVDLPTLFSESDVISLHCPLTPENYH 213
Cdd:PRK06932  137 YFDYpitdvrGSTLGVFGKGCLGTEVGRLAQALGMKVL-YAEHKGASVCREG--YTPFEEVLKQADIVTLHCPLTETTQN 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 214 LLNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENERdlffEDKSNDVIQddVFRRLSachNVLFT 293
Cdd:PRK06932  214 LINAETLALMKPTAFLINTGRGPLVDEQALLDALENGKIAGAALDVLVKEP----PEKDNPLIQ--AAKRLP---NLLIT 284

                         250       260
                  ....*....|....*....|..
gi 1227727900 294 GHQAFLTAEALTSISQTTLQNL 315
Cdd:PRK06932  285 PHIAWASDSAVTTLVNKVAQNI 306
PRK07574 PRK07574
NAD-dependent formate dehydrogenase;
78-260 1.12e-41

NAD-dependent formate dehydrogenase;


Pssm-ID: 181041  Cd Length: 385  Bit Score: 149.05  E-value: 1.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  78 GFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDA--NFSLEGLTGFTMYGKTAGVIGTGKI 155
Cdd:PRK07574  124 GSDHVDLQAASEHGITVAEVTGSNSISVAEHVVMMILALVRNYEPSHRQAVEGgwNIADCVSRSYDLEGMTVGIVGAGRI 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 156 GVAMLRILKGFGMRLLAFDPY--PSAAALELGVEY-VDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNT 232
Cdd:PRK07574  204 GLAVLRRLKPFDVKLHYTDRHrlPEEVEQELGLTYhVSFDSLVSVCDVVTIHCPLHPETEHLFDADVLSRMKRGSYLVNT 283

                         170       180
                  ....*....|....*....|....*...
gi 1227727900 233 SRGALIDSQAAIEALKNQKIGSLGMDVY 260
Cdd:PRK07574  284 ARGKIVDRDAVVRALESGHLAGYAGDVW 311
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
 77-315 3.50e-41

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: 145.30  E-value: 3.50e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  77 AGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLT-GFTMYGKTAGVIGTGKI 155
Cdd:cd12156    73 VGYDGIDLDAARARGIRVTNTPGVLTDDVADLAVGLLLAVLRRIPAADRFVRAGRWPKGAFPlTRKVSGKRVGIVGLGRI 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 156 GVAMLRILKGFGMRLLAFDPYPSAaalelGVEYVDLPTLFS---ESDVISLHCPLTPENYHLLNEAAFDQM-KNGVmIVN 231
Cdd:cd12156   153 GRAIARRLEAFGMEIAYHGRRPKP-----DVPYRYYASLLElaaESDVLVVACPGGPATRHLVNAEVLEALgPDGV-LVN 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 232 TSRGALIDSQAAIEALKNQKIGSLGMDVYENErdlffedksndviqDDVFRRLSACHNVLFTGHQAFLTAEALTSISQTT 311
Cdd:cd12156   227 VARGSVVDEAALIAALQEGRIAGAGLDVFENE--------------PNVPAALLDLDNVVLTPHIASATVETRRAMGDLV 292


                  ....
gi 1227727900 312 LQNL 315
Cdd:cd12156   293 LANL 296
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
 78-260 4.17e-40

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: 143.62  E-value: 4.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  78 GFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDA--NFSLEGLTGFTMYGKTAGVIGTGKI 155
Cdd:cd05302    94 GSDHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILVRNYVPGHEQAIEGgwNVADVVKRAYDLEGKTVGTVGAGRI 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 156 GVAMLRILKGFGMRLLAFDPY--PSAAALELGVEYV-DLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNT 232
Cdd:cd05302   174 GLRVLRRLKPFDVHLLYYDRHrlPEEVEKELGLTRHaDLEDMVSKCDVVTINCPLHPETEGLFNKELLSKMKKGAYLVNT 253

                         170       180
                  ....*....|....*....|....*...
gi 1227727900 233 SRGALIDSQAAIEALKNQKIGSLGMDVY 260
Cdd:cd05302   254 ARGKICDREAVAEALESGHLAGYAGDVW 281
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
 1-263 2.88e-38

