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Conserved domains on  [gi|1285015877|ref|XP_023020063|]
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C-terminal-binding protein isoform X7 [Leptinotarsa decemlineata]

Protein Classification

C-terminal binding protein( domain architecture ID 10143094)

C-terminal binding protein (CtBP) functions as a transcriptional regulator by tethering chromatin remodeling proteins, such as histone deacetylases, histone methyl transferases, and histone demethylases, to DNA-bound transcription factors; CtBP may also have NAD-dependent dehydrogenase activity

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
28-346 8.47e-156

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: 442.72  E-value: 8.47e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  28 PLVALLDGR--DCSIEMPILKDvATVAFCDAQS--TSEIHEKVlNEAVGALMWHTIIlTKEDLEKFKTLRIIVRIGSGVD 103
Cdd:cd05299     1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYAPV-TAEVIEALPRLKVIVRYGVGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 104 NIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREGKKFTGpeqvreAAQGCARIRGDTLGIVGLG 183
Cdd:cd05299    78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWT------VGGPIRRLRGLTLGLVGFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 184 RIGSAVALRAKAFGFNVIFYDPYLPDGIEkSLGLTRVYTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVN 263
Cdd:cd05299   152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVA-ALGGVRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 264 TARGGLVDDDALAQALKQGRIRAAALDVHENEPYNvFAGPLKDAPNLLCTPHAAFYSDASATELREMAASEIRRAITGRI 343
Cdd:cd05299   231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPP-ADSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                  ...
gi 1285015877 344 PEC 346
Cdd:cd05299   310 PRN 312
 
Name Accession Description Interval E-value
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
28-346 8.47e-156

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: 442.72  E-value: 8.47e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  28 PLVALLDGR--DCSIEMPILKDvATVAFCDAQS--TSEIHEKVlNEAVGALMWHTIIlTKEDLEKFKTLRIIVRIGSGVD 103
Cdd:cd05299     1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYAPV-TAEVIEALPRLKVIVRYGVGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 104 NIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREGKKFTGpeqvreAAQGCARIRGDTLGIVGLG 183
Cdd:cd05299    78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWT------VGGPIRRLRGLTLGLVGFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 184 RIGSAVALRAKAFGFNVIFYDPYLPDGIEkSLGLTRVYTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVN 263
Cdd:cd05299   152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVA-ALGGVRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 264 TARGGLVDDDALAQALKQGRIRAAALDVHENEPYNvFAGPLKDAPNLLCTPHAAFYSDASATELREMAASEIRRAITGRI 343
Cdd:cd05299   231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPP-ADSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                  ...
gi 1285015877 344 PEC 346
Cdd:cd05299   310 PRN 312
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
50-353 2.42e-102

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: 307.02  E-value: 2.42e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  50 TVAFCDAQSTSEIHEKVLNEAVGALMWHTIILTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVA 129
Cdd:COG1052    25 EVTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDLAAAKERGITVTNTPGYLTEAVA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 130 DTTLCLILNLYRRTFWLANMVREGK-KFTGPEQVREaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLP 208
Cdd:COG1052   105 EHAVALLLALARRIVEADRRVRAGDwSWSPGLLGRD-------LSGKTLGIIGLGRIGQAVARRAKGFGMKVLYYDRSPK 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 209 DGIEKsLGLTRVyTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAA 288
Cdd:COG1052   178 PEVAE-LGAEYV-SLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARGGLVDEAALIEALKSGRIAGAG 255
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1285015877 289 LDVHENEPyNVFAGPLKDAPNLLCTPHAAFYSDASATELREMAASEIRRAITGRIPeclRNCVNK 353
Cdd:COG1052   256 LDVFEEEP-PPPDHPLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPP---PNPVNP 316
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
30-352 2.97e-83

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: 257.99  E-value: 2.97e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  30 VALLDGRdCSIEMPILKDvATVAFCDAQSTSEIHEKVlnEAVGALMWHTII-LTKEDLEKFKTLRIIVRIGSGVDNIDVK 108
Cdd:pfam00389   1 VLILDPL-SPEALELLKE-GEVEVHDELLTEELLEKA--KDADALIVRSRTkVTAEVLEAAPKLKVIGRAGVGVDNVDLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 109 AAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREGKKFTGPEQVREaaqgcarIRGDTLGIVGLGRIGSA 188
Cdd:pfam00389  77 AATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLE-------LYGKTLGVIGGGGIGGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 189 VALRAKAFGFNVIFYDPYLPDGIEKSLGLTRV-YTLQDLLFQSDC--VSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTA 265
Cdd:pfam00389 150 VAAIAKAFGMGVVAYDPYPNPERAEAGGVEVLsLLLLLLDLPESDdvLTVNPLTTMKTGVIIINEARGMLKDAVAIINAA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 266 RGGLVDDDALAQALKQGRIRAAALDVHENEPynVFAGPLKDAPNLLCTPHAAFYSDASATELREMAASEIRRAITGRIPe 345
Cdd:pfam00389 230 GGGVIDEAALDALLEEGIAAAADLDVEEEPP--PVDSPLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPP- 306

                  ....*..
gi 1285015877 346 clRNCVN 352
Cdd:pfam00389 307 --ANAVN 311
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
81-352 6.88e-66

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: 219.50  E-value: 6.88e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  81 LTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRtFWLANM-VREG----KK 155
Cdd:TIGR01327  52 VTEEVIAAAPKLKVIGRAGVGVDNIDIEAATARGILVVNAPTGNTISAAEHALAMLLAAARN-IPQADAsLKEGewdrKA 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 156 FTGPEqvreaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGIEKSLGLTRVYTLQDLLFQSDCVSL 235
Cdd:TIGR01327 131 FMGTE-----------LYGKTLGVIGLGRIGSIVAKRAKAFGMKVLAYDPYISPERAEQLGVELVDDLDELLARADFITV 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 236 HCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPYNvfAGPLKDAPNLLCTPH 315
Cdd:TIGR01327 200 HTPLTPETRGLIGAEELAKMKKGVIIVNCARGGIIDEAALYEALEEGHVRAAALDVFEKEPPT--DNPLFDLDNVIATPH 277
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1285015877 316 AAfysdASATELRE----MAASEIRRAITGripECLRNCVN 352
Cdd:TIGR01327 278 LG----ASTREAQEnvatQVAEQVLDALKG---LPVPNAVN 311
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
30-341 2.86e-60

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 198.67  E-value: 2.86e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  30 VALLDGR---DCSIEmpILKDVATVAFCDAQSTSEIHEKVLNEAVgaLMWHTIILTKEDLEKFKTLRIIVRIGSGVDNID 106
Cdd:PRK08410    3 IVILDAKtlgDKDLS--VFEEFGDFQIYPTTSPEEVIERIKDANI--IITNKVVIDKEVLSQLPNLKLICITATGTNNVD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 107 VKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREGK-----KFTGPEQVREaaqgcaRIRGDTLGIVG 181
Cdd:PRK08410   79 IEYAKKKGIAVKNVAGYSTESVAQHTFAMLLSLLGRINYYDRYVKSGEysespIFTHISRPLG------EIKGKKWGIIG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 182 LGRIGSAVALRAKAFGFNVIFYDPylpDGIEKSLGLTRVyTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFL 261
Cdd:PRK08410  153 LGTIGKRVAKIAQAFGAKVVYYST---SGKNKNEEYERV-SLEELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGAIL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 262 VNTARGGLVDDDALAQALKQGRIrAAALDVHENEP---YNVFAGPlKDAPNLLCTPHAAFYSDASATELREMAASEIRRA 338
Cdd:PRK08410  229 INVGRGGIVNEKDLAKALDEKDI-YAGLDVLEKEPmekNHPLLSI-KNKEKLLITPHIAWASKEARKTLIEKVKENIKDF 306

                  ...
gi 1285015877 339 ITG 341
Cdd:PRK08410  307 LEG 309
 
Name Accession Description Interval E-value
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
28-346 8.47e-156

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: 442.72  E-value: 8.47e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  28 PLVALLDGR--DCSIEMPILKDvATVAFCDAQS--TSEIHEKVlNEAVGALMWHTIIlTKEDLEKFKTLRIIVRIGSGVD 103
Cdd:cd05299     1 PKVVITDYDfpDLDIEREVLEE-AGVELVDAQSrtEDELIEAA-ADADALLVQYAPV-TAEVIEALPRLKVIVRYGVGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 104 NIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREGKKFTGpeqvreAAQGCARIRGDTLGIVGLG 183
Cdd:cd05299    78 NVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWT------VGGPIRRLRGLTLGLVGFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 184 RIGSAVALRAKAFGFNVIFYDPYLPDGIEkSLGLTRVYTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVN 263
Cdd:cd05299   152 RIGRAVAKRAKAFGFRVIAYDPYVPDGVA-ALGGVRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAFLVN 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 264 TARGGLVDDDALAQALKQGRIRAAALDVHENEPYNvFAGPLKDAPNLLCTPHAAFYSDASATELREMAASEIRRAITGRI 343
Cdd:cd05299   231 TARGGLVDEAALARALKSGRIAGAALDVLEEEPPP-ADSPLLSAPNVILTPHAAWYSEESLAELRRKAAEEVVRVLRGEP 309

                  ...
gi 1285015877 344 PEC 346
Cdd:cd05299   310 PRN 312
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
30-337 5.32e-104

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: 310.72  E-value: 5.32e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  30 VALLDGRDCSIEMPILKD-VATVAFCDAQSTSEIhEKVLNEAVGALMWHTIILTKEDLEKFKTLRIIVRIGSGVDNIDVK 108
Cdd:cd05198     2 VLVLEPLFPPEALEALEAtGFEVIVADDLLADEL-EALLADADALIVSSTTPVTAEVLAKAPKLKFIQVAGAGVDNIDLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 109 AAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREGKKftgpeqVREAAQGCARIRGDTLGIVGLGRIGSA 188
Cdd:cd05198    81 AAKKRGITVTNVPGANAEAVAEHALGLLLALLRRLPRADAAVRRGWG------WLWAGFPGYELEGKTVGIVGLGRIGQR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 189 VALRAKAFGFNVIFYDPYLPDGIEKSLGLTRVyTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGG 268
Cdd:cd05198   155 VAKRLQAFGMKVLYYDRTRKPEPEEDLGFRVV-SLDELLAQSDVVVLHLPLTPETRHLINEEELALMKPGAVLVNTARGG 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1285015877 269 LVDDDALAQALKQGRIRAAALDVHENEPyNVFAGPLKDAPNLLCTPHAAFYSDASATELREMAASEIRR 337
Cdd:cd05198   234 LVDEDALLRALKSGKIAGAALDVFEPEP-LPADHPLLELPNVILTPHIAGYTEEARERMAEIAVENLER 301
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
50-353 2.42e-102

