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Conserved domains on  [gi|2777341964|ref|WP_367887818|]
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Gfo/Idh/MocA family protein [Pseudogemmatithrix spongiicola]

Protein Classification

Gfo/Idh/MocA family protein( domain architecture ID 11430574)

Gfo/Idh/MocA family protein belonging to the NAD(P)(+)-binding Rossmann-fold superfamily, may function as an oxidoreductase that catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

CATH:  3.40.50.720|3.30.360.10
Gene Ontology:  GO:0000166|GO:0003824
PubMed:  30945211|31869345|25704928|26749496

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UDP-GlcNAcDh_Arch super family cl48975
UDP-N-acetylglucosamine 3-dehydrogenase;
5-315 2.67e-67

UDP-N-acetylglucosamine 3-dehydrogenase;


The actual alignment was detected with superfamily member NF040723:

Pssm-ID: 468687 [Multi-domain]  Cd Length: 302  Bit Score: 213.29  E-value: 2.67e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964   5 LRVGVIGTGSLGYHHARILRDLPGIVFKGFYEANADRAGTVARELGIRAYPTLEALLA-DVDAVSIVVPTPFHHAVAKQA 83
Cdd:NF040723    1 LRVGVIGVGAMGYNHARIYSEMEGVELVGIADVNKERVKELAKQYNTKAFTDYKELLKeDLDAVSIVVPTKLHKQVALDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964  84 LEAGKHLLIEKPITVTLEEADELLAIADRVGKLIQIGHIERFNRAIRAALPHVDTPLF-----IDSDRLAPFNPRGSDVA 158
Cdd:NF040723   81 IEAGVNVLVEKPIADTIENAQEIIKAAKKNNVKLMVGHIERFNPAVLKLKEIIDSGLLgkivsISAKRVGPYNPRIRDVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964 159 VVLDLMIHDIDLVLTLIGAPVKDVSAAGLPVLTPSIDIANARITFATGAVATITASRVSKERTRKLRIFQKNGYLSLDLA 238
Cdd:NF040723  161 VILDLGVHDIDVISYLYGSKVKEVYAIAGSVIHPFEDHASIMLRFEHNISGLVETNWLTPHKTRKLTVVGTEGIAYLDYI 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2777341964 239 SGTGEMYrlrkDVDLATLAKqaqpidafVERvvidapeGEPLRLELESFVAAIK-GEQPVaVTGRAGRDALAVALRII 315
Cdd:NF040723  241 NQTLTIH----DEEWVKEAK--------IEK-------EEPLKNELEHFIECVEnGKEPL-VSGEDGLHALKVALAAI 298
 
Name Accession Description Interval E-value
UDP-GlcNAcDh_Arch NF040723
UDP-N-acetylglucosamine 3-dehydrogenase;
5-315 2.67e-67

UDP-N-acetylglucosamine 3-dehydrogenase;


Pssm-ID: 468687 [Multi-domain]  Cd Length: 302  Bit Score: 213.29  E-value: 2.67e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964   5 LRVGVIGTGSLGYHHARILRDLPGIVFKGFYEANADRAGTVARELGIRAYPTLEALLA-DVDAVSIVVPTPFHHAVAKQA 83
Cdd:NF040723    1 LRVGVIGVGAMGYNHARIYSEMEGVELVGIADVNKERVKELAKQYNTKAFTDYKELLKeDLDAVSIVVPTKLHKQVALDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964  84 LEAGKHLLIEKPITVTLEEADELLAIADRVGKLIQIGHIERFNRAIRAALPHVDTPLF-----IDSDRLAPFNPRGSDVA 158
Cdd:NF040723   81 IEAGVNVLVEKPIADTIENAQEIIKAAKKNNVKLMVGHIERFNPAVLKLKEIIDSGLLgkivsISAKRVGPYNPRIRDVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964 159 VVLDLMIHDIDLVLTLIGAPVKDVSAAGLPVLTPSIDIANARITFATGAVATITASRVSKERTRKLRIFQKNGYLSLDLA 238
Cdd:NF040723  161 VILDLGVHDIDVISYLYGSKVKEVYAIAGSVIHPFEDHASIMLRFEHNISGLVETNWLTPHKTRKLTVVGTEGIAYLDYI 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2777341964 239 SGTGEMYrlrkDVDLATLAKqaqpidafVERvvidapeGEPLRLELESFVAAIK-GEQPVaVTGRAGRDALAVALRII 315
Cdd:NF040723  241 NQTLTIH----DEEWVKEAK--------IEK-------EEPLKNELEHFIECVEnGKEPL-VSGEDGLHALKVALAAI 298
MviM COG0673
Predicted dehydrogenase [General function prediction only];
2-233 8.27e-64

