NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|189168259|gb|ACD79254|]
View 

malate dehydrogenase, partial [Vibrio sp. FAL1110]

Protein Classification

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 1-146 1.81e-82

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


The actual alignment was detected with superfamily member cd01337:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 310  Bit Score: 244.71  E-value: 1.81e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259   1 PVSIKGYAGEDP-TPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNTTVPIAAE 79
Cdd:cd01337   50 PAKVTGYLGPEElKKALKGADVVVIPAGVPRKPGMTRDDLFNINAGIVRDLATAVAKACPKALILIISNPVNSTVPIAAE 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189168259  80 VLKKAGVYDKRRLFGITTLDVIRSETFVAELKDKDPGDIRVPVIGGHSGVTILPLLSQVEG-VEFTDE 146
Cdd:cd01337  130 VLKKAGVYDPKRLFGVTTLDVVRANTFVAELLGLDPAKVNVPVIGGHSGVTILPLLSQCQPpFTFDQE 197
 
Name Accession Description Interval E-value
MDH_glyoxysomal_mitochondrial cd01337
Glyoxysomal and mitochondrial malate dehydrogenases; MDH is one of the key enzymes in the ...
 1-146 1.81e-82

Glyoxysomal and mitochondrial malate dehydrogenases; MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. Members of this subfamily are localized to the glycosome and mitochondria. MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133422 [Multi-domain]  Cd Length: 310  Bit Score: 244.71  E-value: 1.81e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259   1 PVSIKGYAGEDP-TPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNTTVPIAAE 79
Cdd:cd01337   50 PAKVTGYLGPEElKKALKGADVVVIPAGVPRKPGMTRDDLFNINAGIVRDLATAVAKACPKALILIISNPVNSTVPIAAE 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189168259  80 VLKKAGVYDKRRLFGITTLDVIRSETFVAELKDKDPGDIRVPVIGGHSGVTILPLLSQVEG-VEFTDE 146
Cdd:cd01337  130 VLKKAGVYDPKRLFGVTTLDVVRANTFVAELLGLDPAKVNVPVIGGHSGVTILPLLSQCQPpFTFDQE 197
PLN00106 PLN00106
malate dehydrogenase
 1-146 7.95e-78

malate dehydrogenase


Pssm-ID: 215058 [Multi-domain]  Cd Length: 323  Bit Score: 233.31  E-value: 7.95e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259   1 PVSIKGYAGEDPTP-ALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNTTVPIAAE 79
Cdd:PLN00106  68 PAQVRGFLGDDQLGdALKGADLVIIPAGVPRKPGMTRDDLFNINAGIVKTLCEAVAKHCPNALVNIISNPVNSTVPIAAE 147

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189168259  80 VLKKAGVYDKRRLFGITTLDVIRSETFVAELKDKDPGDIRVPVIGGHSGVTILPLLSQVEG-VEFTDE 146
Cdd:PLN00106 148 VLKKAGVYDPKKLFGVTTLDVVRANTFVAEKKGLDPADVDVPVVGGHAGITILPLLSQATPkVSFTDE 215
MDH_euk_gproteo TIGR01772
malate dehydrogenase, NAD-dependent; This model represents the NAD-dependent malate ...
 1-141 3.80e-73

malate dehydrogenase, NAD-dependent; This model represents the NAD-dependent malate dehydrogenase found in eukaryotes and certain gamma proteobacteria. The enzyme is involved in the citric acid cycle as well as the glyoxalate cycle. Several isoforms exidt in eukaryotes. In S. cereviseae, for example, there are cytoplasmic, mitochondrial and peroxisomal forms. Although malate dehydrogenases have in some cases been mistaken for lactate dehydrogenases due to the similarity of these two substrates and the apparent ease with which evolution can toggle these activities, critical residues have been identified which can discriminate between the two activities. At the time of the creation of this model no hits above the trusted cutoff contained critical residues typical of lactate dehydrogenases. [Energy metabolism, TCA cycle]