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: 307.02  E-value: 2.42e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  50 TVAFCDAQSTSEIHEKVLNEAVGALMWHTIILTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVA 129
Cdd:COG1052    25 EVTVYEDETSPEELAERAAGADAVITNGKDPIDAEVLEALPGLKLIANRGVGYDNIDLAAAKERGITVTNTPGYLTEAVA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 130 DTTLCLILNLYRRTFWLANMVREGK-KFTGPEQVREaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLP 208
Cdd:COG1052   105 EHAVALLLALARRIVEADRRVRAGDwSWSPGLLGRD-------LSGKTLGIIGLGRIGQAVARRAKGFGMKVLYYDRSPK 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 209 DGIEKsLGLTRVyTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAA 288
Cdd:COG1052   178 PEVAE-LGAEYV-SLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARGGLVDEAALIEALKSGRIAGAG 255
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1285015877 289 LDVHENEPyNVFAGPLKDAPNLLCTPHAAFYSDASATELREMAASEIRRAITGRIPeclRNCVNK 353
Cdd:COG1052   256 LDVFEEEP-PPPDHPLLSLPNVVLTPHIASATEEAREAMAELALDNLLAFLAGEPP---PNPVNP 316
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
49-352 6.47e-97

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: 292.87  E-value: 6.47e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  49 ATVAFCDAQSTSEIHEKvLNEAVGALMWHTIILTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEV 128
Cdd:COG0111    23 IEVVYAPGLDEEELAEA-LADADALIVRSRTKVTAELLAAAPNLKLIGRAGAGVDNIDLAAATERGIPVTNAPGANARAV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 129 ADTTLCLILNLYRRTFWLANMVREG----KKFTGPEqvreaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYD 204
Cdd:COG0111   102 AEYALALLLALARRLPEADRAQRAGrwdrSAFRGRE-----------LRGKTVGIVGLGRIGRAVARRLRAFGMRVLAYD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 205 PYLPDGIEKSLGLTRVYTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRI 284
Cdd:COG0111   171 PSPKPEEAADLGVGLVDSLDELLAEADVVSLHLPLTPETRGLIGAEELAAMKPGAILINTARGGVVDEDALLAALDSGRL 250
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1285015877 285 RAAALDVHENEPyNVFAGPLKDAPNLLCTPHAAFYSDASATELREMAASEIRRAITGRIPeclRNCVN 352
Cdd:COG0111   251 AGAALDVFEPEP-LPADSPLWDLPNVILTPHIAGSTEEAQERAARQVAENIRRFLAGEPL---RNLVN 314
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
58-338 8.43e-91

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: 277.06  E-value: 8.43e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  58 STSEIHEKvLNEAVGALMWHTIIlTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLIL 137
Cdd:cd12172    37 TEEELIEL-LKDADGVIAGLDPI-TEEVLAAAPRLKVISRYGVGYDNIDLEAAKKRGIVVTNTPGANSNSVAELTIGLML 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 138 NLYRRTFWLANMVREGK--KFTGPEqvreaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGIEKSL 215
Cdd:cd12172   115 ALARQIPQADREVRAGGwdRPVGTE-----------LYGKTLGIIGLGRIGKAVARRLSGFGMKVLAYDPYPDEEFAKEH 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 216 GLTRVyTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENE 295
Cdd:cd12172   184 GVEFV-SLEELLKESDFISLHLPLTPETRHLINAAELALMKPGAILINTARGGLVDEEALYEALKSGRIAGAALDVFEEE 262
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1285015877 296 PYNVfAGPLKDAPNLLCTPHAAFYSDASATELREMAASEIRRA 338
Cdd:cd12172   263 PPPA-DSPLLELPNVILTPHIGASTKEAVLRMGTMAAQNVIDV 304
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
80-342 1.88e-86

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: 265.82  E-value: 1.88e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  80 ILTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREG----KK 155
Cdd:cd12173    51 KVTAEVIEAAPRLKVIGRAGVGVDNIDVEAATARGILVVNAPGANTISVAEHTIALMLALARNIPQADASLRAGkwdrKK 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 156 FTGPEqvreaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGIEKSLGlTRVYTLQDLLFQSDCVSL 235
Cdd:cd12173   131 FMGVE-----------LRGKTLGIVGLGRIGREVARRARAFGMKVLAYDPYISAERAAAGG-VELVSLDELLAEADFISL 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 236 HCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPyNVFAGPLKDAPNLLCTPH 315
Cdd:cd12173   199 HTPLTPETRGLINAEELAKMKPGAILINTARGGIVDEAALADALKSGKIAGAALDVFEQEP-PPADSPLLGLPNVILTPH 277
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1285015877 316 AAfysdASATELRE----MAASEIRRAITGR 342
Cdd:cd12173   278 LG----ASTEEAQErvavDAAEQVLAVLAGE 304
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
30-352 2.97e-83

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: 257.99  E-value: 2.97e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  30 VALLDGRdCSIEMPILKDvATVAFCDAQSTSEIHEKVlnEAVGALMWHTII-LTKEDLEKFKTLRIIVRIGSGVDNIDVK 108
Cdd:pfam00389   1 VLILDPL-SPEALELLKE-GEVEVHDELLTEELLEKA--KDADALIVRSRTkVTAEVLEAAPKLKVIGRAGVGVDNVDLD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 109 AAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREGKKFTGPEQVREaaqgcarIRGDTLGIVGLGRIGSA 188
Cdd:pfam00389  77 AATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLE-------LYGKTLGVIGGGGIGGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 189 VALRAKAFGFNVIFYDPYLPDGIEKSLGLTRV-YTLQDLLFQSDC--VSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTA 265
Cdd:pfam00389 150 VAAIAKAFGMGVVAYDPYPNPERAEAGGVEVLsLLLLLLDLPESDdvLTVNPLTTMKTGVIIINEARGMLKDAVAIINAA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 266 RGGLVDDDALAQALKQGRIRAAALDVHENEPynVFAGPLKDAPNLLCTPHAAFYSDASATELREMAASEIRRAITGRIPe 345
Cdd:pfam00389 230 GGGVIDEAALDALLEEGIAAAADLDVEEEPP--PVDSPLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDGGPP- 306

                  ....*..
gi 1285015877 346 clRNCVN 352
Cdd:pfam00389 307 --ANAVN 311
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
78-344 4.47e-81

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: 252.11  E-value: 4.47e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  78 TIILTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREGKKFt 157
Cdd:cd12175    52 RKVIDAELLAAAPRLRLIQQPGVGLDGVDLEAATARGIPVANIPGGNAESVAEHAVMLMLALLRRLPEADRELRAGRWG- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 158 gpeqvREAAQGCARIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPY-LPDGIEKSLGLTRVyTLQDLLFQSDCVSLH 236
Cdd:cd12175   131 -----RPEGRPSRELSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFrDPEAEEKDLGVRYV-ELDELLAESDVVSLH 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 237 CTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPynVFAG-PLKDAPNLLCTPH 315
Cdd:cd12175   205 VPLTPETRHLIGAEELAAMKPGAILINTARGGLVDEEALLAALRSGHLAGAGLDVFWQEP--LPPDdPLLRLDNVILTPH 282
                         250       260
                  ....*....|....*....|....*....
gi 1285015877 316 AAFYSDASATELREMAASEIRRAITGRIP 344
Cdd:cd12175   283 IAGVTDESYQRMAAIVAENIARLLRGEPP 311
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
42-341 4.31e-79

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: 246.92  E-value: 4.31e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  42 MPILKDVATVAFCD---AQSTSEIHEKVlNEAVGALMWHTIILTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVC 118
Cdd:cd05301    14 LALLREGFEVEVWDedrPLPREELLEAA-KGADGLLCTLTDKIDAELLDAAPPLKVIANYSVGYDHIDVDAAKARGIPVT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 119 NVPGYGVEEVADTTLCLILNLYRRTFWLANMVREGKK-------FTGPEqvreaaqgcarIRGDTLGIVGLGRIGSAVAL 191
Cdd:cd05301    93 NTPDVLTDATADLAFALLLAAARRVVEGDRFVRAGEWkgwsptlLLGTD-----------LHGKTLGIVGMGRIGQAVAR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 192 RAKAFGFNVIFYDPYLPDGIEKSLGLTRVyTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVD 271
Cdd:cd05301   162 RAKGFGMKILYHNRSRKPEAEEELGARYV-SLDELLAESDFVSLHCPLTPETRHLINAERLALMKPTAILINTARGGVVD 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1285015877 272 DDALAQALKQGRIRAAALDVHENEPyNVFAGPLKDAPNLLCTPHAafysdASAT-ELR----EMAASEIRRAITG 341
Cdd:cd05301   241 EDALVEALKSGKIAGAGLDVFEPEP-LPADHPLLTLPNVVLLPHI-----GSATvETRtamaELAADNLLAVLAG 309
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
79-336 3.92e-76

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: 239.28  E-value: 3.92e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  79 IILTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREGK---- 154
Cdd:cd12162    53 VVLDAEVLAQLPNLKLIGVLATGYNNVDLAAAKERGITVTNVPGYSTDSVAQHTFALLLALARLVAYHNDVVKAGEwqks 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 155 ----KFTGPeqVREaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYlpdgIEKSLGLTRVyTLQDLLFQS 230
Cdd:cd12162   133 pdfcFWDYP--IIE-------LAGKTLGIIGYGNIGQAVARIARAFGMKVLFAERK----GAPPLREGYV-SLDELLAQS 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 231 DCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPynvfagP------L 304
Cdd:cd12162   199 DVISLHCPLTPETRNLINAEELAKMKPGAILINTARGGLVDEQALADALNSGKIAGAGLDVLSQEP------PradnplL 272
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1285015877 305 KDAPNLLCTPHAAFYSDASATELREMAASEIR 336
Cdd:cd12162   273 KAAPNLIITPHIAWASREARQRLMDILVDNIK 304
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
82-352 1.68e-74