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: 138.04  E-value: 2.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900   1 MKLAVYStkQYDKKYLQQVNESFgfeLEFFDFLLTEKTAkTANGCEAVCIFVNDDgSHPVLEELKKhgVKYIALRCAGFN 80
Cdd:cd05300     1 MKILVLS--PLDDEHLERLRAAA---PGAELRVVTAEEL-TEELADADVLLGNPP-LPELLPAAPR--LRWIQSTSAGVD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  81 NVDLDAAKELGLKVVRVP-AYDPeAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTgFTMYGKTAGVIGTGKIGVAM 159
Cdd:cd05300    72 ALLFPELLERDVVLTNARgIFGP-PIAEYVLGYMLAFARKLPRYARNQAERRWQRRGPV-RELAGKTVLIVGLGDIGREI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 160 LRILKGFGMRLLAFDPypSAAALELGVEYV----DLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRG 235
Cdd:cd05300   150 ARRAKAFGMRVIGVRR--SGRPAPPVVDEVytpdELDELLPEADYVVNALPLTPETRGLFNAERFAAMKPGAVLINVGRG 227

                         250       260
                  ....*....|....*....|....*...
gi 1227727900 236 ALIDSQAAIEALKNQKIGSLGMDVYENE 263
Cdd:cd05300   228 SVVDEDALIEALESGRIAGAALDVFEEE 255
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
 64-263 7.33e-38

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: 137.66  E-value: 7.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  64 LKKHGVKYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRihrayqrtrdANFSLEGltgftmy 143
Cdd:cd12158    53 LEGSKVKFVGTATIGTDHIDTDYLKERGIGFANAPGCNANSVAEYVLSALLVLAQR----------QGFSLKG------- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 144 gKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPYpsAAALELGVEYVDLPTLFSESDVISLHCPLTPE----NYHLLNEAA 219
Cdd:cd12158   116 -KTVGIVGVGNVGSRLARRLEALGMNVLLCDPP--RAEAEGDPGFVSLEELLAEADIITLHVPLTRDgehpTYHLLDEDF 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1227727900 220 FDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENE 263
Cdd:cd12158   193 LAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVWENE 236
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
 56-321 3.06e-37

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: 135.40  E-value: 3.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  56 GSHPVLEEL---KKHGVKYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAY--QRTRDA 130
Cdd:cd12155    45 GYNPDFDELdlaKMKNLKWIQLYSAGVDYLPLEYIKKKGILLTNNSGIHSIPIAEWIVGYILEIYKGLKKAYknQKEKKW 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 131 NFSLEGLTgftMYGKTAGVIGTGKIGVAMLRILKGFGMRLL----------AFDP-YPSAaalelgveyvDLPTLFSESD 199
Cdd:cd12155   125 KMDSSLLE---LYGKTILFLGTGSIGQEIAKRLKAFGMKVIgvntsgrdveYFDKcYPLE----------ELDEVLKEAD 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 200 VISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENErDLffeDKSNDviqdd 279
Cdd:cd12155   192 IVVNVLPLTEETHHLFDEAFFEQMKKGALFINVGRGPSVDEDALIEALKNKQIRGAALDVFEEE-PL---PKDSP----- 262

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1227727900 280 vfrrLSACHNVLFTGHQAFLTA---EALTSI----------SQTTLQNLSNLEKG 321
Cdd:cd12155   263 ----LWDLDNVLITPHISGVSEhfnERLFDIfyenlksfleDGELLKNVVDLNKG 313
PRK06487 PRK06487
2-hydroxyacid dehydrogenase;
70-263 1.07e-36

2-hydroxyacid dehydrogenase;