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 204.00  E-value: 8.27e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964   2 SQPLRVGVIGTGSLGYHHARILRDLPGIVFKGFYEANADRAGTVARELGIRAYPTLEALLAD--VDAVSIVVPTPFHHAV 79
Cdd:COG0673     1 MDKLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEAFAEEYGVRVYTDYEELLADpdIDAVVIATPNHLHAEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964  80 AKQALEAGKHLLIEKPITVTLEEADELLAIADRVGKLIQIGHIERFNRAIRAALPHVD-----TPLFIDSDRLAP----- 149
Cdd:COG0673    81 AIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDsgaigEIRSVRARFGHPrpagp 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964 150 ----FNPRGSDVAVVLDLMIHDIDLVLTLIGAPVKDVSAAGLPVLTPSI---DIANARITFATGAVATITASRVS--KER 220
Cdd:COG0673   161 adwrFDPELAGGGALLDLGIHDIDLARWLLGSEPESVSATGGRLVPDRVevdDTAAATLRFANGAVATLEASWVApgGER 240

                         250
                  ....*....|...
gi 2777341964 221 TRKLRIFQKNGYL 233
Cdd:COG0673   241 DERLEVYGTKGTL 253
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 4-313 6.75e-37

inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]


Pssm-ID: 275173 [Multi-domain]  Cd Length: 330  Bit Score: 135.04  E-value: 6.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964   4 PLRVGVIGTGSLGYHHAR-ILRDLPGIVFKGFYEANADRAGTVARELGI-RAYPTLEALLAD--VDAVSIVVPTPFHHAV 79
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAEnLATHVPGARLKAIVDPFADAAAELAEKLGIePVTQDPEAALADpeIDAVLIASPTDTHADL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964  80 AKQALEAGKHLLIEKPITVTLEEADELLAIADRVGKLIQIGHIERFNRAIRAALPHVD-----TPLFIDSDRLAPFNPRG 154
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEagkigKPEILRITSRDPAPPPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964 155 SDVAV----VLDLMIHDIDLVLTLIGAPVKDVSAAGLPVLTPSI----DIANARIT--FATGAVATITASRvskeRT--- 221
Cdd:TIGR04380 161 AYVKVsgglFLDMTIHDFDMARFLLGSEVEEVYAQGSVLVDPAIgeagDVDTAVITlkFENGAIAVIDNSR----RAayg 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964 222 --RKLRIFQKNGYLSLDLASGTGEMYRLRKDVDLATlakqaqPIDAFVERVvidapeGEPLRLELESFVAAIKGEQPVAV 299
Cdd:TIGR04380 237 ydQRVEVFGSKGMLRAENDTESTVILYDAEGVRGDK------PLNFFLERY------RDAYRAEIQAFVDAILEGRPPPV 304

                         330
                  ....*....|....
gi 2777341964 300 TGRAGRDALAVALR 313
Cdd:TIGR04380 305 TGEDGLKALLLALA 318
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 5-121 2.02e-31

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 114.23  E-value: 2.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964   5 LRVGVIGTGSLGYHHAR-ILRDLPGIVFKGFYEANADRAGTVARELGIRAYPTLEALLAD--VDAVSIVVPTPFHHAVAK 81
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARaLNASQPGAELVAILDPNSERAEAVAESFGVEVYSDLEELLNDpeIDAVIVATPNGLHYDLAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2777341964  82 QALEAGKHLLIEKPITVTLEEADELLAIADRVGKLIQIGH 121
Cdd:pfam01408  81 AALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
PRK11579 PRK11579
putative oxidoreductase; Provisional
 1-126 6.18e-17

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 80.53  E-value: 6.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964   1 MSQPLRVGVIGtgsLGY----HHARILRDLPGIVFKGFYEANADRAGtvARELGIRAYPTLEALLADVDAVSIVVPTP-- 74
Cdd:PRK11579    1 MSDKIRVGLIG---YGYasktFHAPLIAGTPGLELAAVSSSDATKVK--ADWPTVTVVSEPQHLFNDPNIDLIVIPTPnd 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2777341964  75 FHHAVAKQALEAGKHLLIEKPITVTLEEADELLAIADRVGKLIQIGHIERFN 126
Cdd:PRK11579   76 THFPLAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWD 127
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 6-87 1.31e-05