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: 235.59  E-value: 1.68e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  82 TKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRR-TFWLANMVREGKKFTGP- 159
Cdd:cd12178    56 DKEIIDAAKNLKIIANYGAGFDNIDVDYAKEKGIPVTNTPAVSTEPTAELTFGLILALARRiAEGDRLMRRGGFLGWAPl 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 160 -EQVREaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPY-LPDGIEKSLGLTRVyTLQDLLFQSDCVSLHC 237
Cdd:cd12178   136 fFLGHE-------LAGKTLGIIGMGRIGQAVARRAKAFGMKILYYNRHrLSEETEKELGATYV-DLDELLKESDFVSLHA 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 238 TLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPYnvFAGPLKDAPNLLCTPHAa 317
Cdd:cd12178   208 PYTPETHHLIDAAAFKLMKPTAYLINAARGPLVDEKALVDALKTGEIAGAALDVFEFEPE--VSPELKKLDNVILTPHI- 284
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1285015877 318 fysdASAT-----ELREMAASEIRRAITGRIPeclRNCVN 352
Cdd:cd12178   285 ----GNATveardAMAKEAADNIISFLEGKRP---KNIVN 317
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
81-335 6.73e-74

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: 233.58  E-value: 6.73e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  81 LTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREG----KKF 156
Cdd:cd05303    53 VTKEVIDAAKNLKIIARAGVGLDNIDVEYAKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHRANREMKLGkwnkKKY 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 157 TGPEqvreaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGIEKSLGLTRVyTLQDLLFQSDCVSLH 236
Cdd:cd05303   133 KGIE-----------LRGKTLGIIGFGRIGREVAKIARALGMNVIAYDPYPKDEQAVELGVKTV-SLEELLKNSDFISLH 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 237 CTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPYNvfAGPLKDAPNLLCTPHA 316
Cdd:cd05303   201 VPLTPETKHMINKKELELMKDGAIIINTSRGGVIDEEALLEALKSGKLAGAALDVFENEPPP--GSKLLELPNVSLTPHI 278
                         250
                  ....*....|....*....
gi 1285015877 317 AfysdASATELREMAASEI 335
Cdd:cd05303   279 G----ASTKEAQERIGEEL 293
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
36-342 1.86e-73

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: 232.96  E-value: 1.86e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  36 RDCSIEMPILKDV-ATVAFCDAQSTSEIHEKVLNEAVGALMWHTIILTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELG 114
Cdd:cd01619    11 DELEIEKEILKAGgVDVEIVTYLLNDDETAELAKGADAILTAFTDKIDAELLDKAPGLKFISLRATGYDNIDLDYAKELG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 115 IAVCNVPGYGVEEVADTTLCLILNLYRRTfwLANMVREGKKftgpeQVREAAQGCARIRGDTLGIVGLGRIGSAVALRAK 194
Cdd:cd01619    91 IGVTNVPEYSPNAVAEHTIALILALLRNR--KYIDERDKNQ-----DLQDAGVIGRELEDQTVGVVGTGKIGRAVAQRAK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 195 AFGFNVIFYDPYLPDGIEKSlGLTRVyTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDA 274
Cdd:cd01619   164 GFGMKVIAYDPFRNPELEDK-GVKYV-SLEELFKNSDIISLHVPLTPENHHMINEEAFKLMKKGVIIINTARGSLVDTEA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 275 LAQALKQGRIRAAALDVHENE-------------PYNVFAgPLKDAPNLLCTPHAAFYSDASATELREMAASEIRRAITG 341
Cdd:cd01619   242 LIEALDSGKIFGAGLDVLEDEtpdllkdlegeifKDALNA-LLGRRPNVIITPHTAFYTDDALKNMVEISCENIVDFLEG 320

                  .
gi 1285015877 342 R 342
Cdd:cd01619   321 E 321
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
89-341 3.08e-70

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: 224.73  E-value: 3.08e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  89 FKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRtFWLANM-VREGKKftGPEQVREAAQ 167
Cdd:cd12168    74 PPSLKIIAHAGAGYDQIDVDALTKRGIQVSNTPGAVDEATADTALFLILGALRN-FSRAERsARAGKW--RGFLDLTLAH 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 168 GCariRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPY-LPDGIEKSLGlTRVYTLQDLLFQSDCVSLHCTLNEHNHHV 246
Cdd:cd12168   151 DP---RGKTLGILGLGGIGKAIARKAAAFGMKIIYHNRSrLPEELEKALA-TYYVSLDELLAQSDVVSLNCPLTAATRHL 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 247 INEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPynVFAGPLKDAPNLLCTPHAAFYSDASATE 326
Cdd:cd12168   227 INKKEFAKMKDGVIIVNTARGAVIDEDALVDALESGKVASAGLDVFENEP--EVNPGLLKMPNVTLLPHMGTLTVETQEK 304
                         250
                  ....*....|....*
gi 1285015877 327 LREMAASEIRRAITG 341
Cdd:cd12168   305 MEELVLENIEAFLET 319
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
133-317 3.34e-68

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: 214.28  E-value: 3.34e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 133 LCLILNLYRRTFWLANMVREGKkFTGPEQVReaaqgCARIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGIE 212
Cdd:pfam02826   1 LALLLALARRIPEADRQVRAGR-WASPDALL-----GRELSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 213 KSLGLTRVYTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVH 292
Cdd:pfam02826  75 EEELGARYVSLDELLAESDVVSLHLPLTPETRHLINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDVF 154
                         170       180
                  ....*....|....*....|....*
gi 1285015877 293 ENEPYnVFAGPLKDAPNLLCTPHAA 317
Cdd:pfam02826 155 EPEPL-PADHPLLDLPNVILTPHIA 178
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
61-337 4.97e-67

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: 215.86  E-value: 4.97e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  61 EIHEKVLNEAVGA--LMWHTIILTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILN 138
Cdd:cd12171    35 EPEEELLEALKDAdiLITHFAPVTKKVIEAAPKLKLIGVCRGGPENVDVEAATERGIPVLNTPGRNAEAVAEFTVGLMLA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 139 LYRRTFWLANMVREGK--------KFTGPEqvreaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDG 210
Cdd:cd12171   115 ETRNIARAHAALKDGEwrkdyynyDGYGPE-----------LRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVYDPYVDPE 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 211 IEKSLGLTRVyTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALD 290
Cdd:cd12171   184 KIEADGVKKV-SLEELLKRSDVVSLHARLTPETRGMIGAEEFALMKPTAYFINTARAGLVDEDALIEALEEGKIGGAALD 262
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1285015877 291 VHENEPynVFAG-PLKDAPNLLCTPHAAFYSDASATELREMAASEIRR 337
Cdd:cd12171   263 VFPEEP--LPADhPLLKLDNVTLTPHIAGATRDVAERSPEIIAEELKR 308
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
31-349 1.57e-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: 240654 [Multi-domain]  Cd Length: 321  Bit Score: 215.26  E-value: 1.57e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  31 ALLDGRDCSIEMPILKDVATVAFCDAQSTseIHEKVLNEAvgaLMWHTII-------LTKEDLEKFKTLRIIVRIGSGVD 103
Cdd:cd12177     7 SSSFGQYFPEHIQRLKKIGYVDRFEVPPD--ISGKALAEK---LKGYDIIiasvtpnFDKEFFEYNDGLKLIARHGIGYD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 104 NIDVKAAGELGIAVCNVPGYG-VEEVADTTLCLILNLYRRTFWLANMVREGK-----KFTGPEqvreaaqgcarIRGDTL 177
Cdd:cd12177    82 NVDLKAATEHGVIVTRVPGAVeRDAVAEHAVALILTVLRKINQASEAVKEGKwteraNFVGHE-----------LSGKTV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 178 GIVGLGRIGSAVA-LRAKAFGFNVIFYDPYLPDGIEKSLGLTRVyTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMR 256
Cdd:cd12177   151 GIIGYGNIGSRVAeILKEGFNAKVLAYDPYVSEEVIKKKGAKPV-SLEELLAESDIISLHAPLTEETYHMINEKAFSKMK 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 257 PGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPYNVfAGPLKDAPNLLCTPHAAFYSDASATELREMAASEIR 336
Cdd:cd12177   230 KGVILVNTARGELIDEEALIEALKSGKIAGAGLDVLEEEPIKA-DHPLLHYENVVITPHIGAYTYESLYGMGEKVVDDIE 308
                         330
                  ....*....|...
gi 1285015877 337 RAITGRIPECLRN 349
Cdd:cd12177   309 DFLAGKEPKGILN 321
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
84-352 6.20e-66

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: 212.81  E-value: 6.20e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  84 EDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTF----WLANM--------VR 151
Cdd:cd12174    43 HDMDFAPSLKAIARAGAGVNNIDVDAASKRGIVVFNTPGANANAVAELVIAMMLALSRNIIqaikWVTNGdgddiskgVE 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 152 EGKK-FTGPEqvreaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGIEKSLG--LTRVYTLQDLLF 228
Cdd:cd12174   123 KGKKqFVGTE-----------LRGKTLGVIGLGNIGRLVANAALALGMKVIGYDPYLSVEAAWKLSveVQRVTSLEELLA 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 229 QSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEpynvfagPLKDAP 308
Cdd:cd12174   192 TADYITLHVPLTDETRGLINAELLAKMKPGAILLNFARGEIVDEEALLEALDEGKLGGYVTDFPEPA-------LLGHLP 264
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1285015877 309 NLLCTPHAAfysdASATELRE----MAASEIRRAI-TGRIPeclrNCVN 352
Cdd:cd12174   265 NVIATPHLG----ASTEEAEEncavMAARQIMDFLeTGNIT----NSVN 305
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
81-352 6.88e-66

