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Conserved domains on  [gi|633955246|gb|KDD80612|]
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lactate dehydrogenase [Glaesserella parasuis ST4-2]

Protein Classification

2-hydroxyacid dehydrogenase( domain architecture ID 10187446)

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

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

Graphical summary

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List of domain hits

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

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


:

Pssm-ID: 240659  Cd Length: 328  Bit Score: 606.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   1 MKVAVFSTKNYDRKYLEIANQQYHFEFEFFDFMLNERTAKMAEGCDVVCIFVNDDGSRAVLEKLAKVGVKMIALRCASFN 80
Cdd:cd12183    1 MKIAVFSTKPYDREFFEAANEGYGHELTYFEERLTEETASLAKGFDAVCVFVNDDLDAPVLEKLAELGVKLIALRCAGFN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  81 NVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGLIGFNMYKRTVGVIGTGKIGIATT 160
Cdd:cd12183   81 NVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKIHRAYNRVREGNFSLDGLLGFDLHGKTVGVIGTGKIGQAFA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 161 RILKGFGMNILAFDPFKNPIVEEIGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDT 240
Cdd:cd12183  161 RILKGFGCRVLAYDPYPNPELAKLGVEYVDLDELLAESDIISLHCPLTPETHHLINAETIAKMKDGVMLINTSRGGLIDT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 241 PEAIKALKRRKIGALGMDVYENERDLFFEDKSNEVILDDVFRRLSSCHNVLLTGHQAFLTEEALMNISDVTLYNICCLQK 320
Cdd:cd12183  241 KALIEALKSGKIGGLGLDVYEEEAGLFFEDHSDEIIQDDVLARLLSFPNVLITGHQAFFTKEALTNIAETTLENLDDFEA 320


                 ....*...
gi 633955246 321 GGHCENQI 328
Cdd:cd12183  321 GKPLKNEV 328
 
Name Accession Description Interval E-value
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 1-328 0e+00

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


Pssm-ID: 240659  Cd Length: 328  Bit Score: 606.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   1 MKVAVFSTKNYDRKYLEIANQQYHFEFEFFDFMLNERTAKMAEGCDVVCIFVNDDGSRAVLEKLAKVGVKMIALRCASFN 80
Cdd:cd12183    1 MKIAVFSTKPYDREFFEAANEGYGHELTYFEERLTEETASLAKGFDAVCVFVNDDLDAPVLEKLAELGVKLIALRCAGFN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  81 NVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGLIGFNMYKRTVGVIGTGKIGIATT 160
Cdd:cd12183   81 NVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKIHRAYNRVREGNFSLDGLLGFDLHGKTVGVIGTGKIGQAFA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 161 RILKGFGMNILAFDPFKNPIVEEIGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDT 240
Cdd:cd12183  161 RILKGFGCRVLAYDPYPNPELAKLGVEYVDLDELLAESDIISLHCPLTPETHHLINAETIAKMKDGVMLINTSRGGLIDT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 241 PEAIKALKRRKIGALGMDVYENERDLFFEDKSNEVILDDVFRRLSSCHNVLLTGHQAFLTEEALMNISDVTLYNICCLQK 320
Cdd:cd12183  241 KALIEALKSGKIGGLGLDVYEEEAGLFFEDHSDEIIQDDVLARLLSFPNVLITGHQAFFTKEALTNIAETTLENLDDFEA 320


                 ....*...
gi 633955246 321 GGHCENQI 328
Cdd:cd12183  321 GKPLKNEV 328
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
 1-328 9.57e-133

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: 380.20  E-value: 9.57e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   1 MKVAVFSTKNYDRKYLEIANQQyHFEFEFFDF-MLNERTAKMAEGCDVVCIFVNDDGSRAVLEKLAkvGVKMIALRCASF 79
Cdd:COG1052    1 KPILVLDPRTLPDEVLERLEAE-HFEVTVYEDeTSPEELAERAAGADAVITNGKDPIDAEVLEALP--GLKLIANRGVGY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  80 NNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLE-GLIGFNMYKRTVGVIGTGKIGIA 158
Cdd:COG1052   78 DNIDLAAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSpGLLGRDLSGKTLGIIGLGRIGQA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 159 TTRILKGFGMNILAFDPFKNPIVEEIGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLI 238
Cdd:COG1052  158 VARRAKGFGMKVLYYDRSPKPEVAELGAEYVSLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARGGLV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 239 DTPEAIKALKRRKIGALGMDVYENErdlffedksnEVILDDvfrRLSSCHNVLLTGHQAFLTEEALMNISDVTLYNICCL 318
Cdd:COG1052  238 DEAALIEALKSGRIAGAGLDVFEEE----------PPPPDH---PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAF 304

                        330
                 ....*....|
gi 633955246 319 QKGGHCENQI 328
Cdd:COG1052  305 LAGEPPPNPV 314
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
 3-328 4.69e-97

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: 289.58  E-value: 4.69e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246    3 VAVFS-TKNYDRKYLEianqqyHFEFEFFDFMLNERTAKMAEGCDVVCIFVNDDGSRAVLEKLAKVgvKMIALRCASFNN 81
Cdd:pfam00389   1 VLILDpLSPEALELLK------EGEVEVHDELLTEELLEKAKDADALIVRSRTKVTAEVLEAAPKL--KVIGRAGVGVDN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   82 VDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGLIGFNMYKRTVGVIGTGKIGIATTR 161
Cdd:pfam00389  73 VDLDAATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLELYGKTLGVIGGGGIGGGVAA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  162 ILKGFGMNILAFDPFKNPIVEEIGAKYVTLDELYAKSdvitlhcpaTPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTP 241
Cdd:pfam00389 153 IAKAFGMGVVAYDPYPNPERAEAGGVEVLSLLLLLLD---------LPESDDVLTVNPLTTMKTGVIIINEARGMLKDAV 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  242 EAIKALKRRKIGALGMDVYENERDLFFEDKSNEVILDDVFRRLSSCHNVLLTGHQAFLTEEALMNISDVTLYNICCLQKG 321
Cdd:pfam00389 224 AIINAAGGGVIDEAALDALLEEGIAAAADLDVEEEPPPVDSPLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDG 303


                  ....*..
gi 633955246  322 GHCENQI 328
Cdd:pfam00389 304 GPPANAV 310
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
 2-328 6.90e-63

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 202.84  E-value: 6.90e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   2 KVAVFSTKNYDRKYLEIANQQYHFEFEFFDFMLNERTAKMAEGCDVVCIFVNDDGSRAVLEKLAKVGVKMIALRCASFNN 81
Cdd:PRK12480   3 KIMFFGTRDYEKEMALNWGKKNNVEVTTSKELLSSATVDQLKDYDGVTTMQFGKLENDVYPKLESYGIKQIAQRTAGFDM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  82 VDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGLIGFNMYKR-TVGVIGTGKIGIATT 160
Cdd:PRK12480  83 YDLDLAKKHNIVISNVPSYSPETIAEYSVSIALQLVRRFPDIERRVQAHDFTWQAEIMSKPVKNmTVAIIGTGRIGAATA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 161 RILKGFGMNILAFDPFKNPIVEEIGAKYvTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDT 240
Cdd:PRK12480 163 KIYAGFGATITAYDAYPNKDLDFLTYKD-SVKEAIKDADIISLHVPANKESYHLFDKAMFDHVKKGAILVNAARGAVINT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 241 PEAIKALKRRKIGALGMDVYENERDLFFEDKSNEVILDDVFRRLSSCHNVLLTGHQAFLTEEALMNISDVTLYNICCLQK 320
Cdd:PRK12480 242 PDLIAAVNDGTLLGAAIDTYENEAAYFTNDWTNKDIDDKTLLELIEHERILVTPHIAFFSDEAVQNLVEGGLNAALSVIN 321


                 ....*...
gi 633955246 321 GGHCENQI 328
Cdd:PRK12480 322 TGTCETRL 329
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
 58-308 1.35e-54

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: 186.38  E-value: 1.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   58 RAVLEKLAKVgvKMIALRCASFNNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGL 137
Cdd:TIGR01327  54 EEVIAAAPKL--KVIGRAGVGVDNIDIEAATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEGEWDRKAF 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  138 IGFNMYKRTVGVIGTGKIGIATTRILKGFGMNILAFDPFKNPIV-EEIGAKYV-TLDELYAKSDVITLHCPATPENYHLL 215
Cdd:TIGR01327 132 MGTELYGKTLGVIGLGRIGSIVAKRAKAFGMKVLAYDPYISPERaEQLGVELVdDLDELLARADFITVHTPLTPETRGLI 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  216 NKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENErdlffEDKSNEVILDDvfrrlsschNVLLTGH 295
Cdd:TIGR01327 212 GAEELAKMKKGVIIVNCARGGIIDEAALYEALEEGHVRAAALDVFEKE-----PPTDNPLFDLD---------NVIATPH 277

                         250
                  ....*....|...
gi 633955246  296 QAFLTEEALMNIS 308
Cdd:TIGR01327 278 LGASTREAQENVA 290
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
145-231 3.50e-03

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


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 37.43  E-value: 3.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   145 RTVGVIGTGKIGIATTRILKGFGMNilafdpfknPIVEEI-----------GAKYVTLDELYAKSDVItlhCPATpENYH 213
Cdd:smart00997  24 KNVVVAGYGDVGKGVAARLRGLGAR---------VIVTEIdpiraleaamdGFEVMKMEEAAKRADIF---VTAT-GNKD 90

                           90
                   ....*....|....*...
gi 633955246   214 LLNKEAFDKMKDGVMIIN 231
Cdd:smart00997  91 VITREHFRAMKDGAILAN 108
 
Name Accession Description Interval E-value
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 1-328 0e+00

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


Pssm-ID: 240659  Cd Length: 328  Bit Score: 606.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   1 MKVAVFSTKNYDRKYLEIANQQYHFEFEFFDFMLNERTAKMAEGCDVVCIFVNDDGSRAVLEKLAKVGVKMIALRCASFN 80
Cdd:cd12183    1 MKIAVFSTKPYDREFFEAANEGYGHELTYFEERLTEETASLAKGFDAVCVFVNDDLDAPVLEKLAELGVKLIALRCAGFN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  81 NVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGLIGFNMYKRTVGVIGTGKIGIATT 160
Cdd:cd12183   81 NVDLKAAKELGITVVRVPAYSPYAVAEHAVALLLALNRKIHRAYNRVREGNFSLDGLLGFDLHGKTVGVIGTGKIGQAFA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 161 RILKGFGMNILAFDPFKNPIVEEIGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDT 240
Cdd:cd12183  161 RILKGFGCRVLAYDPYPNPELAKLGVEYVDLDELLAESDIISLHCPLTPETHHLINAETIAKMKDGVMLINTSRGGLIDT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 241 PEAIKALKRRKIGALGMDVYENERDLFFEDKSNEVILDDVFRRLSSCHNVLLTGHQAFLTEEALMNISDVTLYNICCLQK 320
Cdd:cd12183  241 KALIEALKSGKIGGLGLDVYEEEAGLFFEDHSDEIIQDDVLARLLSFPNVLITGHQAFFTKEALTNIAETTLENLDDFEA 320


                 ....*...
gi 633955246 321 GGHCENQI 328
Cdd:cd12183  321 GKPLKNEV 328
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
 1-328 9.57e-133