Pssm-ID: 180588 [Multi-domain]  Cd Length: 317  Bit Score: 134.06  E-value: 1.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  70 KYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRI---HRAYQRTR---DANFSLEGLTGFTMY 143
Cdd:PRK06487   68 KLILVAATGTNNVDLAAARERGITVCNCQGYGTPSVAQHTLALLLALATRLpdyQQAVAAGRwqqSSQFCLLDFPIVELE 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 144 GKTAGVIGTGKIGVAMLRILKGFGMR-LLAFDPYPSAAAlelgvEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQ 222
Cdd:PRK06487  148 GKTLGLLGHGELGGAVARLAEAFGMRvLIGQLPGRPARP-----DRLPLDELLPQVDALTLHCPLTEHTRHLIGARELAL 222

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1227727900 223 MKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENE 263
Cdd:PRK06487  223 MKPGALLINTARGGLVDEQALADALRSGHLGGAATDVLSVE 263
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
 76-307 1.27e-35

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: 130.78  E-value: 1.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  76 CAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRI-------HRAyQRTRDANFSLEgltgftMYGKTAG 148
Cdd:cd12176    72 CIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIIMLARRLpdrnaaaHRG-IWNKSATGSHE------VRGKTLG 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 149 VIGTGKIGVAMLRILKGFGMRLLAFDPypsAAALELG--VEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNG 226
Cdd:cd12176   145 IIGYGHIGSQLSVLAEALGMRVIFYDI---AEKLPLGnaRQVSSLEELLAEADFVTLHVPATPSTKNMIGAEEIAQMKKG 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 227 VMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENerdlffEDKSNDviqDDVFRRLSACHNVLFTGHQAFLTAEALTS 306
Cdd:cd12176   222 AILINASRGTVVDIDALAEALRSGHLAGAAVDVFPE------EPASNG---EPFSSPLQGLPNVILTPHIGGSTEEAQEN 292


                  .
gi 1227727900 307 I 307
Cdd:cd12176   293 I 293
PRK00257 PRK00257
4-phosphoerythronate dehydrogenase PdxB;
69-265 1.82e-34

4-phosphoerythronate dehydrogenase PdxB;


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 129.39  E-value: 1.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  69 VKYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRihrayqrtrdanfsleglTGFTMYGKTAG 148
Cdd:PRK00257   59 VRFVGTCTIGTDHLDLDYFAEAGITWSSAPGCNARGVVDYVLGSLLTLAER------------------EGVDLAERTYG 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 149 VIGTGKIGVAMLRILKGFGMRLLAFDPyPSAAALELGvEYVDLPTLFSESDVISLHCPLTPE----NYHLLNEAAFDQMK 224
Cdd:PRK00257  121 VVGAGHVGGRLVRVLRGLGWKVLVCDP-PRQEAEGDG-DFVSLERILEECDVISLHTPLTKEgehpTRHLLDEAFLASLR 198

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1227727900 225 NGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENERD 265
Cdd:PRK00257  199 PGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWEGEPQ 239
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
60-322 3.30e-34

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 127.41  E-value: 3.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  60 VLEELKKhgVKYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLtg 139
Cdd:PRK08410   57 VLSQLPN--LKLICITATGTNNVDIEYAKKKGIAVKNVAGYSTESVAQHTFAMLLSLLGRINYYDRYVKSGEYSESPI-- 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 140 FTMY--------GKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPypSAAALELGVEYVDLPTLFSESDVISLHCPLTPEN 211
Cdd:PRK08410  133 FTHIsrplgeikGKKWGIIGLGTIGKRVAKIAQAFGAKVVYYST--SGKNKNEEYERVSLEELLKTSDIISIHAPLNEKT 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 212 YHLLNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSlGMDVYENErdlffedksnDVIQDDVFRRLSACHNVL 291
Cdd:PRK08410  211 KNLIAYKELKLLKDGAILINVGRGGIVNEKDLAKALDEKDIYA-GLDVLEKE----------PMEKNHPLLSIKNKEKLL 279