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: 219.50  E-value: 6.88e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  81 LTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRtFWLANM-VREG----KK 155
Cdd:TIGR01327  52 VTEEVIAAAPKLKVIGRAGVGVDNIDIEAATARGILVVNAPTGNTISAAEHALAMLLAAARN-IPQADAsLKEGewdrKA 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 156 FTGPEqvreaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGIEKSLGLTRVYTLQDLLFQSDCVSL 235
Cdd:TIGR01327 131 FMGTE-----------LYGKTLGVIGLGRIGSIVAKRAKAFGMKVLAYDPYISPERAEQLGVELVDDLDELLARADFITV 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 236 HCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPYNvfAGPLKDAPNLLCTPH 315
Cdd:TIGR01327 200 HTPLTPETRGLIGAEELAKMKKGVIIVNCARGGIIDEAALYEALEEGHVRAAALDVFEKEPPT--DNPLFDLDNVIATPH 277
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1285015877 316 AAfysdASATELRE----MAASEIRRAITGripECLRNCVN 352
Cdd:TIGR01327 278 LG----ASTREAQEnvatQVAEQVLDALKG---LPVPNAVN 311
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
81-342 6.55e-64

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: 208.67  E-value: 6.55e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  81 LTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREG----KKF 156
Cdd:cd12187    53 LDAEVLEKLPRLKLIATRSTGFDHIDLEACRERGIAVCNVPDYGEATVAEHAFALLLALSRKLREAIERTRRGdfsqAGL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 157 TGPEqvreaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGIEKSLGLTRVyTLQDLLFQSDCVSLH 236
Cdd:cd12187   133 RGFE-----------LAGKTLGVVGTGRIGRRVARIARGFGMKVLAYDVVPDEELAERLGFRYV-SLEELLQESDIISLH 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 237 CTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEP----------YNVFAGPLKD 306
Cdd:cd12187   201 VPYTPQTHHLINRENFALMKPGAVLINTARGAVVDTEALVRALKEGKLAGAGLDVLEQEEvlreeaelfrEDVSPEDLKK 280
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1285015877 307 A---------PNLLCTPHAAFYSDASATELREMAASEIRRAITGR 342
Cdd:cd12187   281 LladhallrkPNVIITPHVAYNTKEALERILDTTVENIKAFAAGQ 325
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
81-342 7.93e-64

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: 207.84  E-value: 7.93e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  81 LTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREGKK---FT 157
Cdd:cd12161    59 LPGEVIEACKNLKMISVAFTGVDHVDLEACKERGITVSNAAGYSTEAVAELTIGLAIDLLRNIVPCDAAVRAGGTkagLI 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 158 GPEqvreaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGIeKSLGLTRVyTLQDLLFQSDCVSLHC 237
Cdd:cd12161   139 GRE-----------LAGKTVGIVGTGAIGLRVARLFKAFGCKVLAYSRSEKEEA-KALGIEYV-SLDELLAESDIVSLHL 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 238 TLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPYNVFAGPLKDAPNLLCTPHAA 317
Cdd:cd12161   206 PLNDETKGLIGKEKLALMKESAILINTARGPVVDNEALADALNEGKIAGAGIDVFDMEPPLPADYPLLHAPNTILTPHVA 285
                         250       260
                  ....*....|....*....|....*
gi 1285015877 318 FYSDASATELREMAASEIRRAITGR 342
Cdd:cd12161   286 FATEEAMEKRAEIVFDNIEAWLAGK 310
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
77-345 4.72e-62

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: 203.54  E-value: 4.72e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  77 HTIILTKEDLEKFK-------TLRIIvrigsGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANM 149
Cdd:cd12186    52 QTLPYDEEVYEKLAeygikqiALRSA-----GVDMIDLDLAKENGLKITNVPAYSPRAIAEFAVTQALNLLRNTPEIDRR 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 150 VREGK-KFTGPEQVREaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGIEKsLGLTRVyTLQDLLF 228
Cdd:cd12186   127 VAKGDfRWAPGLIGRE-------IRDLTVGIIGTGRIGSAAAKIFKGFGAKVIAYDPYPNPELEK-FLLYYD-SLEDLLK 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 229 QSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENE----PYNVFAGPL 304
Cdd:cd12186   198 QADIISLHVPLTKENHHLINAEAFAKMKDGAILVNAARGGLVDTKALIDALDSGKIAGAALDTYENEtgyfNKDWSGKEI 277
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1285015877 305 KDA--------PNLLCTPHAAFYSDASATELREMAASEIRRAITGRIPE 345
Cdd:cd12186   278 EDEvlkeliamPNVLITPHIAFYTDTAVKNMVEISLDDALEIIEGGTSE 326
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
30-341 2.86e-60

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 198.67  E-value: 2.86e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  30 VALLDGR---DCSIEmpILKDVATVAFCDAQSTSEIHEKVLNEAVgaLMWHTIILTKEDLEKFKTLRIIVRIGSGVDNID 106
Cdd:PRK08410    3 IVILDAKtlgDKDLS--VFEEFGDFQIYPTTSPEEVIERIKDANI--IITNKVVIDKEVLSQLPNLKLICITATGTNNVD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 107 VKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREGK-----KFTGPEQVREaaqgcaRIRGDTLGIVG 181
Cdd:PRK08410   79 IEYAKKKGIAVKNVAGYSTESVAQHTFAMLLSLLGRINYYDRYVKSGEysespIFTHISRPLG------EIKGKKWGIIG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 182 LGRIGSAVALRAKAFGFNVIFYDPylpDGIEKSLGLTRVyTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFL 261
Cdd:PRK08410  153 LGTIGKRVAKIAQAFGAKVVYYST---SGKNKNEEYERV-SLEELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGAIL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 262 VNTARGGLVDDDALAQALKQGRIrAAALDVHENEP---YNVFAGPlKDAPNLLCTPHAAFYSDASATELREMAASEIRRA 338
Cdd:PRK08410  229 INVGRGGIVNEKDLAKALDEKDI-YAGLDVLEKEPmekNHPLLSI-KNKEKLLITPHIAWASKEARKTLIEKVKENIKDF 306

                  ...
gi 1285015877 339 ITG 341
Cdd:PRK08410  307 LEG 309
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
101-319 4.16e-60

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: 198.44  E-value: 4.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 101 GVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREG----KKFTGPEqvreaaqgcarIRGDT 176
Cdd:cd12183    78 GFNNVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKIHRAYNRVREGnfslDGLLGFD-----------LHGKT 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 177 LGIVGLGRIGSAVALRAKAFGFNVIFYDPYlPDGIEKSLGLTRVyTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMR 256
Cdd:cd12183   147 VGVIGTGKIGQAFARILKGFGCRVLAYDPY-PNPELAKLGVEYV-DLDELLAESDIISLHCPLTPETHHLINAETIAKMK 224
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1285015877 257 PGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPYNVFAG----PLKDA--------PNLLCTPHAAFY 319
Cdd:cd12183   225 DGVMLINTSRGGLIDTKALIEALKSGKIGGLGLDVYEEEAGLFFEDhsdeIIQDDvlarllsfPNVLITGHQAFF 299
PRK06487 PRK06487
2-hydroxyacid dehydrogenase;
55-342 3.81e-57

2-hydroxyacid dehydrogenase;


Pssm-ID: 180588 [Multi-domain]  Cd Length: 317  Bit Score: 190.68  E-value: 3.81e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  55 DAQSTSEIHEKvLNEAVGALMwHTIILTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLC 134
Cdd:PRK06487   32 DATTPEQVAER-LRGAQVAIS-NKVALDAAALAAAPQLKLILVAATGTNNVDLAAARERGITVCNCQGYGTPSVAQHTLA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 135 LILNLYRRTFWLANMVREGkkftgpeQVREAAQ------GCARIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYD---- 204
Cdd:PRK06487  110 LLLALATRLPDYQQAVAAG-------RWQQSSQfclldfPIVELEGKTLGLLGHGELGGAVARLAEAFGMRVLIGQlpgr 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 205 PYLPDGIEkslgltrvytLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRI 284
Cdd:PRK06487  183 PARPDRLP----------LDELLPQVDALTLHCPLTEHTRHLIGARELALMKPGALLINTARGGLVDEQALADALRSGHL 252
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 285 RAAALDVHENEPyNVFAGPL--KDAPNLLCTPHAAFYSDASATELREMAASEIRRAITGR 342
Cdd:PRK06487  253 GGAATDVLSVEP-PVNGNPLlaPDIPRLIVTPHSAWGSREARQRIVGQLAENARAFFAGK 311
PRK13243 PRK13243
glyoxylate reductase; Reviewed
83-354 6.23e-57

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 190.39  E-value: 6.23e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  83 KEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREG--------- 153
Cdd:PRK13243   59 CEVFEAAPRLRIVANYAVGYDNIDVEEATRRGIYVTNTPGVLTEATADFAWALLLATARRLVEADHFVRSGewkrrgvaw 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 154 --KKFTGPEqvreaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGIEKSLGLTRVyTLQDLLFQSD 231
Cdd:PRK13243  139 hpLMFLGYD-----------VYGKTIGIIGFGRIGQAVARRAKGFGMRILYYSRTRKPEAEKELGAEYR-PLEELLRESD 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 232 CVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPYNvfAGPLKDAPNLL 311
Cdd:PRK13243  207 FVSLHVPLTKETYHMINEERLKLMKPTAILVNTARGKVVDTKALVKALKEGWIAGAGLDVFEEEPYY--NEELFSLKNVV 284
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1285015877 312 CTPHAAFYSDASATELREMAASEIRRAITGRIPECLrncVNKE 354
Cdd:PRK13243  285 LAPHIGSATFEAREGMAELVAENLIAFKRGEVPPTL---VNRE 324
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
86-318 8.00e-57

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: 189.26  E-value: 8.00e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  86 LEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGyGVEEVADTTLCLILNLYRRTFWLANMVREGkkftgPEQVREA 165
Cdd:cd12169    64 LERLPNLKLLVTTGMRNASIDLAAAKERGIVVCGTGG-GPTATAELTWALILALARNLPEEDAALRAG-----GWQTTLG 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 166 AQgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGIEKSLGLTRVYTLQDLLFQSDCVSLHCTLNEHNHH 245
Cdd:cd12169   138 TG----LAGKTLGIVGLGRIGARVARIGQAFGMRVIAWSSNLTAERAAAAGVEAAVSKEELFATSDVVSLHLVLSDRTRG 213
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1285015877 246 VINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPynVFAG-PLKDAPNLLCTPHAAF 318
Cdd:cd12169   214 LVGAEDLALMKPTALLVNTSRGPLVDEGALLAALRAGRIAGAALDVFDVEP--LPADhPLRGLPNVLLTPHIGY 285
HGDH_LDH_like cd12185
Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, ...
77-336 2.73e-54