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: 380.20  E-value: 9.57e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   1 MKVAVFSTKNYDRKYLEIANQQyHFEFEFFDF-MLNERTAKMAEGCDVVCIFVNDDGSRAVLEKLAkvGVKMIALRCASF 79
Cdd:COG1052    1 KPILVLDPRTLPDEVLERLEAE-HFEVTVYEDeTSPEELAERAAGADAVITNGKDPIDAEVLEALP--GLKLIANRGVGY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  80 NNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLE-GLIGFNMYKRTVGVIGTGKIGIA 158
Cdd:COG1052   78 DNIDLAAAKERGITVTNTPGYLTEAVAEHAVALLLALARRIVEADRRVRAGDWSWSpGLLGRDLSGKTLGIIGLGRIGQA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 159 TTRILKGFGMNILAFDPFKNPIVEEIGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLI 238
Cdd:COG1052  158 VARRAKGFGMKVLYYDRSPKPEVAELGAEYVSLDELLAESDIVSLHCPLTPETRHLINAEELALMKPGAILINTARGGLV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 239 DTPEAIKALKRRKIGALGMDVYENErdlffedksnEVILDDvfrRLSSCHNVLLTGHQAFLTEEALMNISDVTLYNICCL 318
Cdd:COG1052  238 DEAALIEALKSGRIAGAGLDVFEEE----------PPPPDH---PLLSLPNVVLTPHIASATEEAREAMAELALDNLLAF 304

                        330
                 ....*....|
gi 633955246 319 QKGGHCENQI 328
Cdd:COG1052  305 LAGEPPPNPV 314
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 1-324 1.74e-119

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: 346.98  E-value: 1.74e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   1 MKVAVFSTKNYDRKYLEIANQQYHFEFEFFDFMLN-ERTAKMAEGCDVVCIFVNDDGSRAVLEKLAkvGVKMIALRCASF 79
Cdd:cd01619    1 MKVLIYDYRDDELEIEKEILKAGGVDVEIVTYLLNdDETAELAKGADAILTAFTDKIDAELLDKAP--GLKFISLRATGY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  80 NNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGLIGFNMYKRTVGVIGTGKIGIAT 159
Cdd:cd01619   79 DNIDLDYAKELGIGVTNVPEYSPNAVAEHTIALILALLRNRKYIDERDKNQDLQDAGVIGRELEDQTVGVVGTGKIGRAV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 160 TRILKGFGMNILAFDPFKNPIVEEIGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLID 239
Cdd:cd01619  159 AQRAKGFGMKVIAYDPFRNPELEDKGVKYVSLEELFKNSDIISLHVPLTPENHHMINEEAFKLMKKGVIIINTARGSLVD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 240 TPEAIKALKRRKIGALGMDVYENERDLFFEDKSNEVILDDVFRRLSSCHNVLLTGHQAFLTEEALMNISDVTLYNICCLQ 319
Cdd:cd01619  239 TEALIEALDSGKIFGAGLDVLEDETPDLLKDLEGEIFKDALNALLGRRPNVIITPHTAFYTDDALKNMVEISCENIVDFL 318


                 ....*
gi 633955246 320 KGGHC 324
Cdd:cd01619  319 EGEEE 323
HGDH_LDH_like cd12185
Putative Lactate dehydrogenase and (R)-2-Hydroxyglutarate Dehydrogenase-like proteins, ...
 1-324 9.93e-119

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


Pssm-ID: 240661  Cd Length: 322  Bit Score: 344.96  E-value: 9.93e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   1 MKVAVFSTKNYDRKYLEIANQQYHFEFEFFDFMLNERTAKMAEGCDVVCIFVNDDGSRAVLEKLAKVGVKMIALRCASFN 80
Cdd:cd12185    1 MKIFAYGVRPDELEYFEKFAKEYNVEVTLTKEPLTLENAHLAEGYDGISILGKSKISAELLEKLKEAGVKYISTRSIGYD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  81 NVDIQAAKELGIQVVRVqAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGLIGFNMYKRTVGVIGTGKIGIATT 160
Cdd:cd12185   81 HIDLDAAKELGIKVSNV-TYSPNSVADYTVMLMLMALRKYKQIMKRAEVNDYSLGGLQGRELRNLTVGVIGTGRIGQAVI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 161 RILKGFGMNILAFDPFKNPIVEEIgAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDT 240
Cdd:cd12185  160 KNLSGFGCKILAYDPYPNEEVKKY-AEYVDLDTLYKESDIITLHTPLTEETYHLINKESIAKMKDGVIIINTARGELIDT 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 241 PEAIKALKRRKIGALGMDVYENERDLFFEDKSNEVILDDVFRRLSSCHNVLLTGHQAFLTEEALMNISDVTLYNICCLQK 320
Cdd:cd12185  239 EALIEGLESGKIGGAALDVIEGEDGIYYNDRKGDILSNRELAILRSFPNVILTPHMAFYTDQAVSDMVENSIESLVAFEK 318


                 ....
gi 633955246 321 GGHC 324
Cdd:cd12185  319 GGEN 322
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
 1-328 6.85e-115

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


Pssm-ID: 240662  Cd Length: 329  Bit Score: 335.27  E-value: 6.85e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   1 MKVAVFSTKNYDRKYLEIANQQYHFEFEFFDFMLNERTAKMAEGCDVVCIFVNDDGSRAVLEKLAKVGVKMIALRCASFN 80
Cdd:cd12186    1 MKILMYNVRDDEKPYIEEWAKEHPVEVDTTTELLTPETVDLAKGYDGVVVQQTLPYDEEVYEKLAEYGIKQIALRSAGVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  81 NVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLE-GLIGFNMYKRTVGVIGTGKIGIAT 159
Cdd:cd12186   81 MIDLDLAKENGLKITNVPAYSPRAIAEFAVTQALNLLRNTPEIDRRVAKGDFRWApGLIGREIRDLTVGIIGTGRIGSAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 160 TRILKGFGMNILAFDPFKNPIVEEIGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLID 239
Cdd:cd12186  161 AKIFKGFGAKVIAYDPYPNPELEKFLLYYDSLEDLLKQADIISLHVPLTKENHHLINAEAFAKMKDGAILVNAARGGLVD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 240 TPEAIKALKRRKIGALGMDVYENERDLFFEDKSNEVILDDVFRRLSSCHNVLLTGHQAFLTEEALMNISDVTLYNICCLQ 319
Cdd:cd12186  241 TKALIDALDSGKIAGAALDTYENETGYFNKDWSGKEIEDEVLKELIAMPNVLITPHIAFYTDTAVKNMVEISLDDALEII 320


                 ....*....
gi 633955246 320 KGGHCENQI 328
Cdd:cd12186  321 EGGTSENEV 329
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
 2-315 4.38e-102

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: 303.04  E-value: 4.38e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   2 KVAVFSTKNYDRKYLEiaNQQYHFEFEFFDFMLNERTAKMAEGCDVVCIFVNDDGSRAVLEKLAKVgvKMIALRCASFNN 81
Cdd:cd12187    1 KIVFFETEEWEQEYFQ--ELLPGHKVVFTSQELLDDNVEEFKDAEVISVFVYSRLDAEVLEKLPRL--KLIATRSTGFDH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  82 VDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGLIGFNMYKRTVGVIGTGKIGIATTR 161
Cdd:cd12187   77 IDLEACRERGIAVCNVPDYGEATVAEHAFALLLALSRKLREAIERTRRGDFSQAGLRGFELAGKTLGVVGTGRIGRRVAR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 162 ILKGFGMNILAFDPFKNPIVEEI-GAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDT 240
Cdd:cd12187  157 IARGFGMKVLAYDVVPDEELAERlGFRYVSLEELLQESDIISLHVPYTPQTHHLINRENFALMKPGAVLINTARGAVVDT 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 241 PEAIKALKRRKIGALGMDVYENERDL------FFEDKSNE----VILDDVFRRLSschNVLLTGHQAFLTEEALMNISDV 310
Cdd:cd12187  237 EALVRALKEGKLAGAGLDVLEQEEVLreeaelFREDVSPEdlkkLLADHALLRKP---NVIITPHVAYNTKEALERILDT 313


                 ....*
gi 633955246 311 TLYNI 315
Cdd:cd12187  314 TVENI 318
2-Hacid_dh pfam00389
D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; This family represents the ...
 3-328 4.69e-97

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: 289.58  E-value: 4.69e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246    3 VAVFS-TKNYDRKYLEianqqyHFEFEFFDFMLNERTAKMAEGCDVVCIFVNDDGSRAVLEKLAKVgvKMIALRCASFNN 81
Cdd:pfam00389   1 VLILDpLSPEALELLK------EGEVEVHDELLTEELLEKAKDADALIVRSRTKVTAEVLEAAPKL--KVIGRAGVGVDN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   82 VDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGLIGFNMYKRTVGVIGTGKIGIATTR 161
Cdd:pfam00389  73 VDLDAATERGILVTNAPGYNTESVAELTIGLILALARRIPEADASVREGKWKKSGLIGLELYGKTLGVIGGGGIGGGVAA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  162 ILKGFGMNILAFDPFKNPIVEEIGAKYVTLDELYAKSdvitlhcpaTPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTP 241
Cdd:pfam00389 153 IAKAFGMGVVAYDPYPNPERAEAGGVEVLSLLLLLLD---------LPESDDVLTVNPLTTMKTGVIIINEARGMLKDAV 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  242 EAIKALKRRKIGALGMDVYENERDLFFEDKSNEVILDDVFRRLSSCHNVLLTGHQAFLTEEALMNISDVTLYNICCLQKG 321
Cdd:pfam00389 224 AIINAAGGGVIDEAALDALLEEGIAAAADLDVEEEPPPVDSPLLDLPNVILTPHIGGATEEAQERIAEEAAENILAFLDG 303


                  ....*..
gi 633955246  322 GHCENQI 328
Cdd:pfam00389 304 GPPANAV 310
HGDH_like cd12184
(R)-2-Hydroxyglutarate Dehydrogenase and related dehydrogenases, NAD-binding and catalytic ...
 1-328 1.71e-89

(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: 270.70  E-value: 1.71e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   1 MKVAVFSTKNYDRKYLEIANQQYHFEFEFFDFMLNERTAKMAEGCDVVCIFVNDDGSRAVLEKLAKVGVKMIALRCASFN 80
Cdd:cd12184    1 MKIICYGVRPVEKPIFEKLNKKFGYDLTLVEEYLNDENVHLAKGHDAVIVRGNCFADKENLEIYKEYGIKYVFTRTVGFN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  81 NVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGligfNMYKR-----TVGVIGTGKI 155
Cdd:cd12184   81 HIDLEAAKELGFKMARVPSYSPNAIAELAFTLAMTLSRHTAYTASRTANKNFKVDP----FMFSKeirnsTVGIIGTGRI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 156 GIATTRILKGFGMNILAFDPFKNPIVEEIgAKYVTLDELYAKSDVITLHCPATP-ENYHLLNKEAFDKMKDGVMIINTSR 234
Cdd:cd12184  157 GLTAAKLFKGLGAKVIGYDIYPSDAAKDV-VTFVSLDELLKKSDIISLHVPYIKgKNDKLINKEFISKMKDGAILINTAR 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 235 GSLIDTPEAIKALKRRKIGALGMDVYENERDLFFEDKSNEVILDDVFRRLSSCH-NVLLTGHQAFLTEEALMNISDVTLY 313
Cdd:cd12184  236 GELQDEEAILEALESGKLAGFGTDVLNNEKEIFFKDFDGDKIEDPVVEKLLDLYpRVLLTPHIGSYTDEALSNMIETSYE 315

                        330
                 ....*....|....*
gi 633955246 314 NICCLQKGGHCENQI 328
Cdd:cd12184  316 NLKEYLETGDCKNKI 330
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
 15-318 7.35e-89