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 214881 [Multi-domain]  Cd Length: 100  Bit Score: 43.27  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964    6 RVGVIG-TGSLGYHHARILRDLP--GIVFKGfyEANADRAGTvaRELGIRAYPTLEALLA--DVDAVSIVVPTPFHHAVA 80
Cdd:smart00881   7 SVAVVGaSGNLGSFGLAVMRNLLeyGTKFVG--GVYPGKVGP--KVDGVPVYDSVAEAPEetGVDVAVIFVPAEAAPDAI 82


                   ....*..
gi 2777341964   81 KQALEAG 87
Cdd:smart00881  83 DEAIEAG 89
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
 7-77 4.48e-03

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: 38.41  E-value: 4.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2777341964   7 VGVIGTGSLGYHHARILRdlpgivfkGF------YEANADRagTVARELGIRaYPTLEALLADVDAVSIVVP-TP-FHH 77
Cdd:cd12187   142 LGVVGTGRIGRRVARIAR--------GFgmkvlaYDVVPDE--ELAERLGFR-YVSLEELLQESDIISLHVPyTPqTHH 209
 
Name Accession Description Interval E-value
UDP-GlcNAcDh_Arch NF040723
UDP-N-acetylglucosamine 3-dehydrogenase;
5-315 2.67e-67

UDP-N-acetylglucosamine 3-dehydrogenase;


Pssm-ID: 468687 [Multi-domain]  Cd Length: 302  Bit Score: 213.29  E-value: 2.67e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964   5 LRVGVIGTGSLGYHHARILRDLPGIVFKGFYEANADRAGTVARELGIRAYPTLEALLA-DVDAVSIVVPTPFHHAVAKQA 83
Cdd:NF040723    1 LRVGVIGVGAMGYNHARIYSEMEGVELVGIADVNKERVKELAKQYNTKAFTDYKELLKeDLDAVSIVVPTKLHKQVALDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964  84 LEAGKHLLIEKPITVTLEEADELLAIADRVGKLIQIGHIERFNRAIRAALPHVDTPLF-----IDSDRLAPFNPRGSDVA 158
Cdd:NF040723   81 IEAGVNVLVEKPIADTIENAQEIIKAAKKNNVKLMVGHIERFNPAVLKLKEIIDSGLLgkivsISAKRVGPYNPRIRDVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964 159 VVLDLMIHDIDLVLTLIGAPVKDVSAAGLPVLTPSIDIANARITFATGAVATITASRVSKERTRKLRIFQKNGYLSLDLA 238
Cdd:NF040723  161 VILDLGVHDIDVISYLYGSKVKEVYAIAGSVIHPFEDHASIMLRFEHNISGLVETNWLTPHKTRKLTVVGTEGIAYLDYI 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2777341964 239 SGTGEMYrlrkDVDLATLAKqaqpidafVERvvidapeGEPLRLELESFVAAIK-GEQPVaVTGRAGRDALAVALRII 315
Cdd:NF040723  241 NQTLTIH----DEEWVKEAK--------IEK-------EEPLKNELEHFIECVEnGKEPL-VSGEDGLHALKVALAAI 298
MviM COG0673
Predicted dehydrogenase [General function prediction only];
2-233 8.27e-64

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 204.00  E-value: 8.27e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964   2 SQPLRVGVIGTGSLGYHHARILRDLPGIVFKGFYEANADRAGTVARELGIRAYPTLEALLAD--VDAVSIVVPTPFHHAV 79
Cdd:COG0673     1 MDKLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEAFAEEYGVRVYTDYEELLADpdIDAVVIATPNHLHAEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964  80 AKQALEAGKHLLIEKPITVTLEEADELLAIADRVGKLIQIGHIERFNRAIRAALPHVD-----TPLFIDSDRLAP----- 149
Cdd:COG0673    81 AIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDsgaigEIRSVRARFGHPrpagp 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964 150 ----FNPRGSDVAVVLDLMIHDIDLVLTLIGAPVKDVSAAGLPVLTPSI---DIANARITFATGAVATITASRVS--KER 220
Cdd:COG0673   161 adwrFDPELAGGGALLDLGIHDIDLARWLLGSEPESVSATGGRLVPDRVevdDTAAATLRFANGAVATLEASWVApgGER 240