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: 183.18  E-value: 2.73e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  77 HTIILTKEDLEKFKTL-------RIIvrigsGVDNIDVKAAGELGIAVCNVPgYGVEEVADTTLCLILNLYRRTFWLanM 149
Cdd:cd12185    52 GKSKISAELLEKLKEAgvkyistRSI-----GYDHIDLDAAKELGIKVSNVT-YSPNSVADYTVMLMLMALRKYKQI--M 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 150 VR-EGKKFT-GPEQVREaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGIEKslGLTRVyTLQDLL 227
Cdd:cd12185   124 KRaEVNDYSlGGLQGRE-------LRNLTVGVIGTGRIGQAVIKNLSGFGCKILAYDPYPNEEVKK--YAEYV-DLDTLY 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 228 FQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEP---YNVFAGP- 303
Cdd:cd12185   194 KESDIITLHTPLTEETYHLINKESIAKMKDGVIIINTARGELIDTEALIEGLESGKIGGAALDVIEGEDgiyYNDRKGDi 273
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1285015877 304 --------LKDAPNLLCTPHAAFYSDASateLREMAASEIR 336
Cdd:cd12185   274 lsnrelaiLRSFPNVILTPHMAFYTDQA---VSDMVENSIE 311
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
76-356 2.61e-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: 180.84  E-value: 2.61e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  76 WHTIILTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREGKK 155
Cdd:cd12167    57 WGTPPLDAELLARAPRLRAVVHAAGSVRGLVTDAVWERGILVTSAADANAEPVAEFTLAAILLALRRIPRFAAAYRAGRD 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 156 FTGPEQVreaaqGCARIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGIEKSLGLTRVyTLQDLLFQSDCVSL 235
Cdd:cd12167   137 WGWPTRR-----GGRGLYGRTVGIVGFGRIGRAVVELLRPFGLRVLVYDPYLPAAEAAALGVELV-SLDELLARSDVVSL 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 236 HCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRaAALDVHENEPynVFAG-PLKDAPNLLCTP 314
Cdd:cd12167   211 HAPLTPETRGMIDARLLALMRDGATFINTARGALVDEAALLAELRSGRLR-AALDVTDPEP--LPPDsPLRTLPNVLLTP 287
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1285015877 315 HAAfysDASATELR---EMAASEIRRAITGRIPEClrnCVNKEYF 356
Cdd:cd12167   288 HIA---GSTGDERRrlgDYALDELERFLAGEPLLH---EVTPERL 326
PRK06932 PRK06932
2-hydroxyacid dehydrogenase;
79-335 3.47e-53

2-hydroxyacid dehydrogenase;


Pssm-ID: 235890 [Multi-domain]  Cd Length: 314  Bit Score: 180.00  E-value: 3.47e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  79 IILTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRtfwLANMVRE--GKKF 156
Cdd:PRK06932   53 VLFTRETLAQLPKLKLIAITATGTNNVDLVAAKELGIAVKNVTGYSSTTVPEHVLGMIFALKHS---LMGWYRDqlSDRW 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 157 TGPEQVREAAQGCARIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDpylpdgiEKSLGLTRV-YT-LQDLLFQSDCVS 234
Cdd:PRK06932  130 ATCKQFCYFDYPITDVRGSTLGVFGKGCLGTEVGRLAQALGMKVLYAE-------HKGASVCREgYTpFEEVLKQADIVT 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 235 LHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEP---YNVFAGPLKDAPNLL 311
Cdd:PRK06932  203 LHCPLTETTQNLINAETLALMKPTAFLINTGRGPLVDEQALLDALENGKIAGAALDVLVKEPpekDNPLIQAAKRLPNLL 282
                         250       260
                  ....*....|....*....|....
gi 1285015877 312 CTPHAAFYSDASATELREMAASEI 335
Cdd:PRK06932  283 ITPHIAWASDSAVTTLVNKVAQNI 306
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
69-331 3.33e-50

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: 171.88  E-value: 3.33e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  69 EAVGALMWHTIILTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLAN 148
Cdd:cd12156    42 RIRAVVTNGETGLSAALIAALPALELIASFGVGYDGIDLDAARARGIRVTNTPGVLTDDVADLAVGLLLAVLRRIPAADR 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 149 MVREGKKFTGPEQVReaaqgcARIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGieksLGLTRVYTLQDLLF 228
Cdd:cd12156   122 FVRAGRWPKGAFPLT------RKVSGKRVGIVGLGRIGRAIARRLEAFGMEIAYHGRRPKPD----VPYRYYASLLELAA 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 229 QSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPyNVFAGpLKDAP 308
Cdd:cd12156   192 ESDVLVVACPGGPATRHLVNAEVLEALGPDGVLVNVARGSVVDEAALIAALQEGRIAGAGLDVFENEP-NVPAA-LLDLD 269
                         250       260
                  ....*....|....*....|....*
gi 1285015877 309 NLLCTPHAafysdASATE--LREMA 331
Cdd:cd12156   270 NVVLTPHI-----ASATVetRRAMG 289
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
81-315 2.73e-49

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: 169.68  E-value: 2.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  81 LTKEDLEKFKTLriiVRIGS---GVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREGkkft 157
Cdd:cd12176    54 LTEEVLEAAPKL---LAIGCfciGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIIMLARRLPDRNAAAHRG---- 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 158 gpeQVREAAQGCARIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDpylpdgIEKSLGL---TRVYTLQDLLFQSDCVS 234
Cdd:cd12176   127 ---IWNKSATGSHEVRGKTLGIIGYGHIGSQLSVLAEALGMRVIFYD------IAEKLPLgnaRQVSSLEELLAEADFVT 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 235 LHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPYN---VFAGPLKDAPNLL 311
Cdd:cd12176   198 LHVPATPSTKNMIGAEEIAQMKKGAILINASRGTVVDIDALAEALRSGHLAGAAVDVFPEEPASngePFSSPLQGLPNVI 277

                  ....
gi 1285015877 312 CTPH 315
Cdd:cd12176   278 LTPH 281
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
81-315 1.62e-47

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: 166.35  E-value: 1.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  81 LTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRrtfwlaNMVregkkfTGPE 160
Cdd:cd05302    74 MTAERIAKAKNLKLALTAGIGSDHVDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILVR------NYV------PGHE 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 161 QVREAA---QGCAR----IRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPY-LPDGIEKSLGLTRVYTLQDLLFQSDC 232
Cdd:cd05302   142 QAIEGGwnvADVVKraydLEGKTVGTVGAGRIGLRVLRRLKPFDVHLLYYDRHrLPEEVEKELGLTRHADLEDMVSKCDV 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 233 VSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPynvfAG---PLKDAPN 309
Cdd:cd05302   222 VTINCPLHPETEGLFNKELLSKMKKGAYLVNTARGKICDREAVAEALESGHLAGYAGDVWFPQP----APkdhPWRTMPN 297

                  ....*.
gi 1285015877 310 LLCTPH 315
Cdd:cd05302   298 NAMTPH 303
PRK11790 PRK11790
phosphoglycerate dehydrogenase;
81-315 9.53e-46

phosphoglycerate dehydrogenase;


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 163.04  E-value: 9.53e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  81 LTKEDLEKFKTLriiVRIGS---GVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREGK--K 155
Cdd:PRK11790   65 LTEEVLAAAEKL---VAIGCfciGTNQVDLDAAAKRGIPVFNAPFSNTRSVAELVIGEIILLLRGIPEKNAKAHRGGwnK 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 156 ftgpeqvreAAQGCARIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDpylpdgIEKSLGL---TRVYTLQDLLFQSDC 232
Cdd:PRK11790  142 ---------SAAGSFEVRGKTLGIVGYGHIGTQLSVLAESLGMRVYFYD------IEDKLPLgnaRQVGSLEELLAQSDV 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 233 VSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPY---NVFAGPLKDAPN 309
Cdd:PRK11790  207 VSLHVPETPSTKNMIGAEELALMKPGAILINASRGTVVDIDALADALKSGHLAGAAIDVFPVEPKsngDPFESPLRGLDN 286

                  ....*.
gi 1285015877 310 LLCTPH 315
Cdd:PRK11790  287 VILTPH 292
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
80-329 2.77e-45

(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: 159.77  E-value: 2.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  80 ILTKEDLEKFKTLRI---IVRIgSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREgKKF 156
Cdd:cd12184    55 FADKENLEIYKEYGIkyvFTRT-VGFNHIDLEAAKELGFKMARVPSYSPNAIAELAFTLAMTLSRHTAYTASRTAN-KNF 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 157 TgpeqvrEAAQGCAR-IRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGIEKSLglTRVyTLQDLLFQSDCVSL 235
Cdd:cd12184   133 K------VDPFMFSKeIRNSTVGIIGTGRIGLTAAKLFKGLGAKVIGYDIYPSDAAKDVV--TFV-SLDELLKKSDIISL 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 236 HCT-LNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENE-------------PYNVFA 301
Cdd:cd12184   204 HVPyIKGKNDKLINKEFISKMKDGAILINTARGELQDEEAILEALESGKLAGFGTDVLNNEkeiffkdfdgdkiEDPVVE 283
                         250       260
                  ....*....|....*....|....*...
gi 1285015877 302 GPLKDAPNLLCTPHAAFYSDASATELRE 329
Cdd:cd12184   284 KLLDLYPRVLLTPHIGSYTDEALSNMIE 311
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
58-341 7.96e-45