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


Pssm-ID: 240622 [Multi-domain]  Cd Length: 302  Bit Score: 268.34  E-value: 7.35e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  15 YLEIANQQYHFEFEFFDFMLNERTAKMAEGCDVVCIFVNDDGSRAVLEKLAKVgvKMIALRCASFNNVDIQAAKELGIQV 94
Cdd:cd05198   12 EALEALEATGFEVIVADDLLADELEALLADADALIVSSTTPVTAEVLAKAPKL--KFIQVAGAGVDNIDLDAAKKRGITV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  95 VRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSL-EGLIGFNMYKRTVGVIGTGKIGIATTRILKGFGMNILAF 173
Cdd:cd05198   90 TNVPGANAEAVAEHALGLLLALLRRLPRADAAVRRGWGWLwAGFPGYELEGKTVGIVGLGRIGQRVAKRLQAFGMKVLYY 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 174 DPFKNPIVEEI-GAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKI 252
Cdd:cd05198  170 DRTRKPEPEEDlGFRVVSLDELLAQSDVVVLHLPLTPETRHLINEEELALMKPGAVLVNTARGGLVDEDALLRALKSGKI 249

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 253 GALGMDVYENE----RDLFFEDKsnevilddvfrrlsschNVLLTGHQAFLTEEALMNISDVTLYNICCL 318
Cdd:cd05198  250 AGAALDVFEPEplpaDHPLLELP-----------------NVILTPHIAGYTEEARERMAEIAVENLERF 302
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
 1-328 1.69e-86

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: 262.44  E-value: 1.69e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   1 MKVAVfsTKNYDRKYLEIANQQYHFEFEFFDFMLNERTAKMAEGCDVVCIFVNDDGSRAVLEKLAKVgvKMIALRCASFN 80
Cdd:COG0111    1 MKILI--LDDLPPEALEALEAAPGIEVVYAPGLDEEELAEALADADALIVRSRTKVTAELLAAAPNL--KLIGRAGAGVD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  81 NVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGLIGFNMYKRTVGVIGTGKIGIATT 160
Cdd:COG0111   77 NIDLAAATERGIPVTNAPGANARAVAEYALALLLALARRLPEADRAQRAGRWDRSAFRGRELRGKTVGIVGLGRIGRAVA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 161 RILKGFGMNILAFDPFKNPI-VEEIGAKYV-TLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLI 238
Cdd:COG0111  157 RRLRAFGMRVLAYDPSPKPEeAADLGVGLVdSLDELLAEADVVSLHLPLTPETRGLIGAEELAAMKPGAILINTARGGVV 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 239 DTPEAIKALKRRKIGALGMDVYENErdlffedksnEVILDDVFRRLSschNVLLTGHQAFLTEEALMNISDVTLYNICCL 318
Cdd:COG0111  237 DEDALLAALDSGRLAGAALDVFEPE----------PLPADSPLWDLP---NVILTPHIAGSTEEAQERAARQVAENIRRF 303

                        330
                 ....*....|
gi 633955246 319 QKGGHCENQI 328
Cdd:COG0111  304 LAGEPLRNLV 313
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 2-315 1.32e-79

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: 244.70  E-value: 1.32e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   2 KVAVFST--KNYDRKYLEIANQQyHFEFEFFDF---MLNERTAKMAEGCDVVcIFVNDDGSRAVLEKL------AKVGVk 70
Cdd:cd12172    1 KVLVTPRsfSKYSEEAKELLEAA-GFEVVLNPLgrpLTEEELIELLKDADGV-IAGLDPITEEVLAAAprlkviSRYGV- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  71 mialrcaSFNNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSleGLIGFNMYKRTVGVI 150
Cdd:cd12172   78 -------GYDNIDLEAAKKRGIVVTNTPGANSNSVAELTIGLMLALARQIPQADREVRAGGWD--RPVGTELYGKTLGII 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 151 GTGKIGIATTRILKGFGMNILAFDPFKNP-IVEEIGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMI 229
Cdd:cd12172  149 GLGRIGKAVARRLSGFGMKVLAYDPYPDEeFAKEHGVEFVSLEELLKESDFISLHLPLTPETRHLINAAELALMKPGAIL 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 230 INTSRGSLIDTPEAIKALKRRKIGALGMDVYENERdlffedksnevilDDVFRRLSSCHNVLLTGHQAFLTEEALMNISD 309
Cdd:cd12172  229 INTARGGLVDEEALYEALKSGRIAGAALDVFEEEP-------------PPADSPLLELPNVILTPHIGASTKEAVLRMGT 295


                 ....*.
gi 633955246 310 VTLYNI 315
Cdd:cd12172  296 MAAQNV 301
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
 79-308 5.61e-74

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: 230.38  E-value: 5.61e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  79 FNNVDIQAAKELGIQVVrvqaYSPEA----VAEHTVGLMLTLNRRIHRAYQRTREANFSLEGLIGFNMYKRTVGVIGTGK 154
Cdd:cd12173   73 VDNIDVEAATARGILVV----NAPGAntisVAEHTIALMLALARNIPQADASLRAGKWDRKKFMGVELRGKTLGIVGLGR 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 155 IGIATTRILKGFGMNILAFDPFKNP-IVEEIGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTS 233
Cdd:cd12173  149 IGREVARRARAFGMKVLAYDPYISAeRAAAGGVELVSLDELLAEADFISLHTPLTPETRGLINAEELAKMKPGAILINTA 228

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 633955246 234 RGSLIDTPEAIKALKRRKIGALGMDVYENErdlffedksnEVILDDVFRRLSschNVLLTGHQAFLTEEALMNIS 308
Cdd:cd12173  229 RGGIVDEAALADALKSGKIAGAALDVFEQE----------PPPADSPLLGLP---NVILTPHLGASTEEAQERVA 290
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
 1-307 7.21e-74

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: 230.09  E-value: 7.21e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   1 MKVAV----FSTKNYDRKYLEIAnqqyhfEFEFFDFMLnERTAKMAE---GCDVVCIFVNDDGsRAVLEKLAKVgvKMIA 73
Cdd:cd05299    1 PKVVItdydFPDLDIEREVLEEA------GVELVDAQS-RTEDELIEaaaDADALLVQYAPVT-AEVIEALPRL--KVIV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  74 lRCAS-FNNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGLIGfnMYK---RTVGV 149
Cdd:cd05299   71 -RYGVgVDNVDVAAATERGIPVCNVPDYCTEEVADHALALILALARKLPFLDRAVRAGGWDWTVGGP--IRRlrgLTLGL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 150 IGTGKIGIATTRILKGFGMNILAFDPFKNPIVEEI-GAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVM 228
Cdd:cd05299  148 VGFGRIGRAVAKRAKAFGFRVIAYDPYVPDGVAALgGVRVVSLDELLARSDVVSLHCPLTPETRHLIDAEALALMKPGAF 227

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 633955246 229 IINTSRGSLIDTPEAIKALKRRKIGALGMDVYENErdlffedksnEVILDDVFRRLSschNVLLTGHQAFLTEEALMNI 307
Cdd:cd05299  228 LVNTARGGLVDEAALARALKSGRIAGAALDVLEEE----------PPPADSPLLSAP---NVILTPHAAWYSEESLAEL 293
2-Hacid_dh_11 cd12175
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 34-321 9.61e-72

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: 224.76  E-value: 9.61e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  34 LNERTAKMAEgCDVVCIFVNDDGSRAVLEKLAKVgvKMIALRCASFNNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLM 113
Cdd:cd12175   34 LDEEAALLAD-ADVLVPGMRKVIDAELLAAAPRL--RLIQQPGVGLDGVDLEAATARGIPVANIPGGNAESVAEHAVMLM 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 114 LTLNRRIHRAYQRTREAN-FSLEGLIGFNMYKRTVGVIGTGKIGIATTRILKGFGMNILAFDPFKNPIVEEI--GAKYVT 190
Cdd:cd12175  111 LALLRRLPEADRELRAGRwGRPEGRPSRELSGKTVGIVGLGNIGRAVARRLRGFGVEVIYYDRFRDPEAEEKdlGVRYVE 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 191 LDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENErdlffed 270
Cdd:cd12175  191 LDELLAESDVVSLHVPLTPETRHLIGAEELAAMKPGAILINTARGGLVDEEALLAALRSGHLAGAGLDVFWQE------- 263

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 633955246 271 ksnEVILDDVFRRLsscHNVLLTGHQAFLTEEALMNISDVTLYNICCLQKG 321
Cdd:cd12175  264 ---PLPPDDPLLRL---DNVILTPHIAGVTDESYQRMAAIVAENIARLLRG 308
2-Hacid_dh_4 cd12162
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 26-315 2.06e-70

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: 221.17  E-value: 2.06e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  26 EFEFFDFMLNERTAKMAEGCDVVciFVNDDG-SRAVLEKLAKVgvKMIALRCASFNNVDIQAAKELGIQVVRVQAYSPEA 104
Cdd:cd12162   26 ELTVYDRTSPEEVVERIKDADIV--ITNKVVlDAEVLAQLPNL--KLIGVLATGYNNVDLAAAKERGITVTNVPGYSTDS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 105 VAEHTVGLMLTLnRRIHRAYQRTREAN-------FS--------LEGligfnmykRTVGVIGTGKIGIATTRILKGFGMN 169
Cdd:cd12162  102 VAQHTFALLLAL-ARLVAYHNDVVKAGewqkspdFCfwdypiieLAG--------KTLGIIGYGNIGQAVARIARAFGMK 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 170 ILAFDPFKNPiveEIGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKR 249
Cdd:cd12162  173 VLFAERKGAP---PLREGYVSLDELLAQSDVISLHCPLTPETRNLINAEELAKMKPGAILINTARGGLVDEQALADALNS 249

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 633955246 250 RKIGALGMDVyenerdLFFEDKSNEVILddvfrrLSSCHNVLLTGHQAFLTEEALMNISDVTLYNI 315
Cdd:cd12162  250 GKIAGAGLDV------LSQEPPRADNPL------LKAAPNLIITPHIAWASREARQRLMDILVDNI 303
GDH cd05301
D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH); D-glycerate dehydrogenase (GDH, ...
 24-315 5.07e-70

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


Pssm-ID: 240626 [Multi-domain]  Cd Length: 309  Bit Score: 220.34  E-value: 5.07e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  24 HFEFEFFD---FMLNERTAKMAEGCDVVCIFVNDDGSRAVLEKLAKVgvKMIALRCASFNNVDIQAAKELGIQVvrvqAY 100
Cdd:cd05301   20 GFEVEVWDedrPLPREELLEAAKGADGLLCTLTDKIDAELLDAAPPL--KVIANYSVGYDHIDVDAAKARGIPV----TN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 101 SP----EAVAEHTVGLMLTLNRRIHRAYQRTREANF---SLEGLIGFNMYKRTVGVIGTGKIGIATTRILKGFGMNILAF 173
Cdd:cd05301   94 TPdvltDATADLAFALLLAAARRVVEGDRFVRAGEWkgwSPTLLLGTDLHGKTLGIVGMGRIGQAVARRAKGFGMKILYH 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 174 DPFKNPIVEE-IGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKI 252
Cdd:cd05301  174 NRSRKPEAEEeLGARYVSLDELLAESDFVSLHCPLTPETRHLINAERLALMKPTAILINTARGGVVDEDALVEALKSGKI 253

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 633955246 253 GALGMDVYENErdlffedksnEVILDDvfrRLSSCHNVLLTGHQAFLTEEALMNISDVTLYNI 315
Cdd:cd05301  254 AGAGLDVFEPE----------PLPADH---PLLTLPNVVLLPHIGSATVETRTAMAELAADNL 303
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 44-306 5.47e-66