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1227727900 292 FTGHQAFLTAEALTSISQTTLQNLSNLEKGE 322
Cdd:PRK08410  280 ITPHIAWASKEARKTLIEKVKENIKDFLEGG 310
PLN02306 PLN02306
hydroxypyruvate reductase
 43-263 3.93e-31

hydroxypyruvate reductase


Pssm-ID: 177941  Cd Length: 386  Bit Score: 120.73  E-value: 3.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  43 NGCEAVCIFVNDDGSHPVLEELKKHGVKYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHR 122
Cdd:PLN02306   61 DKCDGVIGQLTEDWGETLFSALSKAGGKAFSNMAVGYNNVDVEAANKYGIAVGNTPGVLTETTAELAASLSLAAARRIVE 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 123 AYQRTRDANFslEG-----LTGFTMYGKTAGVIGTGKIGVAMLRIL-KGFGMRLLAFDPYPSAAALELGVEYVDL----- 191
Cdd:PLN02306  141 ADEFMRAGLY--EGwlphlFVGNLLKGQTVGVIGAGRIGSAYARMMvEGFKMNLIYYDLYQSTRLEKFVTAYGQFlkang 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 192 ------------PTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDV 259
Cdd:PLN02306  219 eqpvtwkrassmEEVLREADVISLHPVLDKTTYHLINKERLALMKKEAVLVNASRGPVIDEVALVEHLKANPMFRVGLDV 298


                  ....
gi 1227727900 260 YENE 263
Cdd:PLN02306  299 FEDE 302
2-Hacid_dh_2 cd12159
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 56-263 6.31e-31

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


Pssm-ID: 240636  Cd Length: 303  Bit Score: 118.14  E-value: 6.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  56 GSHPVLEEL-KKHGVKYIALRCAGFNNVdLDAAKELGLKVVRVPA---YDpEAVAEHAIGMMMTLNRRIH-RAYQRTRDA 130
Cdd:cd12159    36 GSAREPERLpASPGVRWVQLPFAGVEAF-VEAGVITDPGRRWTNAagaYA-ETVAEHALALLLAGLRQLPaRARATTWDP 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 131 NFSLEGLTgfTMYGKTAGVIGTGKIGVAMLRILKGFGMRLLAFD----PYPSAAALelgVEYVDLPTLFSESDVISLHCP 206
Cdd:cd12159   114 AEEDDLVT--LLRGSTVAIVGAGGIGRALIPLLAPFGAKVIAVNrsgrPVEGADET---VPADRLDEVWPDADHVVLAAP 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1227727900 207 LTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENE 263
Cdd:cd12159   189 LTPETRHLVDAAALAAMKPHAWLVNVARGPLVDTDALVDALRSGEIAGAALDVTDPE 245
PLN02928 PLN02928
oxidoreductase family protein
 78-300 1.36e-29

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 115.55  E-value: 1.36e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  78 GFNNVDLDAAKELGLKVVRVPAY---DPEAVAEHAIGMMMTLNRRIHRAYQRTRDANfsLEGLTGFTMYGKTAGVIGTGK 154
Cdd:PLN02928   92 GLEGVDVDAATKHGIKVARIPSEgtgNAASCAEMAIYLMLGLLRKQNEMQISLKARR--LGEPIGDTLFGKTVFILGYGA 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 155 IGVAMLRILKGFGMRLLA-----------FDPYPSAAALELGVE---YVDLPTLFSESDVISLHCPLTPENYHLLNEAAF 220
Cdd:PLN02928  170 IGIELAKRLRPFGVKLLAtrrswtsepedGLLIPNGDVDDLVDEkggHEDIYEFAGEADIVVLCCTLTKETAGIVNDEFL 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 221 DQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENERdlffEDKSNDVIQDDvfrrlsachNVLFTGHQAFLT 300
Cdd:PLN02928  250 SSMKKGALLVNIARGGLLDYDAVLAALESGHLGGLAIDVAWSEP----FDPDDPILKHP---------NVIITPHVAGVT 316
PRK15409 PRK15409
glyoxylate/hydroxypyruvate reductase GhrB;
78-263 6.50e-29

glyoxylate/hydroxypyruvate reductase GhrB;