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: 158.22  E-value: 7.96e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  58 STSEIHEKVLN-EAVGALMWHTIilTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLI 136
Cdd:cd12157    34 SREELLRRCKDaDGLMAFMPDRI--DADFLDACPRLKIIACALKGYDNFDVEACTARGIWVTIVPDLLTEPTAELTIGLL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 137 LNLYRRTFWLANMVREGKkFTGPEQvREAAQGcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPY-LPDGIEKSL 215
Cdd:cd12157   112 IGLGRHILAGDRFVRSGK-FGGWRP-KFYGTG---LDGKTVGILGMGALGRAIARRLSGFGATLLYYDPHpLDQAEEQAL 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 216 GLTRVyTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENE 295
Cdd:cd12157   187 NLRRV-ELDELLESSDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRGSVVDEAAVAEALKSGHLGGYAADVFEME 265
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1285015877 296 -------PYNVFAGPLKDAPNLLCTPHAAFYSDASATELREMAASEIRRAITG 341
Cdd:cd12157   266 dwarpdrPRSIPQELLDQHDRTVFTPHIGSAVDEVRLEIELEAALNILQALQG 318
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
78-344 9.95e-43

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: 152.40  E-value: 9.95e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  78 TIILTKED-LEKFKTLRIIVRIGSGVDNIDVKAAGElGIAVCNVPGYGvEEVADTTLCLILNLYRRTFWLANMVREGKkf 156
Cdd:cd12165    46 GGRLTKEEaLAALKRLKLIQVPSAGVDHLPLERLPE-GVVVANNHGNS-PAVAEHALALILALAKRIVEYDNDLRRGI-- 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 157 tgPEQVREAAQGCARIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYD--PYLPDGIEKSLGLTRvytLQDLLFQSDCVS 234
Cdd:cd12165   122 --WHGRAGEEPESKELRGKTVGILGYGHIGREIARLLKAFGMRVIGVSrsPKEDEGADFVGTLSD---LDEALEQADVVV 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 235 LHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDV--HENEPYNVFAG---PLKDAPN 309
Cdd:cd12165   197 VALPLTKQTRGLIGAAELAAMKPGAILVNVGRGPVVDEEALYEALKERPIAGAAIDVwwRYPSRGDPVAPsryPFHELPN 276
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1285015877 310 LLCTPHAAFYSDASATELREMAASEIRRAITGRIP 344
Cdd:cd12165   277 VIMSPHNAGWTEETFRRRIDEAAENIRRYLRGEPL 311
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
83-338 2.22e-42

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: 151.29  E-value: 2.22e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  83 KEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREGKkftgpeQV 162
Cdd:cd12179    54 KEFIEKATNLKFIARAGAGLENIDLEYAKEKGIELFNAPEGNRDAVGEHALGMLLALFNKLNRADQEVRNGI------WD 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 163 REAAQGcARIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDpylpdgIEKSLGLTRV--YTLQDLLFQSDCVSLHCTLN 240
Cdd:cd12179   128 REGNRG-VELMGKTVGIIGYGNMGKAFAKRLSGFGCKVIAYD------KYKNFGDAYAeqVSLETLFKEADILSLHIPLT 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 241 EHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEP---YNVFAGP-----LKDAPNLLC 312
Cdd:cd12179   201 PETRGMVNKEFISSFKKPFYFINTARGKVVVTKDLVKALKSGKILGACLDVLEYEKasfESIFNQPeafeyLIKSPKVIL 280
                         250       260
                  ....*....|....*....|....*.
gi 1285015877 313 TPHAAFYSDASATELREMAASEIRRA 338
Cdd:cd12179   281 TPHIAGWTFESYEKIAEVLVDKIKAL 306
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
98-320 3.91e-42

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: 151.91  E-value: 3.91e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  98 IGS---GVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLanmvregkkftgpeqvreaaqgcarIRG 174
Cdd:cd12158    61 VGTatiGTDHIDTDYLKERGIGFANAPGCNANSVAEYVLSALLVLAQRQGFS-------------------------LKG 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 175 DTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDgIEKSLGLTrvyTLQDLLFQSDCVSLHCTLN---EHN-HHVINEF 250
Cdd:cd12158   116 KTVGIVGVGNVGSRLARRLEALGMNVLLCDPPRAE-AEGDPGFV---SLEELLAEADIITLHVPLTrdgEHPtYHLLDED 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 251 TIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPyNVFAGPLKDApnLLCTPHAAFYS 320
Cdd:cd12158   192 FLAALKPGQILINASRGAVIDNQALLALLQRGKDLRVVLDVWENEP-EIDLELLDKV--DIATPHIAGYS 258
PRK07574 PRK07574
NAD-dependent formate dehydrogenase;
81-291 4.08e-42

NAD-dependent formate dehydrogenase;


Pssm-ID: 181041  Cd Length: 385  Bit Score: 152.91  E-value: 4.08e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  81 LTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRrtfwlaNMVregkkfTGPE 160
Cdd:PRK07574  104 LTAERIAKAPNLKLAITAGIGSDHVDLQAASEHGITVAEVTGSNSISVAEHVVMMILALVR------NYE------PSHR 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 161 QVREA----AQGCAR---IRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPY-LPDGIEKSLGLTRVYTLQDLLFQSDC 232
Cdd:PRK07574  172 QAVEGgwniADCVSRsydLEGMTVGIVGAGRIGLAVLRRLKPFDVKLHYTDRHrLPEEVEQELGLTYHVSFDSLVSVCDV 251
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1285015877 233 VSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDV 291
Cdd:PRK07574  252 VTIHCPLHPETEHLFDADVLSRMKRGSYLVNTARGKIVDRDAVVRALESGHLAGYAGDV 310
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
69-354 1.29e-40

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: 146.90  E-value: 1.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  69 EAVGALMWHTIILT----KEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPG-YGvEEVADTTLCLILNLYRRT 143
Cdd:cd05300    33 ELTEELADADVLLGnpplPELLPAAPRLRWIQSTSAGVDALLFPELLERDVVLTNARGiFG-PPIAEYVLGYMLAFARKL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 144 FWLANMVREgKKFTGPEQVREaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIfydpylpdGI-----EKSLGLT 218
Cdd:cd05300   112 PRYARNQAE-RRWQRRGPVRE-------LAGKTVLIVGLGDIGREIARRAKAFGMRVI--------GVrrsgrPAPPVVD 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 219 RVYT---LQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENE 295
Cdd:cd05300   176 EVYTpdeLDELLPEADYVVNALPLTPETRGLFNAERFAAMKPGAVLINVGRGSVVDEDALIEALESGRIAGAALDVFEEE 255
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 296 PYNvfAG-PLKDAPNLLCTPHAAFYSDASATELREMAASEIRRAITGripECLRNCVNKE 354
Cdd:cd05300   256 PLP--ADsPLWDLPNVIITPHISGDSPSYPERVVEIFLENLRRYLAG---EPLLNVVDKD 310
PRK15409 PRK15409
glyoxylate/hydroxypyruvate reductase GhrB;
59-352 5.14e-40

glyoxylate/hydroxypyruvate reductase GhrB;


Pssm-ID: 185307  Cd Length: 323  Bit Score: 145.67  E-value: 5.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  59 TSEIHEKVLNEAVGAL-MWHTIilTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLIL 137
Cdd:PRK15409   35 TVEQHAAAFAEAEGLLgSGEKV--DAALLEKMPKLRAASTISVGYDNFDVDALTARKILLMHTPTVLTETVADTLMALVL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 138 NLYRRTFWLANMVREG--KKFTGPEQVreaaqGCaRIRGDTLGIVGLGRIGSAVALRAKaFGFNV-IFYDPYLP-DGIEK 213
Cdd:PRK15409  113 STARRVVEVAERVKAGewTASIGPDWF-----GT-DVHHKTLGIVGMGRIGMALAQRAH-FGFNMpILYNARRHhKEAEE 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 214 SLGlTRVYTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHE 293
Cdd:PRK15409  186 RFN-ARYCDLDTLLQESDFVCIILPLTDETHHLFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFE 264
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1285015877 294 NEPYNVfAGPLKDAPNLLCTPHAafysdASAT-ELR-EMAASEIRR---AITGRIPEclrNCVN 352
Cdd:PRK15409  265 QEPLSV-DSPLLSLPNVVAVPHI-----GSAThETRyNMAACAVDNlidALQGKVEK---NCVN 319
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
48-331 8.62e-38

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 139.88  E-value: 8.62e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  48 VATVAFCDAQSTSEIHEkvLNEAVGALmwhtiiltkedLEKFKTLRIIVRiGSGVDNIDVKAAGELGIAVCNVPGYGVEE 127
Cdd:PRK08605   40 VEEVEGFDGLSLSQQIP--LSEAIYKL-----------LNELGIKQIAQR-SAGFDTYDLELATKYNLIISNVPSYSPES 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 128 VADTTLCLILNLYRRTFWLANMVREgKKFTGPEQVReaaqgcARIRGD-TLGIVGLGRIGSAVA-LRAKAFGFNVIFYDP 205
Cdd:PRK08605  106 IAEFTVTQAINLVRHFNQIQTKVRE-HDFRWEPPIL------SRSIKDlKVAVIGTGRIGLAVAkIFAKGYGSDVVAYDP 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 206 YLPDGIEKSLglTRVYTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIR 285
Cdd:PRK08605  179 FPNAKAATYV--DYKDTIEEAVEGADIVTLHMPATKYNHYLFNADLFKHFKKGAVFVNCARGSLVDTKALLDALDNGLIK 256
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1285015877 286 AAALDVHENE----PYNVFAGPLKDA--------PNLLCTPHAAFYSDASATELREMA 331
Cdd:PRK08605  257 GAALDTYEFErplfPSDQRGQTINDPlleslinrEDVILTPHIAFYTDAAVKNLIVDA 314
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
76-321 1.41e-34

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: 130.78  E-value: 1.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  76 WHTIILTKeDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMvREGKK 155
Cdd:cd12155    46 YNPDFDEL-DLAKMKNLKWIQLYSAGVDYLPLEYIKKKGILLTNNSGIHSIPIAEWIVGYILEIYKGLKKAYKN-QKEKK 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 156 FTGPEQVREaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIfydpylpdGIEKS----LGLTRVYTLQDL---LF 228
Cdd:cd12155   124 WKMDSSLLE-------LYGKTILFLGTGSIGQEIAKRLKAFGMKVI--------GVNTSgrdvEYFDKCYPLEELdevLK 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 229 QSDCV--SLHCTlnEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPYNVfAGPLKD 306
Cdd:cd12155   189 EADIVvnVLPLT--EETHHLFDEAFFEQMKKGALFINVGRGPSVDEDALIEALKNKQIRGAALDVFEEEPLPK-DSPLWD 265
                         250
                  ....*....|....*
gi 1285015877 307 APNLLCTPHAAFYSD 321
Cdd:cd12155   266 LDNVLITPHISGVSE 280
2-Hacid_dh_15 cd12180
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
126-342 6.09e-34