Pssm-ID: 130833 [Multi-domain]  Cd Length: 312  Bit Score: 221.13  E-value: 3.80e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259    1 PVSIKGYAGEDP-TPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNTTVPIAAE 79
Cdd:TIGR01772  49 AASVKGFSGEEGlENALKGADVVVIPAGVPRKPGMTRDDLFNVNAGIVKDLVAAVAESCPKAMILVITNPVNSTVPIAAE 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189168259   80 VLKKAGVYDKRRLFGITTLDVIRSETFVAELKDKDPGDIRVPVIGGHSGVTILPLLSQVEGV 141
Cdd:TIGR01772 129 VLKKKGVYDPNKLFGVTTLDIVRANTFVAELKGKDPMEVNVPVIGGHSGETIIPLISQCPGK 190
Ldh_1_N pfam00056
lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic ...
 1-94 3.67e-31

lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic enzymes which catalyze the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis. L-2-hydroxyisocaproate dehydrogenases are also members of the family. Malate dehydrogenases catalyze the interconversion of malate to oxaloacetate. The enzyme participates in the citric acid cycle. L-lactate dehydrogenase is also found as a lens crystallin in bird and crocodile eyes. N-terminus (this family) is a Rossmann NAD-binding fold. C-terminus is an unusual alpha+beta fold.


Pssm-ID: 395010 [Multi-domain]  Cd Length: 141  Bit Score: 108.46  E-value: 3.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259    1 PVSIKGYAGEDPTPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNttvpIAAEV 80
Cdd:pfam00056  52 FLLVPGIVGGGDYEDLKDADVVVITAGVPRKPGMTRLDLLNVNAKIFKSIGPALAKYAPNAIVLVVSNPVD----ILTYV 127

                          90
                  ....*....|....
gi 189168259   81 LKKAGVYDKRRLFG 94
Cdd:pfam00056 128 AWKASGFPPNRVFG 141
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ...
 11-138 2.21e-29

Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 439809 [Multi-domain]  Cd Length: 302  Bit Score: 108.18  E-value: 2.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259  11 DPTPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNTTVPIAAEVLKkagvYDKR 90
Cdd:COG0039   61 GDYEDLADADVVVITAGAPRKPGMSRLDLLEANAKIFKSVGEAIKKYAPDAIVLVVTNPVDVMTYIAQKASG----LPKE 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 189168259  91 RLFGI-TTLDVIRSETFVAELKDKDPGDIRVPVIGGHsGVTILPLLSQV 138
Cdd:COG0039  137 RVIGMgTVLDSARFRSFLAEKLGVSPRDVHAYVLGEH-GDSMVPLWSHA 184
 
Name Accession Description Interval E-value
MDH_glyoxysomal_mitochondrial cd01337
Glyoxysomal and mitochondrial malate dehydrogenases; MDH is one of the key enzymes in the ...
 1-146 1.81e-82

Glyoxysomal and mitochondrial malate dehydrogenases; MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. Members of this subfamily are localized to the glycosome and mitochondria. MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133422 [Multi-domain]  Cd Length: 310  Bit Score: 244.71  E-value: 1.81e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259   1 PVSIKGYAGEDP-TPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNTTVPIAAE 79
Cdd:cd01337   50 PAKVTGYLGPEElKKALKGADVVVIPAGVPRKPGMTRDDLFNINAGIVRDLATAVAKACPKALILIISNPVNSTVPIAAE 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189168259  80 VLKKAGVYDKRRLFGITTLDVIRSETFVAELKDKDPGDIRVPVIGGHSGVTILPLLSQVEG-VEFTDE 146
Cdd:cd01337  130 VLKKAGVYDPKRLFGVTTLDVVRANTFVAELLGLDPAKVNVPVIGGHSGVTILPLLSQCQPpFTFDQE 197
PLN00106 PLN00106
malate dehydrogenase
 1-146 7.95e-78

malate dehydrogenase


Pssm-ID: 215058 [Multi-domain]  Cd Length: 323  Bit Score: 233.31  E-value: 7.95e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259   1 PVSIKGYAGEDPTP-ALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNTTVPIAAE 79
Cdd:PLN00106  68 PAQVRGFLGDDQLGdALKGADLVIIPAGVPRKPGMTRDDLFNINAGIVKTLCEAVAKHCPNALVNIISNPVNSTVPIAAE 147