Pssm-ID: 185307  Cd Length: 323  Bit Score: 113.31  E-value: 6.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  78 GFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSL---EGLTGFTMYGKTAGVIGTGK 154
Cdd:PRK15409   76 GYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLSTARRVVEVAERVKAGEWTAsigPDWFGTDVHHKTLGIVGMGR 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 155 IGVAML-RILKGFGMRLLAFDPYPSAAALE-LGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNT 232
Cdd:PRK15409  156 IGMALAqRAHFGFNMPILYNARRHHKEAEErFNARYCDLDTLLQESDFVCIILPLTDETHHLFGAEQFAKMKSSAIFINA 235

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1227727900 233 SRGALIDSQAAIEALKNQKIGSLGMDVYENE 263
Cdd:PRK15409  236 GRGPVVDENALIAALQKGEIHAAGLDVFEQE 266
PLN03139 PLN03139
formate dehydrogenase; Provisional
 78-260 3.17e-27

formate dehydrogenase; Provisional


Pssm-ID: 178684  Cd Length: 386  Bit Score: 109.94  E-value: 3.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  78 GFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLT--GFTMYGKTAGVIGTGKI 155
Cdd:PLN03139  131 GSDHIDLPAAAAAGLTVAEVTGSNVVSVAEDELMRILILLRNFLPGYHQVVSGEWNVAGIAyrAYDLEGKTVGTVGAGRI 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 156 GVAMLRILKGFGMRLLAFDPYPSAAALE--LGVEYV-DLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNT 232
Cdd:PLN03139  211 GRLLLQRLKPFNCNLLYHDRLKMDPELEkeTGAKFEeDLDAMLPKCDVVVINTPLTEKTRGMFNKERIAKMKKGVLIVNN 290

                         170       180
                  ....*....|....*....|....*...
gi 1227727900 233 SRGALIDSQAAIEALKNQKIGSLGMDVY 260
Cdd:PLN03139  291 ARGAIMDTQAVADACSSGHIGGYGGDVW 318
PRK11790 PRK11790
phosphoglycerate dehydrogenase;
76-303 3.44e-26

phosphoglycerate dehydrogenase;


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 107.19  E-value: 3.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  76 CAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIhraYQRTRDA-----NFSLEGltGFTMYGKTAGVI 150
Cdd:PRK11790   83 CIGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIILLLRGI---PEKNAKAhrggwNKSAAG--SFEVRGKTLGIV 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 151 GTGKIGvAMLRIL-KGFGMRLLAFDPypsAAALELG--VEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGV 227
Cdd:PRK11790  158 GYGHIG-TQLSVLaESLGMRVYFYDI---EDKLPLGnaRQVGSLEELLAQSDVVSLHVPETPSTKNMIGAEELALMKPGA 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 228 MIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENerdlffEDKSNdviqDDVF----RRLSachNVLFTGHQAFLTAEA 303
Cdd:PRK11790  234 ILINASRGTVVDIDALADALKSGHLAGAAIDVFPV------EPKSN----GDPFesplRGLD---NVILTPHIGGSTQEA 300
2-Hacid_dh_15 cd12180
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 103-263 2.53e-24

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: 100.49  E-value: 2.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 103 EAVAEHAIGMMMTLNRRIHRAYQRtRDANFSLEGLTgfTMYGKTAGVIGTGKIGVAMLRILKGFGMRLLAF--DPYPSAa 180
Cdd:cd12180    97 EAIAEFVLAAILAAAKRLPEIWVK-GAEQWRREPLG--SLAGSTLGIVGFGAIGQALARRALALGMRVLALrrSGRPSD- 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 181 alELGVEYV-DLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDV 259
Cdd:cd12180   173 --VPGVEAAaDLAELFARSDHLVLAAPLTPETRHLINADVLAQAKPGLHLINIARGGLVDQEALLEALDSGRISLASLDV 250