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: 129.00  E-value: 6.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 126 EEVADTTLCLILNLYRRtfwlanmvREGKKFTGPEQVReaAQGCARIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDP 205
Cdd:cd12180    97 EAIAEFVLAAILAAAKR--------LPEIWVKGAEQWR--REPLGSLAGSTLGIVGFGAIGQALARRALALGMRVLALRR 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 206 ylPDGIEKSLGLTRVYTLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIR 285
Cdd:cd12180   167 --SGRPSDVPGVEAAADLAELFARSDHLVLAAPLTPETRHLINADVLAQAKPGLHLINIARGGLVDQEALLEALDSGRIS 244
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1285015877 286 AAALDVHENEPynVFAG-PLKDAPNLLCTPHAAFYSDASATELREMAASEIRRAITGR 342
Cdd:cd12180   245 LASLDVTDPEP--LPEGhPLYTHPRVRLSPHTSAIAPDGRRNLADRFLENLARYRAGQ 300
PLN02306 PLN02306
hydroxypyruvate reductase
101-341 3.76e-32

hydroxypyruvate reductase


Pssm-ID: 177941  Cd Length: 386  Bit Score: 125.74  E-value: 3.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 101 GVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREGKK-------FTGpeqvreaaqgcARIR 173
Cdd:PLN02306   96 GYNNVDVEAANKYGIAVGNTPGVLTETTAELAASLSLAAARRIVEADEFMRAGLYegwlphlFVG-----------NLLK 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 174 GDTLGIVGLGRIGSAVA-LRAKAFGFNVIFYDPYLPDGIEKSLGL---------------TRVYTLQDLLFQSDCVSLHC 237
Cdd:PLN02306  165 GQTVGVIGAGRIGSAYArMMVEGFKMNLIYYDLYQSTRLEKFVTAygqflkangeqpvtwKRASSMEEVLREADVISLHP 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 238 TLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPYnvFAGPLKDAPNLLCTPHAA 317
Cdd:PLN02306  245 VLDKTTYHLINKERLALMKKEAVLVNASRGPVIDEVALVEHLKANPMFRVGLDVFEDEPY--MKPGLADMKNAVVVPHIA 322
                         250       260
                  ....*....|....*....|....
gi 1285015877 318 FYSDASATELREMAASEIRRAITG 341
Cdd:PLN02306  323 SASKWTREGMATLAALNVLGKLKG 346
PLN02928 PLN02928
oxidoreductase family protein
81-344 3.88e-31

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 122.10  E-value: 3.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  81 LTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGV---EEVADTTLCLILNLYRRTFWLANMVReGKKFT 157
Cdd:PLN02928   72 LDADIIARASQMKLIMQFGVGLEGVDVDAATKHGIKVARIPSEGTgnaASCAEMAIYLMLGLLRKQNEMQISLK-ARRLG 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 158 GPEQVReaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGIEKSLGLT------------RVYTLQD 225
Cdd:PLN02928  151 EPIGDT--------LFGKTVFILGYGAIGIELAKRLRPFGVKLLATRRSWTSEPEDGLLIPngdvddlvdekgGHEDIYE 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 226 LLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPYNVfAGPLK 305
Cdd:PLN02928  223 FAGEADIVVLCCTLTKETAGIVNDEFLSSMKKGALLVNIARGGLLDYDAVLAALESGHLGGLAIDVAWSEPFDP-DDPIL 301
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1285015877 306 DAPNLLCTPHAAFYSDASATELREMAASEIRRAITGRIP 344
Cdd:PLN02928  302 KHPNVIITPHVAGVTEYSYRSMGKIVGDAALQLHAGRPL 340
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
86-329 3.50e-30

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 119.25  E-value: 3.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  86 LEKFKTLRIIVRIgSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREgKKFTGPEQVREA 165
Cdd:PRK12480   65 LESYGIKQIAQRT-AGFDMYDLDLAKKHNIVISNVPSYSPETIAEYSVSIALQLVRRFPDIERRVQA-HDFTWQAEIMSK 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 166 AqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYlPDgieKSLG-LTRVYTLQDLLFQSDCVSLHCTLNEHNH 244
Cdd:PRK12480  143 P-----VKNMTVAIIGTGRIGAATAKIYAGFGATITAYDAY-PN---KDLDfLTYKDSVKEAIKDADIISLHVPANKESY 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 245 HVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENE-PYNVFAGPLKDA-----------PNLLC 312
Cdd:PRK12480  214 HLFDKAMFDHVKKGAILVNAARGAVINTPDLIAAVNDGTLLGAAIDTYENEaAYFTNDWTNKDIddktlleliehERILV 293
                         250
                  ....*....|....*..
gi 1285015877 313 TPHAAFYSDASATELRE 329
Cdd:PRK12480  294 TPHIAFFSDEAVQNLVE 310
PLN03139 PLN03139
formate dehydrogenase; Provisional
76-315 1.38e-29

formate dehydrogenase; Provisional


Pssm-ID: 178684  Cd Length: 386  Bit Score: 118.41  E-value: 1.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  76 WHTIILTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREGKk 155
Cdd:PLN03139  106 FHPAYVTAERIKKAKNLELLLTAGIGSDHIDLPAAAAAGLTVAEVTGSNVVSVAEDELMRILILLRNFLPGYHQVVSGE- 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 156 ftgpEQVREAAQGCARIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPY-LPDGIEKSLGLTRVYTLQDLLFQSDCVS 234
Cdd:PLN03139  185 ----WNVAGIAYRAYDLEGKTVGTVGAGRIGRLLLQRLKPFNCNLLYHDRLkMDPELEKETGAKFEEDLDAMLPKCDVVV 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 235 LHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPynvfAG---PLKDAPNLL 311
Cdd:PLN03139  261 INTPLTEKTRGMFNKERIAKMKKGVLIVNNARGAIMDTQAVADACSSGHIGGYGGDVWYPQP----APkdhPWRYMPNHA 336

                  ....
gi 1285015877 312 CTPH 315
Cdd:PLN03139  337 MTPH 340
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
84-345 1.09e-26

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: 108.83  E-value: 1.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  84 EDLEKFKTLRIIVRIGSGVDNIdVKAAGElGIAVCNvpGYGVEE--VADTTLCLILNLYRRTfwlanmvregkkftgPEQ 161
Cdd:cd12166    53 EALRALPRLRVVQTLSAGYDGV-LPLLPE-GVTLCN--ARGVHDasTAELAVALILASLRGL---------------PRF 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 162 VREAAQG-CARIRGDTLG-----IVGLGRIGSAVALRAKAFGFNVifydpylpdgiekslglTRVYT------------- 222
Cdd:cd12166   114 VRAQARGrWEPRRTPSLAdrrvlIVGYGSIGRAIERRLAPFEVRV-----------------TRVARtarpgeqvhgide 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 223 LQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRaAALDVHENEPYNVFAg 302
Cdd:cd12166   177 LPALLPEADVVVLIVPLTDETRGLVDAEFLARMPDGALLVNVARGPVVDTDALVAELASGRLR-AALDVTDPEPLPPGH- 254
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1285015877 303 PLKDAPNLLCTPHAAFYSDASATELREMAASEIRRAITGRIPE 345
Cdd:cd12166   255 PLWSAPGVLITPHVGGATPAFLPRAYALVRRQLRRYAAGEPLE 297
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
84-352 1.24e-25

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: 106.04  E-value: 1.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  84 EDLEKFKTLRIIVRIGSGVDNIDvKAAGELGIAVCNV--PGYGvEEVADTTLCLILNLYRRTF----------WLANMVR 151
Cdd:cd12164    51 GLLARLPNLKAIFSLGAGVDHLL-ADPDLPDVPIVRLvdPGLA-QGMAEYVLAAVLRLHRDMDryaaqqrrgvWKPLPQR 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 152 EgkkftgPEQVReaaqgcarirgdtLGIVGLGRIGSAVALRAKAFGFNVIFYD--PYLPDGIEKSLGLTRvytLQDLLFQ 229
Cdd:cd12164   129 P------AAERR-------------VGVLGLGELGAAVARRLAALGFPVSGWSrsPKDIEGVTCFHGEEG---LDAFLAQ 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 230 SDcvSLHCTL--NEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPYNVfAGPLKDA 307
Cdd:cd12164   187 TD--ILVCLLplTPETRGILNAELLARLPRGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEQEPLPA-DHPLWRH 263
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1285015877 308 PNLLCTPHAAfySDASATELREMAASEIRRAITGRIPEclrNCVN 352
Cdd:cd12164   264 PRVTVTPHIA--AITDPDSAAAQVAENIRRLEAGEPLP---NLVD 303
2-Hacid_dh_2 cd12159
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
114-317 6.06e-25

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


Pssm-ID: 240636  Cd Length: 303  Bit Score: 103.88  E-value: 6.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 114 GIAVCNVPGYGVEEVADTTLCLILNLYRRtfwLANMVRegkkfTGPEQVREAAQGCARIRGDTLGIVGLGRIGSAVALRA 193
Cdd:cd12159    73 GRRWTNAAGAYAETVAEHALALLLAGLRQ---LPARAR-----ATTWDPAEEDDLVTLLRGSTVAIVGAGGIGRALIPLL 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 194 KAFGFNVIFYD--PYLPDGIEKSLGLTRvytLQDLLFQSDCVSLHCTLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVD 271
Cdd:cd12159   145 APFGAKVIAVNrsGRPVEGADETVPADR---LDEVWPDADHVVLAAPLTPETRHLVDAAALAAMKPHAWLVNVARGPLVD 221
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1285015877 272 DDALAQALKQGRIRAAALDVHENEPynVFAG-PLKDAPNLLCTPHAA 317
Cdd:cd12159   222 TDALVDALRSGEIAGAALDVTDPEP--LPDGhPLWSLPNALITPHVA 266
PRK00257 PRK00257
4-phosphoerythronate dehydrogenase PdxB;
101-320 1.22e-24