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189168259  80 VLKKAGVYDKRRLFGITTLDVIRSETFVAELKDKDPGDIRVPVIGGHSGVTILPLLSQVEG-VEFTDE 146
Cdd:PLN00106 148 VLKKAGVYDPKKLFGVTTLDVVRANTFVAEKKGLDPADVDVPVVGGHAGITILPLLSQATPkVSFTDE 215
MDH_euk_gproteo TIGR01772
malate dehydrogenase, NAD-dependent; This model represents the NAD-dependent malate ...
 1-141 3.80e-73

malate dehydrogenase, NAD-dependent; This model represents the NAD-dependent malate dehydrogenase found in eukaryotes and certain gamma proteobacteria. The enzyme is involved in the citric acid cycle as well as the glyoxalate cycle. Several isoforms exidt in eukaryotes. In S. cereviseae, for example, there are cytoplasmic, mitochondrial and peroxisomal forms. Although malate dehydrogenases have in some cases been mistaken for lactate dehydrogenases due to the similarity of these two substrates and the apparent ease with which evolution can toggle these activities, critical residues have been identified which can discriminate between the two activities. At the time of the creation of this model no hits above the trusted cutoff contained critical residues typical of lactate dehydrogenases. [Energy metabolism, TCA cycle]


Pssm-ID: 130833 [Multi-domain]  Cd Length: 312  Bit Score: 221.13  E-value: 3.80e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259    1 PVSIKGYAGEDP-TPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNTTVPIAAE 79
Cdd:TIGR01772  49 AASVKGFSGEEGlENALKGADVVVIPAGVPRKPGMTRDDLFNVNAGIVKDLVAAVAESCPKAMILVITNPVNSTVPIAAE 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189168259   80 VLKKAGVYDKRRLFGITTLDVIRSETFVAELKDKDPGDIRVPVIGGHSGVTILPLLSQVEGV 141
Cdd:TIGR01772 129 VLKKKGVYDPNKLFGVTTLDIVRANTFVAELKGKDPMEVNVPVIGGHSGETIIPLISQCPGK 190
PTZ00325 PTZ00325
malate dehydrogenase; Provisional
 1-146 2.01e-67

malate dehydrogenase; Provisional


Pssm-ID: 240360 [Multi-domain]  Cd Length: 321  Bit Score: 206.82  E-value: 2.01e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259   1 PVSIKGYA-GEDPTPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNTTVPIAAE 79
Cdd:PTZ00325  58 PAKVTGYAdGELWEKALRGADLVLICAGVPRKPGMTRDDLFNTNAPIVRDLVAAVASSAPKAIVGIVSNPVNSTVPIAAE 137

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189168259  80 VLKKAGVYDKRRLFGITTLDVIRSETFVAELKDKDPGDIRVPVIGGHSGVTILPLLSQVeGVEFTDE 146
Cdd:PTZ00325 138 TLKKAGVYDPRKLFGVTTLDVVRARKFVAEALGMNPYDVNVPVVGGHSGVTIVPLLSQT-GLSLPEE 203
LDH_MDH_like cd00650
NAD-dependent, lactate dehydrogenase-like, 2-hydroxycarboxylate dehydrogenase family; Members ...
 4-138 1.97e-33

NAD-dependent, lactate dehydrogenase-like, 2-hydroxycarboxylate dehydrogenase family; Members of this family include ubiquitous enzymes like L-lactate dehydrogenases (LDH), L-2-hydroxyisocaproate dehydrogenases, and some malate dehydrogenases (MDH). LDH catalyzes the last step of glycolysis in which pyruvate is converted to L-lactate. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH/MDH-like proteins are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133419 [Multi-domain]  Cd Length: 263  Bit Score: 117.81  E-value: 1.97e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259   4 IKGYAGEDPTPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNttvpIAAEVLKK 83
Cdd:cd00650   56 IKVSITDDPYEAFKDADVVIITAGVGRKPGMGRLDLLKRNVPIVKEIGDNIEKYSPDAWIIVVSNPVD----IITYLVWR 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 189168259  84 AGVYDKRRLFGITTLDVIRSETFVAELKDKDPGDIRVPVIGGHSGvTILPLLSQV 138
Cdd:cd00650  132 YSGLPKEKVIGLGTLDPIRFRRILAEKLGVDPDDVKVYILGEHGG-SQVPDWSTV 185
Ldh_1_N pfam00056
lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic ...
 1-94 3.67e-31

lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic enzymes which catalyze the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis. L-2-hydroxyisocaproate dehydrogenases are also members of the family. Malate dehydrogenases catalyze the interconversion of malate to oxaloacetate. The enzyme participates in the citric acid cycle. L-lactate dehydrogenase is also found as a lens crystallin in bird and crocodile eyes. N-terminus (this family) is a Rossmann NAD-binding fold. C-terminus is an unusual alpha+beta fold.