                  ....
gi 1227727900 260 YENE 263
Cdd:cd12180   251 TDPE 254
2-Hacid_dh_9 cd12170
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 69-317 3.81e-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: 240647 [Multi-domain]  Cd Length: 294  Bit Score: 91.59  E-value: 3.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  69 VKYIALRCAGFN----NVDLDAAKELGLKVVRVPAYDPEAVAEHAIgmmMTLNRRIHrAYQRTRDANFSLEgLTGftmyg 144
Cdd:cd12170    69 IKYIGMCCSLYSeesaNVDIAAARENGITVTGIRDYGDEGVVEYVI---SELIRLLH-GFGGKQWKEEPRE-LTG----- 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 145 KTAGVIGTGKIGVAMLRILKGFGMRLLAFDPYPSAAALELGVEYVDLPTLFSESDVISLHcplTPENYHLLNEAAFDQMK 224
Cdd:cd12170   139 LKVGIIGLGTTGQMIADALSFFGADVYYYSRTRKPDAEAKGIRYLPLNELLKTVDVICTC---LPKNVILLGEEEFELLG 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 225 NGVMIVNTSRGALIDSQAAIEALKNQKigslgmdvyeneRDLFFEDKSNDVIQDDVFRRlsacHNVLFTGHQAFLTAEAL 304
Cdd:cd12170   216 DGKILFNTSLGPSFEVEALKKWLKASG------------YNIFDCDTAGALGDEELLRY----PNVICTNKSAGWTRQAF 279

                         250
                  ....*....|...
gi 1227727900 305 TSISQTTLQNLSN 317
Cdd:cd12170   280 ERLSQKVLANLEE 292
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 104-259 1.06e-20

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: 90.34  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 104 AVAEHAIGMMMTLNRRIHRAYQRTRDANFslEGLTGFTMYGKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPYPSAAALE 183
Cdd:cd12166    94 STAELAVALILASLRGLPRFVRAQARGRW--EPRRTPSLADRRVLIVGYGSIGRAIERRLAPFEVRVTRVARTARPGEQV 171

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1227727900 184 LGVEyvDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIgSLGMDV 259
Cdd:cd12166   172 HGID--ELPALLPEADVVVLIVPLTDETRGLVDAEFLARMPDGALLVNVARGPVVDTDALVAELASGRL-RAALDV 244
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
 64-266 2.00e-19

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 88.04  E-value: 2.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  64 LKKHGVKYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRihrayqrtrdanfsleglTGFTMY 143
Cdd:PRK15438   54 LAGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAER------------------DGFSLH 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 144 GKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPyPSAAALELGvEYVDLPTLFSESDVISLHCPLTPE----NYHLLNEAA 219
Cdd:PRK15438  116 DRTVGIVGVGNVGRRLQARLEALGIKTLLCDP-PRADRGDEG-DFRSLDELVQEADILTFHTPLFKDgpykTLHLADEKL 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1227727900 220 FDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENERDL 266
Cdd:PRK15438  194 IRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPEL 240
2-Hacid_dh_5 cd12163
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 15-327 1.24e-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: 240640  Cd Length: 334  Bit Score: 85.02  E-value: 1.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  15 YLQQVNESF-GFELEFFDFLLTEKTAKTANG--CEAVCIFVNDdGSHPVLEELKKhgVKYIALRCAGFNNvdldAAKElg 91
Cdd:cd12163     1 WLAKLRKRFpGLEIRWVESAPPDGPPEDVPAevWEGVTILCTF-HPHPDAEDVPN--LRLVQLFSAGADH----WLGH-- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  92 lkvvrvPAY-DPE------------AVAEHAIGMMMTLNRRIHRAY--QRTRDANFSLEGLTGFTMYGKTAGVIGTGKIG 156
Cdd:cd12163    72 ------PLYkDPEvplctasgihgpQIAEWVIGTWLVLSHHFLQYIelQKEQTWGRRQEAYSVEDSVGKRVGILGYGSIG 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 157 VAMLRILKGFGMRLLAF----------------------DP---YPSA-------AALElgvEYvdlptLFSESD--VIS 202
Cdd:cd12163   146 RQTARLAQALGMEVYAYtrsprptpesrkddgyivpgtgDPdgsIPSAwfsgtdkASLH---EF-----LRQDLDllVVS 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 203 LhcPLTPENYHLLNEAAFDQM-KNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENErdlffedksndviqddvf 281
Cdd:cd12163   218 L--PLTPATKHLLGAEEFEILaKRKTFVSNIARGSLVDTDALVAALESGQIRGAALDVTDPE------------------ 277