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


Pssm-ID: 240648 [Multi-domain]  Cd Length: 310  Bit Score: 210.09  E-value: 5.47e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  44 GCDVvcIFVNDDG-SRAVLEKLAKVgvKMIA-LRcASFNNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIH 121
Cdd:cd12171   46 DADI--LITHFAPvTKKVIEAAPKL--KLIGvCR-GGPENVDVEAATERGIPVLNTPGRNAEAVAEFTVGLMLAETRNIA 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 122 RAYQRTRE----ANFSLEGLIGFNMYKRTVGVIGTGKIGIATTRILKGFGMNILAFDPFKNP-IVEEIGAKYVTLDELYA 196
Cdd:cd12171  121 RAHAALKDgewrKDYYNYDGYGPELRGKTVGIVGFGAIGRRVAKRLKAFGAEVLVYDPYVDPeKIEADGVKKVSLEELLK 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 197 KSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENErdlffedksnEVI 276
Cdd:cd12171  201 RSDVVSLHARLTPETRGMIGAEEFALMKPTAYFINTARAGLVDEDALIEALEEGKIGGAALDVFPEE----------PLP 270

                        250       260       270
                 ....*....|....*....|....*....|
gi 633955246 277 LDDVFRRLSschNVLLTGHQAFLTEEALMN 306
Cdd:cd12171  271 ADHPLLKLD---NVTLTPHIAGATRDVAER 297
2-Hacid_dh_13 cd12178
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 40-315 4.60e-65

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: 207.86  E-value: 4.60e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  40 KMAEGCDVVCIFVNDDGSRAVLEKLAKVgvKMIALRCASFNNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRR 119
Cdd:cd12178   39 ERIADYDALITPLSTPVDKEIIDAAKNL--KIIANYGAGFDNIDVDYAKEKGIPVTNTPAVSTEPTAELTFGLILALARR 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 120 IHRAYQRTREANFS----LEGLiGFNMYKRTVGVIGTGKIGIATTRILKGFGMNILAFDPFKNPIVEE--IGAKYVTLDE 193
Cdd:cd12178  117 IAEGDRLMRRGGFLgwapLFFL-GHELAGKTLGIIGMGRIGQAVARRAKAFGMKILYYNRHRLSEETEkeLGATYVDLDE 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 194 LYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENErdlffedksn 273
Cdd:cd12178  196 LLKESDFVSLHAPYTPETHHLIDAAAFKLMKPTAYLINAARGPLVDEKALVDALKTGEIAGAALDVFEFE---------- 265

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 633955246 274 evilDDVFRRLSSCHNVLLTGHQAFLTEEALMNISDVTLYNI 315
Cdd:cd12178  266 ----PEVSPELKKLDNVILTPHIGNATVEARDAMAKEAADNI 303
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 110-297 6.16e-65

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


Pssm-ID: 427007 [Multi-domain]  Cd Length: 178  Bit Score: 202.73  E-value: 6.16e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  110 VGLMLTLNRRIHRAYQRTREANFSLE-GLIGFNMYKRTVGVIGTGKIGIATTRILKGFGMNILAFDPFKNPIV--EEIGA 186
Cdd:pfam02826   1 LALLLALARRIPEADRQVRAGRWASPdALLGRELSGKTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEeeEELGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  187 KYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENERdl 266
Cdd:pfam02826  81 RYVSLDELLAESDVVSLHLPLTPETRHLINAERLALMKPGAILINTARGGLVDEDALIAALKSGRIAGAALDVFEPEP-- 158

                         170       180       190
                  ....*....|....*....|....*....|.
gi 633955246  267 ffedksnevILDDvfRRLSSCHNVLLTGHQA 297
Cdd:pfam02826 159 ---------LPAD--HPLLDLPNVILTPHIA 178
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
 70-315 6.93e-65

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: 207.01  E-value: 6.93e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  70 KMIAlRCAS-FNNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGLIGFNMYKRTVG 148
Cdd:cd05303   65 KIIA-RAGVgLDNIDVEYAKKKGIKVINTPGASSNSVAELVIGLMLSLARFIHRANREMKLGKWNKKKYKGIELRGKTLG 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 149 VIGTGKIGIATTRILKGFGMNILAFDPF-KNPIVEEIGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGV 227
Cdd:cd05303  144 IIGFGRIGREVAKIARALGMNVIAYDPYpKDEQAVELGVKTVSLEELLKNSDFISLHVPLTPETKHMINKKELELMKDGA 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 228 MIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENErdlffedksnevilDDVFRRLSSCHNVLLTGHQAFLTEEALMNI 307
Cdd:cd05303  224 IIINTSRGGVIDEEALLEALKSGKLAGAALDVFENE--------------PPPGSKLLELPNVSLTPHIGASTKEAQERI 289


                 ....*...
gi 633955246 308 SDVTLYNI 315
Cdd:cd05303  290 GEELANKI 297
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 28-263 2.02e-63

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: 203.71  E-value: 2.02e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  28 EFFDFMLNERTAKMAE---GCDVVCIFVNDDGSRAVLEklAKVGVKMIALRCASFNNVDIQAAKELGIQVVRVQ-AYSPE 103
Cdd:cd12177   28 DRFEVPPDISGKALAEklkGYDIIIASVTPNFDKEFFE--YNDGLKLIARHGIGYDNVDLKAATEHGVIVTRVPgAVERD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 104 AVAEHTVGLMLTLNRRIHRAYQRTREANFSLEG-LIGFNMYKRTVGVIGTGKIGIATTRILK-GFGMNILAFDPFKNP-I 180
Cdd:cd12177  106 AVAEHAVALILTVLRKINQASEAVKEGKWTERAnFVGHELSGKTVGIIGYGNIGSRVAEILKeGFNAKVLAYDPYVSEeV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 181 VEEIGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVY 260
Cdd:cd12177  186 IKKKGAKPVSLEELLAESDIISLHAPLTEETYHMINEKAFSKMKKGVILVNTARGELIDEEALIEALKSGKIAGAGLDVL 265


                 ...
gi 633955246 261 ENE 263
Cdd:cd12177  266 EEE 268
GDH_like_1 cd12161
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
 26-315 2.99e-63

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: 203.22  E-value: 2.99e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  26 EFEFFDfMLNERTAKMAE---GCDVVCIfVNDDGSRAVLEKLAKVgvKMIALRCASFNNVDIQAAKELGIQVVRVQAYSP 102
Cdd:cd12161   28 EFVYYD-TKTTDTAELIErskDADIVMI-ANMPLPGEVIEACKNL--KMISVAFTGVDHVDLEACKERGITVSNAAGYST 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 103 EAVAEHTVGLMLTLNRRIHRAYQRTREANFSlEGLIGFNMYKRTVGVIGTGKIGIATTRILKGFGMNILAFDPFKNPIVE 182
Cdd:cd12161  104 EAVAELTIGLAIDLLRNIVPCDAAVRAGGTK-AGLIGRELAGKTVGIVGTGAIGLRVARLFKAFGCKVLAYSRSEKEEAK 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 183 EIGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYEN 262
Cdd:cd12161  183 ALGIEYVSLDELLAESDIVSLHLPLNDETKGLIGKEKLALMKESAILINTARGPVVDNEALADALNEGKIAGAGIDVFDM 262

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 633955246 263 ERDLffedksnevildDVFRRLSSCHNVLLTGHQAFLTEEALMNISDVTLYNI 315
Cdd:cd12161  263 EPPL------------PADYPLLHAPNTILTPHVAFATEEAMEKRAEIVFDNI 303
PRK12480 PRK12480
D-lactate dehydrogenase; Provisional
 2-328 6.90e-63

D-lactate dehydrogenase; Provisional


Pssm-ID: 183550  Cd Length: 330  Bit Score: 202.84  E-value: 6.90e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   2 KVAVFSTKNYDRKYLEIANQQYHFEFEFFDFMLNERTAKMAEGCDVVCIFVNDDGSRAVLEKLAKVGVKMIALRCASFNN 81
Cdd:PRK12480   3 KIMFFGTRDYEKEMALNWGKKNNVEVTTSKELLSSATVDQLKDYDGVTTMQFGKLENDVYPKLESYGIKQIAQRTAGFDM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  82 VDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGLIGFNMYKR-TVGVIGTGKIGIATT 160
Cdd:PRK12480  83 YDLDLAKKHNIVISNVPSYSPETIAEYSVSIALQLVRRFPDIERRVQAHDFTWQAEIMSKPVKNmTVAIIGTGRIGAATA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 161 RILKGFGMNILAFDPFKNPIVEEIGAKYvTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDT 240
Cdd:PRK12480 163 KIYAGFGATITAYDAYPNKDLDFLTYKD-SVKEAIKDADIISLHVPANKESYHLFDKAMFDHVKKGAILVNAARGAVINT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 241 PEAIKALKRRKIGALGMDVYENERDLFFEDKSNEVILDDVFRRLSSCHNVLLTGHQAFLTEEALMNISDVTLYNICCLQK 320
Cdd:PRK12480 242 PDLIAAVNDGTLLGAAIDTYENEAAYFTNDWTNKDIDDKTLLELIEHERILVTPHIAFFSDEAVQNLVEGGLNAALSVIN 321


                 ....*...
gi 633955246 321 GGHCENQI 328
Cdd:PRK12480 322 TGTCETRL 329
PRK08605 PRK08605
D-lactate dehydrogenase; Validated
 1-307 1.53e-62

D-lactate dehydrogenase; Validated


Pssm-ID: 181499  Cd Length: 332  Bit Score: 201.90  E-value: 1.53e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   1 MKVAVFSTKNYDRKYLEIANQQYHFEFEFFDFMLNERTAKMAEGCDVVCIFVNDDGSRAVLEKLAKVGVKMIALRCASFN 80
Cdd:PRK08605   2 TKIKIMSVRDEDAPYIKAWAEKHHVEVDLTKEALTDDNVEEVEGFDGLSLSQQIPLSEAIYKLLNELGIKQIAQRSAGFD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  81 NVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGLI-GFNMYKRTVGVIGTGKIGIAT 159
Cdd:PRK08605  82 TYDLELATKYNLIISNVPSYSPESIAEFTVTQAINLVRHFNQIQTKVREHDFRWEPPIlSRSIKDLKVAVIGTGRIGLAV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 160 TRIL-KGFGMNILAFDPFKNPIVEEIGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLI 238
Cdd:PRK08605 162 AKIFaKGYGSDVVAYDPFPNAKAATYVDYKDTIEEAVEGADIVTLHMPATKYNHYLFNADLFKHFKKGAVFVNCARGSLV 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 633955246 239 DTPEAIKALKRRKIGALGMDVYENERDLFFEDKSNEVILDDVFRRLSSCHNVLLTGHQAFLTEEALMNI 307
Cdd:PRK08605 242 DTKALLDALDNGLIKGAALDTYEFERPLFPSDQRGQTINDPLLESLINREDVILTPHIAFYTDAAVKNL 310
PGDH TIGR01327
D-3-phosphoglycerate dehydrogenase; This model represents a long form of D-3-phosphoglycerate ...
 58-308 1.35e-54