Pssm-ID: 395010 [Multi-domain]  Cd Length: 141  Bit Score: 108.46  E-value: 3.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259    1 PVSIKGYAGEDPTPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNttvpIAAEV 80
Cdd:pfam00056  52 FLLVPGIVGGGDYEDLKDADVVVITAGVPRKPGMTRLDLLNVNAKIFKSIGPALAKYAPNAIVLVVSNPVD----ILTYV 127

                          90
                  ....*....|....
gi 189168259   81 LKKAGVYDKRRLFG 94
Cdd:pfam00056 128 AWKASGFPPNRVFG 141
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ...
 11-138 2.21e-29

Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 439809 [Multi-domain]  Cd Length: 302  Bit Score: 108.18  E-value: 2.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259  11 DPTPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNTTVPIAAEVLKkagvYDKR 90
Cdd:COG0039   61 GDYEDLADADVVVITAGAPRKPGMSRLDLLEANAKIFKSVGEAIKKYAPDAIVLVVTNPVDVMTYIAQKASG----LPKE 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 189168259  91 RLFGI-TTLDVIRSETFVAELKDKDPGDIRVPVIGGHsGVTILPLLSQV 138
Cdd:COG0039  137 RVIGMgTVLDSARFRSFLAEKLGVSPRDVHAYVLGEH-GDSMVPLWSHA 184
PRK06223 PRK06223
malate dehydrogenase; Reviewed
 15-136 1.67e-27

malate dehydrogenase; Reviewed


Pssm-ID: 180477 [Multi-domain]  Cd Length: 307  Bit Score: 103.29  E-value: 1.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259  15 ALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNTTVpiaaEVLKKAGVYDKRRLFG 94
Cdd:PRK06223  67 DIAGSDVVVITAGVPRKPGMSRDDLLGINAKIMKDVAEGIKKYAPDAIVIVVTNPVDAMT----YVALKESGFPKNRVIG 142

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 189168259  95 ITT-LDVIRSETFVAELKDKDPGDIRVPVIGGHsGVTILPLLS 136
Cdd:PRK06223 143 MAGvLDSARFRTFIAEELNVSVKDVTAFVLGGH-GDSMVPLVR 184
LDH-like_MDH cd01339
L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an ...
 16-145 5.34e-27

L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an LDH-like structure and an MDH enzymatic activity. Some members, like MJ0490 from Methanococcus jannaschii, exhibit both MDH and LDH activities. Tetrameric MDHs, including those from phototrophic bacteria, are more similar to LDHs than to other MDHs. LDH catalyzes the last step of glycolysis in which pyruvate is converted to L-lactate. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH-like MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133424 [Multi-domain]  Cd Length: 300  Bit Score: 101.78  E-value: 5.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259  16 LEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNTTVPIAaevLKKAGVyDKRRLFGI 95
Cdd:cd01339   64 IAGSDVVVITAGIPRKPGMSRDDLLGTNAKIVKEVAENIKKYAPNAIVIVVTNPLDVMTYVA---YKASGF-PRNRVIGM 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189168259  96 -TTLDVIRSETFVAELKDKDPGDIRVPVIGGHsGVTILPLL--SQVEGVEFTD 145
Cdd:cd01339  140 aGVLDSARFRYFIAEELGVSVKDVQAMVLGGH-GDTMVPLPrySTVGGIPLTE 191
LDH-like_MDH_nadp cd05294
A lactate dehydrogenases-like structure with malate dehydrogenase enzymatic activity; The ...
 18-136 2.97e-21