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1227727900 282 rRLSACH------NVLFTGHQAFLTAEALTSISQTTLQNLSNLEKGETCPNE 327
Cdd:cd12163   278 -PLPADHplwsapNVIITPHVSWQTQEYFDRALDVLEENLERLRKGEPLINL 328
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 54-264 8.53e-18

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: 82.28  E-value: 8.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  54 DDGSHPVLEE---LKKHGVKYIALRCAGFNNVDL-DAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTrd 129
Cdd:cd12154    70 KVKEPLTNAEyalIQKLGDRLLFTYTIGADHRDLtEALARAGLTAIAVEGVELPLLTSNSIGAGELSVQFIARFLEVQ-- 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 130 anFSLEGLTGFTMYGKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPYPSA---AALELGVEYVDLPTLFSESDVISLHCP 206
Cdd:cd12154   148 --QPGRLGGAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEAleqLEELGGKNVEELEEALAEADVIVTTTL 225

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 207 LTPENYHLLN-EAAFDQMKNGVMIVNTSRGALIDSQAAI-EALKNQKIGSLGMDVYENER 264
Cdd:cd12154   226 LPGKRAGILVpEELVEQMKPGSVIVNVAVGAVGCVQALHtQLLEEGHGVVHYGDVNMPGP 285
PRK06436 PRK06436
2-hydroxyacid dehydrogenase;
70-263 2.82e-16

2-hydroxyacid dehydrogenase;


Pssm-ID: 235800 [Multi-domain]  Cd Length: 303  Bit Score: 78.00  E-value: 2.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  70 KYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPeAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTgfTMYGKTAGV 149
Cdd:PRK06436   51 KMIQSLSAGVDHIDVSGIPENVVLCSNAGAYSI-SVAEHAFALLLAWAKNICENNYNMKNGNFKQSPTK--LLYNKSLGI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 150 IGTGKIGVAMLRILKGFGMRLLAFdpypSAAALELGVE--YVDLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGV 227
Cdd:PRK06436  128 LGYGGIGRRVALLAKAFGMNIYAY----TRSYVNDGISsiYMEPEDIMKKSDFVLISLPLTDETRGMINSKMLSLFRKGL 203

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1227727900 228 MIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENE 263
Cdd:PRK06436  204 AIINVARADVVDKNDMLNFLRNHNDKYYLSDVWWNE 239
2-Hacid_dh_3 cd12160
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 105-263 8.79e-16

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: 76.65  E-value: 8.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 105 VAEHAIGMMMTLNRRIH--RAYQRTRDANFSLEGLTG-------FTMYGKTAGVIGTGKIGVAMLRILKGFGMRLLafdP 175
Cdd:cd12160    95 VAEHTLALILAAVRRLDemREAQREHRWAGELGGLQPlrpagrlTTLLGARVLIWGFGSIGQRLAPLLTALGARVT---G 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 176 YPSAAALELGVEYV---DLPTLFSESDVISLHCPLTPENYHLLNEAAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKI 252
Cdd:cd12160   172 VARSAGERAGFPVVaedELPELLPETDVLVMILPATPSTAHALDAEVLAALPKHAWVVNVGRGATVDEDALVAALESGRL 251

                         170
                  ....*....|.
gi 1227727900 253 GSLGMDVYENE 263
Cdd:cd12160   252 GGAALDVTATE 262
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
 77-326 4.69e-14