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: 186.38  E-value: 1.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   58 RAVLEKLAKVgvKMIALRCASFNNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGL 137
Cdd:TIGR01327  54 EEVIAAAPKL--KVIGRAGVGVDNIDIEAATARGILVVNAPTGNTISAAEHALAMLLAAARNIPQADASLKEGEWDRKAF 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  138 IGFNMYKRTVGVIGTGKIGIATTRILKGFGMNILAFDPFKNPIV-EEIGAKYV-TLDELYAKSDVITLHCPATPENYHLL 215
Cdd:TIGR01327 132 MGTELYGKTLGVIGLGRIGSIVAKRAKAFGMKVLAYDPYISPERaEQLGVELVdDLDELLARADFITVHTPLTPETRGLI 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  216 NKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENErdlffEDKSNEVILDDvfrrlsschNVLLTGH 295
Cdd:TIGR01327 212 GAEELAKMKKGVIIVNCARGGIIDEAALYEALEEGHVRAAALDVFEKE-----PPTDNPLFDLD---------NVIATPH 277

                         250
                  ....*....|...
gi 633955246  296 QAFLTEEALMNIS 308
Cdd:TIGR01327 278 LGASTREAQENVA 290
Mand_dh_like cd12168
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ...
 68-322 8.45e-54

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: 178.90  E-value: 8.45e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  68 GVKMIALRCASFNNVDIQAAKELGIQVvrvqAYSPEAVAEHT--VGLMLTLN--RRIHRAYQRTREANFS--LEGLIGFN 141
Cdd:cd12168   76 SLKIIAHAGAGYDQIDVDALTKRGIQV----SNTPGAVDEATadTALFLILGalRNFSRAERSARAGKWRgfLDLTLAHD 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 142 MYKRTVGVIGTGKIGIATTRILKGFGMNILAFDPFKNPIVEE--IGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEA 219
Cdd:cd12168  152 PRGKTLGILGLGGIGKAIARKAAAFGMKIIYHNRSRLPEELEkaLATYYVSLDELLAQSDVVSLNCPLTAATRHLINKKE 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 220 FDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENErdlffedksnevilDDVFRRLSSCHNVLLTGHQAFL 299
Cdd:cd12168  232 FAKMKDGVIIVNTARGAVIDEDALVDALESGKVASAGLDVFENE--------------PEVNPGLLKMPNVTLLPHMGTL 297

                        250       260
                 ....*....|....*....|....
gi 633955246 300 TEEALMNISDVTLYNI-CCLQKGG 322
Cdd:cd12168  298 TVETQEKMEELVLENIeAFLETGK 321
PGDH_like_1 cd12169
Putative D-3-Phosphoglycerate Dehydrogenases; Phosphoglycerate dehydrogenases (PGDHs) catalyze ...
 43-315 2.16e-53

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: 177.32  E-value: 2.16e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  43 EGCDVVCI------FvnddgSRAVLEKLAKVgvKMIALRCASFNNVDIQAAKELGIQVVRVQaYSPEAVAEHTVGLMLTL 116
Cdd:cd12169   45 APFDAIVLmrertpF-----PAALLERLPNL--KLLVTTGMRNASIDLAAAKERGIVVCGTG-GGPTATAELTWALILAL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 117 NRRIHRAYQRTREANFSleGLIGFNMYKRTVGVIGTGKIGIATTRILKGFGMNILAFDPfkNPIVE---EIGAKY-VTLD 192
Cdd:cd12169  117 ARNLPEEDAALRAGGWQ--TTLGTGLAGKTLGIVGLGRIGARVARIGQAFGMRVIAWSS--NLTAEraaAAGVEAaVSKE 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 193 ELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENErdlffedks 272
Cdd:cd12169  193 ELFATSDVVSLHLVLSDRTRGLVGAEDLALMKPTALLVNTSRGPLVDEGALLAALRAGRIAGAALDVFDVE--------- 263

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 633955246 273 nEVILDDVFRRLSschNVLLTGHQAFLTEEALMNISDVTLYNI 315
Cdd:cd12169  264 -PLPADHPLRGLP---NVLLTPHIGYVTEEAYEGFYGQAVENI 302
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 81-321 5.81e-52

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: 174.29  E-value: 5.81e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  81 NVDiQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHR---AYQRTREANFSlEGLIGFNMYKRTVGVIGTGKIGI 157
Cdd:cd12167   86 LVT-DAVWERGILVTSAADANAEPVAEFTLAAILLALRRIPRfaaAYRAGRDWGWP-TRRGGRGLYGRTVGIVGFGRIGR 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 158 ATTRILKGFGMNILAFDPFKNP-IVEEIGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGS 236
Cdd:cd12167  164 AVVELLRPFGLRVLVYDPYLPAaEAAALGVELVSLDELLARSDVVSLHAPLTPETRGMIDARLLALMRDGATFINTARGA 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 237 LIDTPEAIKALKRRKIGALgMDVYENErdlffedksnEVILDDVFRRLSschNVLLTGHQAFLTEEALMNISDVTLYNIC 316
Cdd:cd12167  244 LVDEAALLAELRSGRLRAA-LDVTDPE----------PLPPDSPLRTLP---NVLLTPHIAGSTGDERRRLGDYALDELE 309


                 ....*
gi 633955246 317 CLQKG 321
Cdd:cd12167  310 RFLAG 314
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
 46-307 6.64e-49

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: 165.92  E-value: 6.64e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  46 DVVCIFVNDDGSRAVLEKLAKVgvKMIALRCASFNNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRA-- 123
Cdd:cd12157   46 DGLMAFMPDRIDADFLDACPRL--KIIACALKGYDNFDVEACTARGIWVTIVPDLLTEPTAELTIGLLIGLGRHILAGdr 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 124 YQRTREAN-----FSLEGLIGfnmykRTVGVIGTGKIGIATTRILKGFGMNILAFDPFKNPIVEE--IGAKYVTLDELYA 196
Cdd:cd12157  124 FVRSGKFGgwrpkFYGTGLDG-----KTVGILGMGALGRAIARRLSGFGATLLYYDPHPLDQAEEqaLNLRRVELDELLE 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 197 KSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENErDLFFEDKSNEVI 276
Cdd:cd12157  199 SSDFLVLALPLTPDTLHLINAEALAKMKPGALLVNPCRGSVVDEAAVAEALKSGHLGGYAADVFEME-DWARPDRPRSIP 277

                        250       260       270
                 ....*....|....*....|....*....|.
gi 633955246 277 LDdvfrRLSSCHNVLLTGHQAFLTEEALMNI 307
Cdd:cd12157  278 QE----LLDQHDRTVFTPHIGSAVDEVRLEI 304
2-Hacid_dh_14 cd12179
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 58-310 1.27e-47

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: 162.46  E-value: 1.27e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  58 RAVLEKLAKVgvKMIALRCASFNNVDIQAAKELGIQVVRvqaySPE----AVAEHTVGLMLTLNRRIHRAYQRTREANFS 133
Cdd:cd12179   54 KEFIEKATNL--KFIARAGAGLENIDLEYAKEKGIELFN----APEgnrdAVGEHALGMLLALFNKLNRADQEVRNGIWD 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 134 LEGLIGFNMYKRTVGVIGTGKIGIATTRILKGFGMNILAFDPFKNPIVEEigAKYVTLDELYAKSDVITLHCPATPENYH 213
Cdd:cd12179  128 REGNRGVELMGKTVGIIGYGNMGKAFAKRLSGFGCKVIAYDKYKNFGDAY--AEQVSLETLFKEADILSLHIPLTPETRG 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 214 LLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENERDLFFEDKSneviLDDVFRRLSSCHNVLLT 293
Cdd:cd12179  206 MVNKEFISSFKKPFYFINTARGKVVVTKDLVKALKSGKILGACLDVLEYEKASFESIFN----QPEAFEYLIKSPKVILT 281

                        250
                 ....*....|....*..
gi 633955246 294 GHQAFLTEEALMNISDV 310
Cdd:cd12179  282 PHIAGWTFESYEKIAEV 298
PRK13243 PRK13243
glyoxylate reductase; Reviewed
 1-321 6.57e-47

glyoxylate reductase; Reviewed


Pssm-ID: 183914  Cd Length: 333  Bit Score: 161.50  E-value: 6.57e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   1 MKVAVFSTKNYDRKYLEIANQqyHFEFEFFD---FMLNERTAKMAEGCDVVCIFVNDDGSRAVLEKLAKVgvKMIALRCA 77
Cdd:PRK13243   1 MKPKVFITREIPENGIEMLEE--HFEVEVWEderEIPREVLLEKVRDVDALVTMLSERIDCEVFEAAPRL--RIVANYAV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  78 SFNNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEG-------LIGFNMYKRTVGVI 150
Cdd:PRK13243  77 GYDNIDVEEATRRGIYVTNTPGVLTEATADFAWALLLATARRLVEADHFVRSGEWKRRGvawhplmFLGYDVYGKTIGII 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 151 GTGKIGIATTRILKGFGMNILAFDPFKNPIVE-EIGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMI 229
Cdd:PRK13243 157 GFGRIGQAVARRAKGFGMRILYYSRTRKPEAEkELGAEYRPLEELLRESDFVSLHVPLTKETYHMINEERLKLMKPTAIL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 230 INTSRGSLIDTPEAIKALKRRKIGALGMDVYENerdlffEDKSNEvilddvfrRLSSCHNVLLTGHQAFLTEEALMNISD 309
Cdd:PRK13243 237 VNTARGKVVDTKALVKALKEGWIAGAGLDVFEE------EPYYNE--------ELFSLKNVVLAPHIGSATFEAREGMAE 302

                        330
                 ....*....|..
gi 633955246 310 VTLYNICCLQKG 321
Cdd:PRK13243 303 LVAENLIAFKRG 314
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 68-271 5.94e-46

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: 158.11  E-value: 5.94e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  68 GVKMIAlRC-ASFNNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSL---------EGL 137
Cdd:cd12174   50 SLKAIA-RAgAGVNNIDVDAASKRGIVVFNTPGANANAVAELVIAMMLALSRNIIQAIKWVTNGDGDDiskgvekgkKQF 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 138 IGFNMYKRTVGVIGTGKIGIATTRILKGFGMNILAFDPFknPIVEE---IGAKYV---TLDELYAKSDVITLHCPATPEN 211
Cdd:cd12174  129 VGTELRGKTLGVIGLGNIGRLVANAALALGMKVIGYDPY--LSVEAawkLSVEVQrvtSLEELLATADYITLHVPLTDET 206

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 212 YHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGAlGMDVYENERDLFFEDK 271
Cdd:cd12174  207 RGLINAELLAKMKPGAILLNFARGEIVDEEALLEALDEGKLGG-YVTDFPEPALLGHLPN 265
HPPR cd12156
Hydroxy(phenyl)pyruvate Reductase, D-isomer-specific 2-hydroxyacid-related dehydrogenase; ...
 57-315 3.79e-44

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: 153.01  E-value: 3.79e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  57 SRAVLEKLAKVgvKMIALRCASFNNVDIQAAKELGIQVvrvqAYSP----EAVAEHTVGLMLTLNRRIHRAYQRTRE--- 129
Cdd:cd12156   55 SAALIAALPAL--ELIASFGVGYDGIDLDAARARGIRV----TNTPgvltDDVADLAVGLLLAVLRRIPAADRFVRAgrw 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 130 --ANFSLegliGFNMYKRTVGVIGTGKIGIATTRILKGFGMNILAFDPFKNPIVEeiGAKYVTLDELYAKSDVITLHCPA 207
Cdd:cd12156  129 pkGAFPL----TRKVSGKRVGIVGLGRIGRAIARRLEAFGMEIAYHGRRPKPDVP--YRYYASLLELAAESDVLVVACPG 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 208 TPENYHLLNKEAFDKM-KDGVmIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENErdlffedksnevilDDVFRRLSS 286
Cdd:cd12156  203 GPATRHLVNAEVLEALgPDGV-LVNVARGSVVDEAALIAALQEGRIAGAGLDVFENE--------------PNVPAALLD 267