                         250
                  ....*....|...
gi 2777341964 221 TRKLRIFQKNGYL 233
Cdd:COG0673   241 DERLEVYGTKGTL 253
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 4-313 6.75e-37

inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]


Pssm-ID: 275173 [Multi-domain]  Cd Length: 330  Bit Score: 135.04  E-value: 6.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964   4 PLRVGVIGTGSLGYHHAR-ILRDLPGIVFKGFYEANADRAGTVARELGI-RAYPTLEALLAD--VDAVSIVVPTPFHHAV 79
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAEnLATHVPGARLKAIVDPFADAAAELAEKLGIePVTQDPEAALADpeIDAVLIASPTDTHADL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964  80 AKQALEAGKHLLIEKPITVTLEEADELLAIADRVGKLIQIGHIERFNRAIRAALPHVD-----TPLFIDSDRLAPFNPRG 154
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEagkigKPEILRITSRDPAPPPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964 155 SDVAV----VLDLMIHDIDLVLTLIGAPVKDVSAAGLPVLTPSI----DIANARIT--FATGAVATITASRvskeRT--- 221
Cdd:TIGR04380 161 AYVKVsgglFLDMTIHDFDMARFLLGSEVEEVYAQGSVLVDPAIgeagDVDTAVITlkFENGAIAVIDNSR----RAayg 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964 222 --RKLRIFQKNGYLSLDLASGTGEMYRLRKDVDLATlakqaqPIDAFVERVvidapeGEPLRLELESFVAAIKGEQPVAV 299
Cdd:TIGR04380 237 ydQRVEVFGSKGMLRAENDTESTVILYDAEGVRGDK------PLNFFLERY------RDAYRAEIQAFVDAILEGRPPPV 304

                         330
                  ....*....|....
gi 2777341964 300 TGRAGRDALAVALR 313
Cdd:TIGR04380 305 TGEDGLKALLLALA 318
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 5-121 2.02e-31

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 114.23  E-value: 2.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964   5 LRVGVIGTGSLGYHHAR-ILRDLPGIVFKGFYEANADRAGTVARELGIRAYPTLEALLAD--VDAVSIVVPTPFHHAVAK 81
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARaLNASQPGAELVAILDPNSERAEAVAESFGVEVYSDLEELLNDpeIDAVIVATPNGLHYDLAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2777341964  82 QALEAGKHLLIEKPITVTLEEADELLAIADRVGKLIQIGH 121
Cdd:pfam01408  81 AALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
PRK11579 PRK11579
putative oxidoreductase; Provisional
 1-126 6.18e-17

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 80.53  E-value: 6.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964   1 MSQPLRVGVIGtgsLGY----HHARILRDLPGIVFKGFYEANADRAGtvARELGIRAYPTLEALLADVDAVSIVVPTP-- 74
Cdd:PRK11579    1 MSDKIRVGLIG---YGYasktFHAPLIAGTPGLELAAVSSSDATKVK--ADWPTVTVVSEPQHLFNDPNIDLIVIPTPnd 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2777341964  75 FHHAVAKQALEAGKHLLIEKPITVTLEEADELLAIADRVGKLIQIGHIERFN 126
Cdd:PRK11579   76 THFPLAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWD 127
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
 159-311 2.09e-08

Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 427044  Cd Length: 203  Bit Score: 53.58  E-value: 2.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964 159 VVLDLMIHDIDLVLTLIGAPVKDVSAAGlpvltpSIDIANARITFATGAVAT--ITASRVSKERTRKLRIFQKNGYLSLD 236
Cdd:pfam02894  42 ALYDLGIHTIDLLIYLFGEPPSVVAVYA------SEDTAFATLEFKNGAVGTleTSGGSIVEANGHRISIHGTKGSIELD 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964 237 LAsgtgemyrlrkDVDLATLAKQAQPIDAFVERVVI---------DAPEGEPLRLELESFVAAIKGEQPVAVTGRAGRDA 307
Cdd:pfam02894 116 GI-----------DDGLLSVTVVGEPGWATDDPMVRkggdevpefLGSFAGGYLLEYDAFLEAVRGGKVVLVDAEDGLYA 184


                  ....
gi 2777341964 308 LAVA 311
Cdd:pfam02894 185 LAVI 188
PRK10206 PRK10206
putative oxidoreductase; Provisional
 57-178 4.37e-07