4-phosphoerythronate dehydrogenase PdxB;


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 104.35  E-value: 1.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 101 GVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILNLYRRtfwlanmvrEGkkftgpeqvreaaqgcARIRGDTLGIV 180
Cdd:PRK00257   68 GTDHLDLDYFAEAGITWSSAPGCNARGVVDYVLGSLLTLAER---------EG----------------VDLAERTYGVV 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 181 GLGRIGSAVALRAKAFGFNVIFYDPylPDgiEKSLGLTRVYTLQDLLFQSDCVSLHCTLN-EHNH---HVINEFTIKQMR 256
Cdd:PRK00257  123 GAGHVGGRLVRVLRGLGWKVLVCDP--PR--QEAEGDGDFVSLERILEECDVISLHTPLTkEGEHptrHLLDEAFLASLR 198
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1285015877 257 PGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEP-YNVFAGPLKDapnlLCTPHAAFYS 320
Cdd:PRK00257  199 PGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWEGEPqIDLELADLCT----IATPHIAGYS 259
2-Hacid_dh_3 cd12160
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
92-342 1.74e-22

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: 97.06  E-value: 1.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  92 LRIIVRIGSGVDniDVKAAG-ELGIAVCNVPGYGVEEVADTTLCLILNLYRRTFWLANMVREGK---KFTGPEQVREAaQ 167
Cdd:cd12160    60 LRWVQALAAGPD--AVLAAGfAPEVAVTSGRGLHDGTVAEHTLALILAAVRRLDEMREAQREHRwagELGGLQPLRPA-G 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 168 GCARIRGDTLGIVGLGRIGSAVALRAKAFGFNVIfydpylpdGIEKSLGlTR----VYT---LQDLLFQSDCVSLHCTLN 240
Cdd:cd12160   137 RLTTLLGARVLIWGFGSIGQRLAPLLTALGARVT--------GVARSAG-ERagfpVVAedeLPELLPETDVLVMILPAT 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 241 EHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPYNVfAGPLKDAPNLLCTPHAAFYS 320
Cdd:cd12160   208 PSTAHALDAEVLAALPKHAWVVNVGRGATVDEDALVAALESGRLGGAALDVTATEPLPA-SSPLWDAPNLILTPHAAGGR 286
                         250       260
                  ....*....|....*....|..
gi 1285015877 321 DASATELremAASEIRRAITGR 342
Cdd:cd12160   287 PQGAEEL---IAENLRAFLAGG 305
2-Hacid_dh_5 cd12163
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
173-315 7.03e-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: 84.25  E-value: 7.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 173 RGDTLGIVGLGRIGSAVALRAKAFGFNVIFY-------------DPYL------PDGI--------EKSLGLTRVYTLQ- 224
Cdd:cd12163   132 VGKRVGILGYGSIGRQTARLAQALGMEVYAYtrsprptpesrkdDGYIvpgtgdPDGSipsawfsgTDKASLHEFLRQDl 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 225 DLLFqsdcVSLhcTLNEHNHHVIN--EFTIKQMRpGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPynVFAG 302
Cdd:cd12163   212 DLLV----VSL--PLTPATKHLLGaeEFEILAKR-KTFVSNIARGSLVDTDALVAALESGQIRGAALDVTDPEP--LPAD 282
                         170
                  ....*....|....
gi 1285015877 303 -PLKDAPNLLCTPH 315
Cdd:cd12163   283 hPLWSAPNVIITPH 296
PRK06436 PRK06436
2-hydroxyacid dehydrogenase;
79-354 5.94e-17

2-hydroxyacid dehydrogenase;


Pssm-ID: 235800 [Multi-domain]  Cd Length: 303  Bit Score: 81.08  E-value: 5.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  79 IILTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEeVADTTLCLILNLYRRTFWLANMVREGKKFTG 158
Cdd:PRK06436   37 AILIKGRYVPGKKTKMIQSLSAGVDHIDVSGIPENVVLCSNAGAYSIS-VAEHAFALLLAWAKNICENNYNMKNGNFKQS 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 159 PEQVreaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGiekslGLTRVY-TLQDLLFQSDCVSLHC 237
Cdd:PRK06436  116 PTKL---------LYNKSLGILGYGGIGRRVALLAKAFGMNIYAYTRSYVND-----GISSIYmEPEDIMKKSDFVLISL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 238 TLNEHNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEPyNVFAGPLKdapNLLCTPH-A 316
Cdd:PRK06436  182 PLTDETRGMINSKMLSLFRKGLAIINVARADVVDKNDMLNFLRNHNDKYYLSDVWWNEP-IITETNPD---NVILSPHvA 257
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1285015877 317 AFYSDASATELREMAASEIRRAITGRiPeclRNCVNKE 354
Cdd:PRK06436  258 GGMSGEIMQPAVALAFENIKNFFEGK-P---KNIVRKE 291
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
73-296 1.07e-15

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 78.02  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  73 ALMWHTIILTKEDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEEVADTTLCLILnlyrrtfwlanMVRE 152
Cdd:PRK15438   40 ALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLL-----------MLAE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 153 GKKFTgpeqvreaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPylPDGIEKSLGLTRvyTLQDLLFQSDC 232
Cdd:PRK15438  109 RDGFS--------------LHDRTVGIVGVGNVGRRLQARLEALGIKTLLCDP--PRADRGDEGDFR--SLDELVQEADI 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1285015877 233 VSLHCTLNEHNH----HVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKQGRIRAAALDVHENEP 296
Cdd:PRK15438  171 LTFHTPLFKDGPyktlHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEP 238
2-Hacid_dh_9 cd12170
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
57-317 1.87e-15

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: 76.57  E-value: 1.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  57 QSTSEIHEKVLNEAVGALMWHTIIlTKEDLEKFKTLRIIVRIGSGVD----NIDVKAAGELGIAVCNVPGYGVEEVADTT 132
Cdd:cd12170    35 ESDEEIIERIGDADCVLVSYTTQI-DEEVLEACPNIKYIGMCCSLYSeesaNVDIAAARENGITVTGIRDYGDEGVVEYV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 133 LC-LI--LNLYRRTFWLaNMVREgkkftgpeqvreaaqgcarIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYD-PYLP 208
Cdd:cd12170   114 ISeLIrlLHGFGGKQWK-EEPRE-------------------LTGLKVGIIGLGTTGQMIADALSFFGADVYYYSrTRKP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 209 DGIEKSLgltRVYTLQDLLFQSDCVSLHctLNEhNHHVINEFTIKQMRPGAFLVNTARGGLVDDDALAQALKqgriraaa 288
Cdd:cd12170   174 DAEAKGI---RYLPLNELLKTVDVICTC--LPK-NVILLGEEEFELLGDGKILFNTSLGPSFEVEALKKWLK-------- 239
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1285015877 289 ldvheNEPYNVF---------AGPLKDAPNLLCTPHAA 317
Cdd:cd12170   240 -----ASGYNIFdcdtagalgDEELLRYPNVICTNKSA 272
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
85-310 1.44e-13

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: 71.11  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  85 DLEKFKTLRIIVRIGSGVDNIDVK-AAGELGIAVCNVPGYGVEEVADTtlcLILNLYRRTFWLANMVREgkkftgpeQVR 163
Cdd:cd12154    81 ALIQKLGDRLLFTYTIGADHRDLTeALARAGLTAIAVEGVELPLLTSN---SIGAGELSVQFIARFLEV--------QQP 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 164 EAAQGCARIRGDTLGIVGLGRIGSAVALRAKAFGFNVIFYDPyLPDGIE--KSLGLTRVYTLQDLLFQSDCVSLHCTLNE 241
Cdd:cd12154   150 GRLGGAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDI-NVEALEqlEELGGKNVEELEEALAEADVIVTTTLLPG 228
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1285015877 242 HNHHVIN-EFTIKQMRPGAFLVNTARGGLVDDDAL-AQALKQGRIRAAALDVHENEPYNVFAGPLKDAPNL 310
Cdd:cd12154   229 KRAGILVpEELVEQMKPGSVIVNVAVGAVGCVQALhTQLLEEGHGVVHYGDVNMPGPGCAMGVPWDATLRL 299
ghrA PRK15469
glyoxylate/hydroxypyruvate reductase GhrA;
73-340 9.46e-10

glyoxylate/hydroxypyruvate reductase GhrA;


Pssm-ID: 185366  Cd Length: 312  Bit Score: 59.43  E-value: 9.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877  73 ALMWHTIIltkeDLEKFKTLRIIVRIGSGVDNIDVKAAGELGIAVCNVPGYGVEevaDTTLCL---------ILNLYRRT 143
Cdd:PRK15469   42 ALVWHPPV----EMLAGRDLKAVFALGAGVDSILSKLQAHPEMLDPSVPLFRLE---DTGMGEqmqeyavsqVLHWFRRF 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 144 FWLANMVREGKKFTGPEQVREAAqgcarirgdTLGIVGLGRIGSAVALRAKAFGFNVIFYD---PYLPdGIEKSLGL--- 217
Cdd:PRK15469  115 DDYQALQNSSHWQPLPEYHREDF---------TIGILGAGVLGSKVAQSLQTWGFPLRCWSrsrKSWP-GVQSFAGReel 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285015877 218 ------TRVytLQDLLFQS-DCVSlhctlnehnhhVINEFTIKQMRPGAFLVNTARG-GLVDDDALAqALKQGRIRAAAL 289
Cdd:PRK15469  185 saflsqTRV--LINLLPNTpETVG-----------IINQQLLEQLPDGAYLLNLARGvHVVEDDLLA-ALDSGKVKGAML 250
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1285015877 290 DVHENEPYNVfAGPLKDAPNLLCTPHAAfysdasATELREMAASEIRRAIT 340
Cdd:PRK15469  251 DVFSREPLPP-ESPLWQHPRVAITPHVA------AVTRPAEAVEYISRTIA 294
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
177-227 5.41e-03

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 38.58  E-value: 5.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1285015877 177 LGIVGLGRIGSAVALRAKAFGFNVIFYDPYlPDGIE--KSLGLTRVYTLQDLL 227
Cdd:PRK09599    3 LGMIGLGRMGGNMARRLLRGGHEVVGYDRN-PEAVEalAEEGATGADSLEELV 54
 
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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