                        250       260
                 ....*....|....*....|....*....
gi 633955246 287 CHNVLLTGHQAFLTEEALMNISDVTLYNI 315
Cdd:cd12156  268 LDNVVLTPHIASATVETRRAMGDLVLANL 296
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 1-326 2.96e-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: 151.24  E-value: 2.96e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   1 MKVAVfstkNYDRKYLEIANQQY-HFEFEFFDfmLNERTAKMA-EGCDV-VCIFVNDDGSRAVLEKLakvgvKMIALRCA 77
Cdd:cd12165    1 MKVLV----NFKAELREEFEAALeGLYAEVPE--LPDEAAEEAlEDADVlVGGRLTKEEALAALKRL-----KLIQVPSA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  78 SFNNVDIQAAKElGIQVVRVQAYSPeAVAEHTVGLMLTLNRRIHRAYQRTREANF---SLEGLIGFNMYKRTVGVIGTGK 154
Cdd:cd12165   70 GVDHLPLERLPE-GVVVANNHGNSP-AVAEHALALILALAKRIVEYDNDLRRGIWhgrAGEEPESKELRGKTVGILGYGH 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 155 IGIATTRILKGFGMNILAFDpfKNPIVEEIGAKYVT---LDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIIN 231
Cdd:cd12165  148 IGREIARLLKAFGMRVIGVS--RSPKEDEGADFVGTlsdLDEALEQADVVVVALPLTKQTRGLIGAAELAAMKPGAILVN 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 232 TSRGSLIDTPEAIKALKRRKIGALGMDVYENERdlffEDKSNEVILDDVFRRLsscHNVLLTGHQAFLTEEALMNISDVT 311
Cdd:cd12165  226 VGRGPVVDEEALYEALKERPIAGAAIDVWWRYP----SRGDPVAPSRYPFHEL---PNVIMSPHNAGWTEETFRRRIDEA 298

                        330
                 ....*....|....*
gi 633955246 312 LYNICCLQKGGHCEN 326
Cdd:cd12165  299 AENIRRYLRGEPLLN 313
PRK06932 PRK06932
2-hydroxyacid dehydrogenase;
1-315 1.34e-41

2-hydroxyacid dehydrogenase;


Pssm-ID: 235890 [Multi-domain]  Cd Length: 314  Bit Score: 146.87  E-value: 1.34e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   1 MKVaVFSTKNYDRKYLEIANQQYHFEFEFFDFMLNERTAKMAEGCDVV----CIFvnddgSRAVLEKLAKVgvKMIALRC 76
Cdd:PRK06932   2 MKI-VFLDSTAIPKHINIPRPSFPHEWIEYDHTSAEQTIERAKDADIVitskVLF-----TRETLAQLPKL--KLIAITA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  77 ASFNNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGLIGFNMYK------RTVGVI 150
Cdd:PRK06932  74 TGTNNVDLVAAKELGIAVKNVTGYSSTTVPEHVLGMIFALKHSLMGWYRDQLSDRWATCKQFCYFDYPitdvrgSTLGVF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 151 GTGKIGIATTRILKGFGMNILaFDPFKNpiVEEIGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMII 230
Cdd:PRK06932 154 GKGCLGTEVGRLAQALGMKVL-YAEHKG--ASVCREGYTPFEEVLKQADIVTLHCPLTETTQNLINAETLALMKPTAFLI 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 231 NTSRGSLIDTPEAIKALKRRKIGALGMDVYENERdlffEDKSNEVILddVFRRLSschNVLLTGHQAFLTEEALMNISDV 310
Cdd:PRK06932 231 NTGRGPLVDEQALLDALENGKIAGAALDVLVKEP----PEKDNPLIQ--AAKRLP---NLLITPHIAWASDSAVTTLVNK 301


                 ....*
gi 633955246 311 TLYNI 315
Cdd:PRK06932 302 VAQNI 306
FDH cd05302
NAD-dependent Formate Dehydrogenase (FDH); NAD-dependent formate dehydrogenase (FDH) catalyzes ...
 82-260 9.51e-41

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: 145.55  E-value: 9.51e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  82 VDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGlIGFNMYK---RTVGVIGTGKIGIA 158
Cdd:cd05302   98 VDLQAANDRGITVAEVTGSNVVSVAEHVVMMILILVRNYVPGHEQAIEGGWNVAD-VVKRAYDlegKTVGTVGAGRIGLR 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 159 TTRILKGFGMNILAFDPFKNP--IVEEIGAKYV-TLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRG 235
Cdd:cd05302  177 VLRRLKPFDVHLLYYDRHRLPeeVEKELGLTRHaDLEDMVSKCDVVTINCPLHPETEGLFNKELLSKMKKGAYLVNTARG 256

                        170       180
                 ....*....|....*....|....*
gi 633955246 236 SLIDTPEAIKALKRRKIGALGMDVY 260
Cdd:cd05302  257 KICDREAVAEALESGHLAGYAGDVW 281
PRK07574 PRK07574
NAD-dependent formate dehydrogenase;
82-260 5.78e-39

NAD-dependent formate dehydrogenase;


Pssm-ID: 181041  Cd Length: 385  Bit Score: 141.73  E-value: 5.78e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  82 VDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREA--NFSLEGLIGFNMYKRTVGVIGTGKIGIAT 159
Cdd:PRK07574 128 VDLQAASEHGITVAEVTGSNSISVAEHVVMMILALVRNYEPSHRQAVEGgwNIADCVSRSYDLEGMTVGIVGAGRIGLAV 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 160 TRILKGFGMNILAFDPFKNP--IVEEIG-AKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGS 236
Cdd:PRK07574 208 LRRLKPFDVKLHYTDRHRLPeeVEQELGlTYHVSFDSLVSVCDVVTIHCPLHPETEHLFDADVLSRMKRGSYLVNTARGK 287

                        170       180
                 ....*....|....*....|....
gi 633955246 237 LIDTPEAIKALKRRKIGALGMDVY 260
Cdd:PRK07574 288 IVDRDAVVRALESGHLAGYAGDVW 311
PRK06487 PRK06487
2-hydroxyacid dehydrogenase;
70-263 4.66e-38

2-hydroxyacid dehydrogenase;


Pssm-ID: 180588 [Multi-domain]  Cd Length: 317  Bit Score: 137.52  E-value: 4.66e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  70 KMIALRCASFNNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRI---HRAYQRTREANFSLEGLIGFNMYK-- 144
Cdd:PRK06487  68 KLILVAATGTNNVDLAAARERGITVCNCQGYGTPSVAQHTLALLLALATRLpdyQQAVAAGRWQQSSQFCLLDFPIVEle 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 145 -RTVGVIGTGKIGIATTRILKGFGMNILAFDPFKNPIveeiGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKM 223
Cdd:PRK06487 148 gKTLGLLGHGELGGAVARLAEAFGMRVLIGQLPGRPA----RPDRLPLDELLPQVDALTLHCPLTEHTRHLIGARELALM 223

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 633955246 224 KDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENE 263
Cdd:PRK06487 224 KPGALLINTARGGLVDEQALADALRSGHLGGAATDVLSVE 263
PGDH_3 cd12176
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
 43-307 2.55e-37

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: 135.40  E-value: 2.55e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  43 EGCDVVCIFVNDDGSRAVLE---KLAKVGvkmiaLRCASFNNVDIQAAKELGIQVVRvqaySPEA----VAEHTVGLMLT 115
Cdd:cd12176   41 KDVHLLGIRSKTQLTEEVLEaapKLLAIG-----CFCIGTNQVDLDAAAKRGIPVFN----APFSntrsVAELVIGEIIM 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 116 LNRRIhraYQRTREANFSLEGLIGFNMYK---RTVGVIGTGKIGIATTRILKGFGMNILAFDpfknpIVE--EIG-AKYV 189
Cdd:cd12176  112 LARRL---PDRNAAAHRGIWNKSATGSHEvrgKTLGIIGYGHIGSQLSVLAEALGMRVIFYD-----IAEklPLGnARQV 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 190 -TLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENerdlff 268
Cdd:cd12176  184 sSLEELLAEADFVTLHVPATPSTKNMIGAEEIAQMKKGAILINASRGTVVDIDALAEALRSGHLAGAAVDVFPE------ 257

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 633955246 269 EDKSNevilDDVFRR-LSSCHNVLLTGHQAFLTEEALMNI 307
Cdd:cd12176  258 EPASN----GEPFSSpLQGLPNVILTPHIGGSTEEAQENI 293
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
 43-263 1.05e-35

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: 131.10  E-value: 1.05e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  43 EGCDVvcIFVNDDgSRAVLEKLAKVgvKMIALRCASFNNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHR 122
Cdd:cd05300   39 ADADV--LLGNPP-LPELLPAAPRL--RWIQSTSAGVDALLFPELLERDVVLTNARGIFGPPIAEYVLGYMLAFARKLPR 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 123 AYQ-------RTREANFSLEGligfnmykRTVGVIGTGKIGIATTRILKGFGMNILAFD---PFKNPIVEEIgakyVT-- 190
Cdd:cd05300  114 YARnqaerrwQRRGPVRELAG--------KTVLIVGLGDIGREIARRAKAFGMRVIGVRrsgRPAPPVVDEV----YTpd 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 633955246 191 -LDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENE 263
Cdd:cd05300  182 eLDELLPEADYVVNALPLTPETRGLFNAERFAAMKPGAVLINVGRGSVVDEDALIEALESGRIAGAALDVFEEE 255
PGDH_1 cd12155
Phosphoglycerate Dehydrogenase, 2-hydroxyacid dehydrogenase family; Phosphoglycerate ...
 8-307 1.61e-35

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: 1.61e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   8 TKNYDRKYLE-IANQQYHFEFEFFDfmlNERTAKMAEGCDVVCIFvNDDGSRAVLEKLAKVgvKMIALRCASFNNVDIQA 86
Cdd:cd12155    5 TLDYGDEKEEqIEDLGYDVDVVFED---ELSDEEDLEDIEILYGY-NPDFDELDLAKMKNL--KWIQLYSAGVDYLPLEY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  87 AKELGIQVVRVQ-AYSpEAVAEHTVGLMLTLNRRIHRAY--QRTREANFSLEGLigfNMYKRTVGVIGTGKIGIATTRIL 163
Cdd:cd12155   79 IKKKGILLTNNSgIHS-IPIAEWIVGYILEIYKGLKKAYknQKEKKWKMDSSLL---ELYGKTILFLGTGSIGQEIAKRL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 164 KGFGMNIL----------AFD---PFKNpiveeigakyvtLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMII 230
Cdd:cd12155  155 KAFGMKVIgvntsgrdveYFDkcyPLEE------------LDEVLKEADIVVNVLPLTEETHHLFDEAFFEQMKKGALFI 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 231 NTSRGSLIDTPEAIKALKRRKIGALGMDVYENErDLffeDKSNEvilddvfrrLSSCHNVLLTGHQAFLTE---EALMNI 307
Cdd:cd12155  223 NVGRGPSVDEDALIEALKNKQIRGAALDVFEEE-PL---PKDSP---------LWDLDNVLITPHISGVSEhfnERLFDI 289
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
 79-263 1.78e-34

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: 128.80  E-value: 1.78e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  79 FNNVDIQAAKELGIQVvrvqAYSP----EAVAEHTVGLMLTLNRRihrayqrtreANFSLEGligfnmykRTVGVIGTGK 154
Cdd:cd12158   68 TDHIDTDYLKERGIGF----ANAPgcnaNSVAEYVLSALLVLAQR----------QGFSLKG--------KTVGIVGVGN 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 155 IGIATTRILKGFGMNILAFDPFKNPivEEIGAKYVTLDELYAKSDVITLHCPATPE----NYHLLNKEAFDKMKDGVMII 230
Cdd:cd12158  126 VGSRLARRLEALGMNVLLCDPPRAE--AEGDPGFVSLEELLAEADIITLHVPLTRDgehpTYHLLDEDFLAALKPGQILI 203