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: 71.37  E-value: 4.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  77 AGfnnVD-LDAAKEL-GLKVVRVpaYDPE---AVAEHAIGMMMTLNRRI--HRAYQRTRD---------ANFslegltgf 140
Cdd:cd12164    67 AG---VDhLLADPDLpDVPIVRL--VDPGlaqGMAEYVLAAVLRLHRDMdrYAAQQRRGVwkplpqrpaAER-------- 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 141 tmygkTAGVIGTGKIGVAMLRILKGFGMRLLAFDPypSAAALELGVEYV---DLPTLFSESDVisLHC--PLTPENYHLL 215
Cdd:cd12164   134 -----RVGVLGLGELGAAVARRLAALGFPVSGWSR--SPKDIEGVTCFHgeeGLDAFLAQTDI--LVCllPLTPETRGIL 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 216 NEAAFDQMKNGVMIVNTSRGALIDSQAAIEALKNQKIG--SLgmdvyenerdlffedksndviqdDVFRR--LSACH--- 288
Cdd:cd12164   205 NAELLARLPRGAALINVGRGPHLVEADLLAALDSGHLSgaVL-----------------------DVFEQepLPADHplw 261

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1227727900 289 ---NVLFTGHQAfltaeALT---SISQTTLQNLSNLEKGETCPN 326
Cdd:cd12164   262 rhpRVTVTPHIA-----AITdpdSAAAQVAENIRRLEAGEPLPN 300
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 144-201 6.84e-04

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 41.08  E-value: 6.84e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 144 GKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPYPSA--AALELGVEYVDLPTLFSESDVI 201
Cdd:cd08254   166 GETVLVIGLGGLGLNAVQIAKAMGAAVIAVDIKEEKleLAKELGADEVLNSLDDSPKDKK 225
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 145-201 1.44e-03

Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 39.72  E-value: 1.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1227727900 145 KTAGVIGTGKIGVAMLRILK--GFGMRLLAFDPYPS--AAALELGV---EYVDLPTLFSESDVI 201
Cdd:COG0287     2 MRIAIIGLGLIGGSLALALKraGLAHEVVGVDRSPEtlERALELGVidrAATDLEEAVADADLV 65
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
133-231 3.15e-03

S-adenosyl-L-homocysteine hydrolase, NAD binding domain;


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 37.81  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900  133 SLEGL---TGFTMYGKTAGVIGTGKIG--VAMLriLKGFGMRLLAFDPYPsAAALEL---GVEYVDLPTLFSESDVIslh 204
Cdd:smart00997   9 LLDGIlraTNVLLAGKNVVVAGYGDVGkgVAAR--LRGLGARVIVTEIDP-IRALEAamdGFEVMKMEEAAKRADIF--- 82

                           90       100
                   ....*....|....*....|....*...
gi 1227727900  205 cpLTPE-NYHLLNEAAFDQMKNGVMIVN 231
Cdd:smart00997  83 --VTATgNKDVITREHFRAMKDGAILAN 108
ceo_syn cd12181
N(5)-(carboxyethyl)ornithine synthase; N(5)-(carboxyethyl)ornithine synthase (ceo_syn) ...
 132-233 6.39e-03

N(5)-(carboxyethyl)ornithine synthase; N(5)-(carboxyethyl)ornithine synthase (ceo_syn) catalyzes the NADP-dependent conversion of N5-(L-1-carboxyethyl)-L-ornithine to L-ornithine + pyruvate. Ornithine plays a key role in the urea cycle, which in mammals is used in arginine biosynthesis, and is a precursor in polyamine synthesis. ceo_syn is related to the NAD-dependent L-alanine dehydrogenases. Like formate dehydrogenase and related enzymes, ceo_syn is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. These ceo_syn proteins have a partially conserved NAD-binding motif and active site residues that are characteristic of related enzymes such as Saccharopine Dehydrogenase.


Pssm-ID: 240658 [Multi-domain]  Cd Length: 295  Bit Score: 37.98  E-value: 6.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227727900 132 FSLEGLTGFTmyGKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPYPSAAalelgveyvdLPTLFSESDVIsLHCPL--TP 209
Cdd:cd12181   144 LQLYGITPYR--QTKVAVLGFGNTARGAIRALKLGGADVTVYTRRTEAL----------FKEELSEYDII-VNCILqdTD 210

                          90       100
                  ....*....|....*....|....
gi 1227727900 210 ENYHLLNEAAFDQMKNGVMIVNTS 233
Cdd:cd12181   211 RPDHIIYEEDLKRLKPGALIIDVS 234
 
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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