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 50.98  E-value: 4.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964  57 LEALLADVDAVSIVVPT--PFHHAVAKQALEAGKHLLIEKPITVTLEEADELLAIADRVGKLIQIGHIERFN-------R 127
Cdd:PRK10206   56 LDEVLNDPDVKLVVVCThaDSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKGLTVTPYQNRRFDscfltakK 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2777341964 128 AIRAAL--PHVDTPLFIDSDR-LAPFNPRGSDVAVVLDLMIHDIDLVLTLIGAP 178
Cdd:PRK10206  136 AIESGKlgEIVEVESHFDYYRpVAETKPGLPQDGAFYGLGVHTMDQIISLFGRP 189
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 6-87 1.31e-05

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 214881 [Multi-domain]  Cd Length: 100  Bit Score: 43.27  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964    6 RVGVIG-TGSLGYHHARILRDLP--GIVFKGfyEANADRAGTvaRELGIRAYPTLEALLA--DVDAVSIVVPTPFHHAVA 80
Cdd:smart00881   7 SVAVVGaSGNLGSFGLAVMRNLLeyGTKFVG--GVYPGKVGP--KVDGVPVYDSVAEAPEetGVDVAVIFVPAEAAPDAI 82


                   ....*..
gi 2777341964   81 KQALEAG 87
Cdd:smart00881  83 DEAIEAG 89
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 5-72 5.23e-04

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 41.34  E-value: 5.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2777341964   5 LRVGVIGTGSLGYHHARILRDlPGIVFKGFYEANADRAGTVARELGIRAYPTLEALLADVDAVSIVVP 72
Cdd:COG5495     4 MKIGIIGAGRVGTALAAALRA-AGHEVVGVYSRSPASAERAAALLGAVPALDLEELAAEADLVLLAVP 70
PRK13304 PRK13304
aspartate dehydrogenase;
5-92 1.64e-03

aspartate dehydrogenase;


Pssm-ID: 237343 [Multi-domain]  Cd Length: 265  Bit Score: 39.59  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964   5 LRVGVIGTGSLGYHHAR-ILRDLPGIVFKGFYEANADRAGTVARELGIRAYPTLEALLADVDavsIVVPTPFHHAV---A 80
Cdd:PRK13304    2 LKIGIVGCGAIASLITKaILSGRINAELYAFYDRNLEKAENLASKTGAKACLSIDELVEDVD---LVVECASVNAVeevV 78

                          90
                  ....*....|..
gi 2777341964  81 KQALEAGKHLLI 92
Cdd:PRK13304   79 PKSLENGKDVII 90
COG3804 COG3804
Uncharacterized conserved protein [Function unknown];
4-89 2.24e-03

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443017 [Multi-domain]  Cd Length: 338  Bit Score: 39.40  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964   4 PLRVGVIGTGSLGYHHARILRDLPGIVFKGFYEANADRAGT-------VARELGIRAYPTLEALLA-DVDAVSIVVPTPF 75
Cdd:COG3804     1 KIRVVQWGTGNMGRGAIRAILAHPGLELVGAIDHSPAKVGKdagelagLGRPLGVKATDDADAVLAlDADVVVYATDSRL 80

                          90
                  ....*....|....*.
gi 2777341964  76 HHAVA--KQALEAGKH 89
Cdd:COG3804    81 EEAVDdlERLLEAGVN 96
LdhA COG1052
Lactate dehydrogenase or related 2-hydroxyacid dehydrogenase [Energy production and conversion, ...
 6-86 3.60e-03

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: 38.53  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2777341964   6 RVGVIGTGSLGYHHARILrdlpgivfKGF-----YeanADRAG-TVARELGIRaYPTLEALLADVDAVSIVVP-TPF-HH 77
Cdd:COG1052   145 TLGIIGLGRIGQAVARRA--------KGFgmkvlY---YDRSPkPEVAELGAE-YVSLDELLAESDIVSLHCPlTPEtRH 212


                  ....*....
gi 2777341964  78 AVAKQALEA 86
Cdd:COG1052   213 LINAEELAL 221
LDH_like_1 cd12187
D-Lactate and related Dehydrogenase like proteins, NAD-binding and catalytic domains; ...
 7-77 4.48e-03

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: 38.41  E-value: 4.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2777341964   7 VGVIGTGSLGYHHARILRdlpgivfkGF------YEANADRagTVARELGIRaYPTLEALLADVDAVSIVVP-TP-FHH 77
Cdd:cd12187   142 LGVVGTGRIGRRVARIAR--------GFgmkvlaYDVVPDE--ELAERLGFR-YVSLEELLQESDIISLHVPyTPqTHH 209
 
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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