                        170       180       190
                 ....*....|....*....|....*....|...
gi 633955246 231 NTSRGSLIDTPEAIKALKRRKIGALGMDVYENE 263
Cdd:cd12158  204 NASRGAVIDNQALLALLQRGKDLRVVLDVWENE 236
PRK08410 PRK08410
D-2-hydroxyacid dehydrogenase;
26-315 1.00e-33

D-2-hydroxyacid dehydrogenase;


Pssm-ID: 181414 [Multi-domain]  Cd Length: 311  Bit Score: 125.87  E-value: 1.00e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  26 EFEFFDFMLNERTAKMAEGCDVVC---IFVNDDgsraVLEKLAKVgvKMIALRCASFNNVDIQAAKELGIQVVRVQAYSP 102
Cdd:PRK08410  24 DFQIYPTTSPEEVIERIKDANIIItnkVVIDKE----VLSQLPNL--KLICITATGTNNVDIEYAKKKGIAVKNVAGYST 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 103 EAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGLI-----GFNMYK-RTVGVIGTGKIGIATTRILKGFGMNILAFDPF 176
Cdd:PRK08410  98 ESVAQHTFAMLLSLLGRINYYDRYVKSGEYSESPIFthisrPLGEIKgKKWGIIGLGTIGKRVAKIAQAFGAKVVYYSTS 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 177 -KNpivEEIGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGAl 255
Cdd:PRK08410 178 gKN---KNEEYERVSLEELLKTSDIISIHAPLNEKTKNLIAYKELKLLKDGAILINVGRGGIVNEKDLAKALDEKDIYA- 253

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 256 GMDVYENErdlffedksnEVILDDVFRRLSSCHNVLLTGHQAFLTEEALMNISDVTLYNI 315
Cdd:PRK08410 254 GLDVLEKE----------PMEKNHPLLSIKNKEKLLITPHIAWASKEARKTLIEKVKENI 303
2-Hacid_dh_2 cd12159
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 99-263 2.74e-30

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: 116.60  E-value: 2.74e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  99 AYSpEAVAEHTVGLMLTLNRRIHRAyQRTREANFSLEGLIGFNMYKRTVGVIGTGKIGIATTRILKGFGMNILAFDPFKN 178
Cdd:cd12159   82 AYA-ETVAEHALALLLAGLRQLPAR-ARATTWDPAEEDDLVTLLRGSTVAIVGAGGIGRALIPLLAPFGAKVIAVNRSGR 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 179 PiVEeiGAKYVT----LDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGA 254
Cdd:cd12159  160 P-VE--GADETVpadrLDEVWPDADHVVLAAPLTPETRHLVDAAALAAMKPHAWLVNVARGPLVDTDALVDALRSGEIAG 236


                 ....*....
gi 633955246 255 LGMDVYENE 263
Cdd:cd12159  237 AALDVTDPE 245
PLN02306 PLN02306
hydroxypyruvate reductase
 45-263 3.80e-30

hydroxypyruvate reductase


Pssm-ID: 177941  Cd Length: 386  Bit Score: 118.04  E-value: 3.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  45 CDVVCIFVNDDGSRAVLEKLAKVGVKMIALRCASFNNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAY 124
Cdd:PLN02306  63 CDGVIGQLTEDWGETLFSALSKAGGKAFSNMAVGYNNVDVEAANKYGIAVGNTPGVLTETTAELAASLSLAAARRIVEAD 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 125 QRTREANFS--LEGLIGFNMYK-RTVGVIGTGKIGIATTRIL-KGFGMNILAFDPFKNPIVEEIGAKY------------ 188
Cdd:PLN02306 143 EFMRAGLYEgwLPHLFVGNLLKgQTVGVIGAGRIGSAYARMMvEGFKMNLIYYDLYQSTRLEKFVTAYgqflkangeqpv 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 189 -----VTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENE 263
Cdd:PLN02306 223 twkraSSMEEVLREADVISLHPVLDKTTYHLINKERLALMKKEAVLVNASRGPVIDEVALVEHLKANPMFRVGLDVFEDE 302
PRK15409 PRK15409
glyoxylate/hydroxypyruvate reductase GhrB;
57-263 1.06e-28

glyoxylate/hydroxypyruvate reductase GhrB;


Pssm-ID: 185307  Cd Length: 323  Bit Score: 112.92  E-value: 1.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  57 SRAVLEKLAKvgvkmiaLRCAS-----FNNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREAN 131
Cdd:PRK15409  57 DAALLEKMPK-------LRAAStisvgYDNFDVDALTARKILLMHTPTVLTETVADTLMALVLSTARRVVEVAERVKAGE 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 132 FSL---EGLIGFNMYKRTVGVIGTGKIGIA-TTRILKGFGMNILAFDPFKNPIVEE-IGAKYVTLDELYAKSDVITLHCP 206
Cdd:PRK15409 130 WTAsigPDWFGTDVHHKTLGIVGMGRIGMAlAQRAHFGFNMPILYNARRHHKEAEErFNARYCDLDTLLQESDFVCIILP 209

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 633955246 207 ATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENE 263
Cdd:PRK15409 210 LTDETHHLFGAEQFAKMKSSAIFINAGRGPVVDENALIAALQKGEIHAAGLDVFEQE 266
PRK11790 PRK11790
phosphoglycerate dehydrogenase;
57-307 6.33e-27

phosphoglycerate dehydrogenase;


Pssm-ID: 236985 [Multi-domain]  Cd Length: 409  Bit Score: 109.50  E-value: 6.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  57 SRAVLEKlAKvgvKMIALRCasF----NNVDIQAAKELGIQVVrvQA-YS-PEAVAEHTVGLMLTLNRRI-------HRA 123
Cdd:PRK11790  66 TEEVLAA-AE---KLVAIGC--FcigtNQVDLDAAAKRGIPVF--NApFSnTRSVAELVIGEIILLLRGIpeknakaHRG 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 124 -YQRTREANFSLEGligfnmykRTVGVIGTGKIGIATTRILKGFGMNILAFDpfknpiVEE---IG-AKYV-TLDELYAK 197
Cdd:PRK11790 138 gWNKSAAGSFEVRG--------KTLGIVGYGHIGTQLSVLAESLGMRVYFYD------IEDklpLGnARQVgSLEELLAQ 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 198 SDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENerdlffEDKSNevil 277
Cdd:PRK11790 204 SDVVSLHVPETPSTKNMIGAEELALMKPGAILINASRGTVVDIDALADALKSGHLAGAAIDVFPV------EPKSN---- 273

                        250       260       270
                 ....*....|....*....|....*....|....
gi 633955246 278 DDVF----RRLSschNVLLTGHQAFLTEEALMNI 307
Cdd:PRK11790 274 GDPFesplRGLD---NVILTPHIGGSTQEAQENI 304
PLN03139 PLN03139
formate dehydrogenase; Provisional
 80-260 1.25e-26

formate dehydrogenase; Provisional


Pssm-ID: 178684  Cd Length: 386  Bit Score: 108.40  E-value: 1.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  80 NNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIHRAYQRTREANFSLEGLI--GFNMYKRTVGVIGTGKIGI 157
Cdd:PLN03139 133 DHIDLPAAAAAGLTVAEVTGSNVVSVAEDELMRILILLRNFLPGYHQVVSGEWNVAGIAyrAYDLEGKTVGTVGAGRIGR 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 158 ATTRILKGFGMNILAFDPFK-NPIVE-EIGAKYVT-LDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSR 234
Cdd:PLN03139 213 LLLQRLKPFNCNLLYHDRLKmDPELEkETGAKFEEdLDAMLPKCDVVVINTPLTEKTRGMFNKERIAKMKKGVLIVNNAR 292

                        170       180
                 ....*....|....*....|....*.
gi 633955246 235 GSLIDTPEAIKALKRRKIGALGMDVY 260
Cdd:PLN03139 293 GAIMDTQAVADACSSGHIGGYGGDVW 318
PRK00257 PRK00257
4-phosphoerythronate dehydrogenase PdxB;
57-265 8.73e-25

4-phosphoerythronate dehydrogenase PdxB;


Pssm-ID: 166874 [Multi-domain]  Cd Length: 381  Bit Score: 103.19  E-value: 8.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  57 SRAVLEKLAkvgVKMIALRCASFNNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIhrayqrtreanfsleg 136
Cdd:PRK00257  50 DRALLEGSR---VRFVGTCTIGTDHLDLDYFAEAGITWSSAPGCNARGVVDYVLGSLLTLAERE---------------- 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 137 liGFNMYKRTVGVIGTGKIGIATTRILKGFGMNILAFDPFKNpIVEEIGaKYVTLDELYAKSDVITLHCPATPE----NY 212
Cdd:PRK00257 111 --GVDLAERTYGVVGAGHVGGRLVRVLRGLGWKVLVCDPPRQ-EAEGDG-DFVSLERILEECDVISLHTPLTKEgehpTR 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 633955246 213 HLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENERD 265
Cdd:PRK00257 187 HLLDEAFLASLRPGAWLINASRGAVVDNQALREALLSGEDLDAVLDVWEGEPQ 239
2-Hacid_dh_15 cd12180
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 91-263 5.40e-23

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: 97.03  E-value: 5.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  91 GIQVVRVQAYSPEAVAEHTVGLMLTL-----NRRIHRAYQRTREANFSLEGligfnmykRTVGVIGTGKIGIATTRILKG 165
Cdd:cd12180   85 GPVVTCARGVAAEAIAEFVLAAILAAakrlpEIWVKGAEQWRREPLGSLAG--------STLGIVGFGAIGQALARRALA 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 166 FGMNILAFDPFKNPiVEEIGAKYV-TLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAI 244
Cdd:cd12180  157 LGMRVLALRRSGRP-SDVPGVEAAaDLAELFARSDHLVLAAPLTPETRHLINADVLAQAKPGLHLINIARGGLVDQEALL 235

                        170
                 ....*....|....*....
gi 633955246 245 KALKRRKIGALGMDVYENE 263
Cdd:cd12180  236 EALDSGRISLASLDVTDPE 254
2-Hacid_dh_9 cd12170
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 69-315 1.19e-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: 240647 [Multi-domain]  Cd Length: 294  Bit Score: 95.83  E-value: 1.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  69 VKMIALRCASFN----NVDIQAAKELGIQVVRVQAYSPEAVAEHTVGlmlTLNRRIHrAYQRTREANFSLEgLIGfnmyk 144
Cdd:cd12170   69 IKYIGMCCSLYSeesaNVDIAAARENGITVTGIRDYGDEGVVEYVIS---ELIRLLH-GFGGKQWKEEPRE-LTG----- 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 145 RTVGVIGTGKIGIATTRILKGFGMNILAFDPFKNPIVEEIGAKYVTLDELYAKSDVITLHcpaTPENYHLLNKEAFDKMK 224
Cdd:cd12170  139 LKVGIIGLGTTGQMIADALSFFGADVYYYSRTRKPDAEAKGIRYLPLNELLKTVDVICTC---LPKNVILLGEEEFELLG 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 225 DGVMIINTSRGSLIDTPEAIKALKRRKigalgmdvyeneRDLFFEDKSNEVILDDVFRRlsscHNVLLTGHQAFLTEEAL 304
Cdd:cd12170  216 DGKILFNTSLGPSFEVEALKKWLKASG------------YNIFDCDTAGALGDEELLRY----PNVICTNKSAGWTRQAF 279

                        250
                 ....*....|.
gi 633955246 305 MNISDVTLYNI 315
Cdd:cd12170  280 ERLSQKVLANL 290
PLN02928 PLN02928
oxidoreductase family protein
 82-259 5.32e-21

oxidoreductase family protein


Pssm-ID: 215501  Cd Length: 347  Bit Score: 92.05  E-value: 5.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  82 VDIQAAKELGIQVVRVQAY---SPEAVAEHTVGLMLTLNRRiHRAYQrTREANFSLEGLIGFNMYKRTVGVIGTGKIGIA 158
Cdd:PLN02928  96 VDVDAATKHGIKVARIPSEgtgNAASCAEMAIYLMLGLLRK-QNEMQ-ISLKARRLGEPIGDTLFGKTVFILGYGAIGIE 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 159 TTRILKGFGMNILA---------------FDPFKNPIVEEIGaKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKM 223
Cdd:PLN02928 174 LAKRLRPFGVKLLAtrrswtsepedglliPNGDVDDLVDEKG-GHEDIYEFAGEADIVVLCCTLTKETAGIVNDEFLSSM 252

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 633955246 224 KDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDV 259
Cdd:PLN02928 253 KKGALLVNIARGGLLDYDAVLAALESGHLGGLAIDV 288
2-Hacid_dh_7 cd12166
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 104-259 1.23e-20

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


Pssm-ID: 240643 [Multi-domain]  Cd Length: 300  Bit Score: 90.34  E-value: 1.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 104 AVAEHTVGLMLTLNRRIHRAY--QRTRE-ANFSLEGLIGfnmykRTVGVIGTGKIGIATTRILKGFGMNIL--AFDPFKN 178
Cdd:cd12166   94 STAELAVALILASLRGLPRFVraQARGRwEPRRTPSLAD-----RRVLIVGYGSIGRAIERRLAPFEVRVTrvARTARPG 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 179 PIVEEIGAkyvtLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGAlGMD 258
Cdd:cd12166  169 EQVHGIDE----LPALLPEADVVVLIVPLTDETRGLVDAEFLARMPDGALLVNVARGPVVDTDALVAELASGRLRA-ALD 243


                 .
gi 633955246 259 V 259
Cdd:cd12166  244 V 244
PRK06436 PRK06436
2-hydroxyacid dehydrogenase;
70-297 6.90e-19

2-hydroxyacid dehydrogenase;


Pssm-ID: 235800 [Multi-domain]  Cd Length: 303  Bit Score: 85.32  E-value: 6.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  70 KMIALRCASFNNVDIQAAKELGIQVVRVQAYSPeAVAEHTVGLMLTLNRRIHRAYQRTREANFslEGLIGFNMYKRTVGV 149
Cdd:PRK06436  51 KMIQSLSAGVDHIDVSGIPENVVLCSNAGAYSI-SVAEHAFALLLAWAKNICENNYNMKNGNF--KQSPTKLLYNKSLGI 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 150 IGTGKIGIATTRILKGFGMNILAFDpfKNPIVEEIGAKYVTLDELYAKSDVITLHCPATPENYHLLNKEAFDKMKDGVMI 229
Cdd:PRK06436 128 LGYGGIGRRVALLAKAFGMNIYAYT--RSYVNDGISSIYMEPEDIMKKSDFVLISLPLTDETRGMINSKMLSLFRKGLAI 205

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 633955246 230 INTSRGSLIDTPEAIKALKRRKIGALGMDVYENERDLffedksNEVILDdvfrrlsschNVLLTGHQA 297
Cdd:PRK06436 206 INVARADVVDKNDMLNFLRNHNDKYYLSDVWWNEPII------TETNPD----------NVILSPHVA 257
2-Hacid_dh_5 cd12163
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 23-326 1.63e-16

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


Pssm-ID: 240640  Cd Length: 334  Bit Score: 78.85  E-value: 1.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  23 YHFEFEFFDFMLNERTAKMAEGCDVVCIFVNDDGsravLEKLAKVgvKMIALRCASFN---------NVDIQAAKELGIQ 93
Cdd:cd12163   15 RWVESAPPDGPPEDVPAEVWEGVTILCTFHPHPD----AEDVPNL--RLVQLFSAGADhwlghplykDPEVPLCTASGIH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  94 vvrvqaysPEAVAEHTVGLMLTLNRRIHRAY--QRTREANFSLEGLIGFNMYKRTVGVIGTGKIGIATTRILKGFGMNIL 171
Cdd:cd12163   89 --------GPQIAEWVIGTWLVLSHHFLQYIelQKEQTWGRRQEAYSVEDSVGKRVGILGYGSIGRQTARLAQALGMEVY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 172 AFD--PFKNP--------IVEEIGAK--------YVTLDE------LYAKSDVITLHCPATPENYHLLNKEAFDKM-KDG 226
Cdd:cd12163  161 AYTrsPRPTPesrkddgyIVPGTGDPdgsipsawFSGTDKaslhefLRQDLDLLVVSLPLTPATKHLLGAEEFEILaKRK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 227 VMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENERdlffedksnevILDDvfRRLSSCHNVLLTGHQAFLTEEALMN 306
Cdd:cd12163  241 TFVSNIARGSLVDTDALVAALESGQIRGAALDVTDPEP-----------LPAD--HPLWSAPNVIITPHVSWQTQEYFDR 307

                        330       340
                 ....*....|....*....|
gi 633955246 307 ISDVTLYNICCLQKGGHCEN 326
Cdd:cd12163  308 ALDVLEENLERLRKGEPLIN 327
2-Hacid_dh_3 cd12160
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 62-263 5.33e-16

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


Pssm-ID: 240637  Cd Length: 310  Bit Score: 77.03  E-value: 5.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  62 EKLAKVGVKMIALRCasfnnVDIQAAkelGIQVVRVQAYSPEA------------VAEHTVGLMLTLNRRIH--RAYQRT 127
Cdd:cd12160   48 DNLADAARRLTRLRW-----VQALAA---GPDAVLAAGFAPEVavtsgrglhdgtVAEHTLALILAAVRRLDemREAQRE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 128 REANFSLEGLIGFNMYKRT-------VGVIGTGKIGIATTRILKGFGMNIL-----AFDPFKNPIVEEigakyVTLDELY 195
Cdd:cd12160  120 HRWAGELGGLQPLRPAGRLttllgarVLIWGFGSIGQRLAPLLTALGARVTgvarsAGERAGFPVVAE-----DELPELL 194

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 633955246 196 AKSDVITLHCPATPENYHLLNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENE 263
Cdd:cd12160  195 PETDVLVMILPATPSTAHALDAEVLAALPKHAWVVNVGRGATVDEDALVAALESGRLGGAALDVTATE 262
PRK15438 PRK15438
erythronate-4-phosphate dehydrogenase PdxB; Provisional
 64-266 9.98e-16

erythronate-4-phosphate dehydrogenase PdxB; Provisional


Pssm-ID: 185335 [Multi-domain]  Cd Length: 378  Bit Score: 77.25  E-value: 9.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246  64 LAKVGVKMIALRCASFNNVDIQAAKELGIQVVRVQAYSPEAVAEHTVGLMLTLNRRIhrayqrtreanfslegliGFNMY 143
Cdd:PRK15438  54 LAGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAERD------------------GFSLH 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 144 KRTVGVIGTGKIGIATTRILKGFGMNILAFDPFKNPIVEEigAKYVTLDELYAKSDVITLHCPATPE----NYHLLNKEA 219
Cdd:PRK15438 116 DRTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADRGDE--GDFRSLDELVQEADILTFHTPLFKDgpykTLHLADEKL 193

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 633955246 220 FDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENERDL 266
Cdd:PRK15438 194 IRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPEL 240
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 145-252 6.40e-14

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: 6.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 145 RTVGVIGTGKIGIATTRILKGFGMNILAFDPfkNPI----VEEIGAKYV-TLDELYAKSDVITLHCPATPENYHLLN-KE 218
Cdd:cd12154  161 KTVVVVGAGVVGKEAAQMLRGLGAQVLITDI--NVEaleqLEELGGKNVeELEEALAEADVIVTTTLLPGKRAGILVpEE 238

                         90       100       110
                 ....*....|....*....|....*....|....
gi 633955246 219 AFDKMKDGVMIINTSRGSLIDTPeaikALKRRKI 252
Cdd:cd12154  239 LVEQMKPGSVIVNVAVGAVGCVQ----ALHTQLL 268
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
 145-263 5.81e-13

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: 68.29  E-value: 5.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 145 RTVGVIGTGKIGIATTRILKGFGMNILAFDPFKNPIVEeigakyVT-------LDELYAKSDVitLHC--PATPENYHLL 215
Cdd:cd12164  133 RRVGVLGLGELGAAVARRLAALGFPVSGWSRSPKDIEG------VTcfhgeegLDAFLAQTDI--LVCllPLTPETRGIL 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 633955246 216 NKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENE 263
Cdd:cd12164  205 NAELLARLPRGAALINVGRGPHLVEADLLAALDSGHLSGAVLDVFEQE 252
ghrA PRK15469
glyoxylate/hydroxypyruvate reductase GhrA;
143-263 1.54e-04

glyoxylate/hydroxypyruvate reductase GhrA;


Pssm-ID: 185366  Cd Length: 312  Bit Score: 42.86  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246 143 YKR---TVGVIGTGKIGIATTRILKGFGMNILAFDPFKN--PIVEEigakYVTLDELYA---KSDVITLHCPATPENYHL 214
Cdd:PRK15469 132 YHRedfTIGILGAGVLGSKVAQSLQTWGFPLRCWSRSRKswPGVQS----FAGREELSAflsQTRVLINLLPNTPETVGI 207

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 633955246 215 LNKEAFDKMKDGVMIINTSRGSLIDTPEAIKALKRRKIGALGMDVYENE 263
Cdd:PRK15469 208 INQQLLEQLPDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFSRE 256
AdoHcyase_NAD smart00997
S-adenosyl-L-homocysteine hydrolase, NAD binding domain;
145-231 3.50e-03

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


Pssm-ID: 198065 [Multi-domain]  Cd Length: 162  Bit Score: 37.43  E-value: 3.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   145 RTVGVIGTGKIGIATTRILKGFGMNilafdpfknPIVEEI-----------GAKYVTLDELYAKSDVItlhCPATpENYH 213
Cdd:smart00997  24 KNVVVAGYGDVGKGVAARLRGLGAR---------VIVTEIdpiraleaamdGFEVMKMEEAAKRADIF---VTAT-GNKD 90

                           90
                   ....*....|....*...
gi 633955246   214 LLNKEAFDKMKDGVMIIN 231
Cdd:smart00997  91 VITREHFRAMKDGAILAN 108
PRK08296 PRK08296
hypothetical protein; Provisional
 9-83 8.57e-03

hypothetical protein; Provisional


Pssm-ID: 181362  Cd Length: 603  Bit Score: 37.71  E-value: 8.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 633955246   9 KNYDRKY-LEIANQQYHFEF---------EFFDFML-------NERTAKMAEGCDVVcIFVNDDGsravLEKLAKVGVKM 71
Cdd:PRK08296 174 ESYDRLIdLLFRAWQYHFEFlnlgyaaylTFYDFCKqlfpdipDQHITEMVAGIDVI-MFRPDDE----LKRLARLAVEL 248

                         90
                 ....*....|...
gi 633955246  72 -IALRCASFNNVD 83
Cdd:PRK08296 249 gIADIFASGDSPQ 261
 
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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