A lactate dehydrogenases-like structure with malate dehydrogenase enzymatic activity; The LDH-like MDH proteins have a lactate dehyhydrogenase-like (LDH-like) structure and malate dehydrogenase (MDH) enzymatic activity. This subgroup is composed of some archaeal LDH-like MDHs that prefer NADP(H) rather than NAD(H) as a cofactor. One member, MJ0490 from Methanococcus jannaschii, has been observed to form dimers and tetramers during crystalization, although it is believed to exist primarilly as a tetramer in solution. In addition to its MDH activity, MJ0490 also possesses fructose-1,6-bisphosphate-activated LDH activity. Members of this subgroup have a higher sequence similarity to LDHs than to other MDHs. LDH catalyzes the last step of glycolysis in which pyruvate is converted to L-lactate. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH-like MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)- binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenase, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133430 [Multi-domain]  Cd Length: 309  Bit Score: 87.07  E-value: 2.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259  18 GADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNTTVPIAaevLKKAGvYDKRRLFGITT 97
Cdd:cd05294   72 GSDIVIITAGVPRKEGMSRLDLAKKNAKIVKKYAKQIAEFAPDTKILVVTNPVDVMTYKA---LKESG-FDKNRVFGLGT 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 189168259  98 -LDVIRSETFVAELKDKDPGDIRVPVIGGHsGVTILPLLS 136
Cdd:cd05294  148 hLDSLRFKVAIAKHFNVHISEVHTRIIGEH-GDSMVPLIS 186
PTZ00117 PTZ00117
malate dehydrogenase; Provisional
 9-136 1.19e-19

malate dehydrogenase; Provisional


Pssm-ID: 173409 [Multi-domain]  Cd Length: 319  Bit Score: 82.85  E-value: 1.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259   9 GEDPTPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNttvpIAAEVLKKAGVYD 88
Cdd:PTZ00117  64 GTNNYEDIKDSDVVVITAGVQRKEEMTREDLLTINGKIMKSVAESVKKYCPNAFVICVTNPLD----CMVKVFQEKSGIP 139

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 189168259  89 KRRLFGIT-TLDVIRSETFVAELKDKDPGDIRVPVIGGHsGVTILPLLS 136
Cdd:PTZ00117 140 SNKICGMAgVLDSSRFRCNLAEKLGVSPGDVSAVVIGGH-GDLMVPLPR 187
PTZ00082 PTZ00082
L-lactate dehydrogenase; Provisional
 16-138 4.10e-18

L-lactate dehydrogenase; Provisional


Pssm-ID: 173376 [Multi-domain]  Cd Length: 321  Bit Score: 78.58  E-value: 4.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259  16 LEGADVVLISAGVARKPGM-----DRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNTTVPIaaeVLKKAGVyDKR 90
Cdd:PTZ00082  72 IAGSDVVIVTAGLTKRPGKsdkewNRDDLLPLNAKIMDEVAEGIKKYCPNAFVIVITNPLDVMVKL---LQEHSGL-PKN 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 189168259  91 RLFGIT-TLDVIRSETFVAELKDKDPGDIRVPVIGGHsGVTILPLLSQV 138
Cdd:PTZ00082 148 KVCGMAgVLDSSRLRTYIAEKLGVNPRDVHASVIGAH-GDKMVPLPRYV 195
LDH_like cd00300
L-lactate dehydrogenase-like enzymes; Members of this subfamily are tetrameric NAD-dependent ...
 18-138 2.15e-15

L-lactate dehydrogenase-like enzymes; Members of this subfamily are tetrameric NAD-dependent 2-hydroxycarboxylate dehydrogenases including LDHs, L-2-hydroxyisocaproate dehydrogenases (L-HicDH), and LDH-like malate dehydrogenases (MDH). Dehydrogenases catalyze the conversion of carbonyl compounds to alcohols or amino acids. LDHs catalyze the last step of glycolysis in which pyruvate is converted to L-lactate. Vertebrate LDHs are non-allosteric, but some bacterial LDHs are activated by an allosteric effector such as fructose-1,6-bisphosphate. L-HicDH catalyzes the conversion of a variety of 2-oxo carboxylic acids with medium-sized aliphatic or aromatic side chains. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH-like subfamily is part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133418 [Multi-domain]  Cd Length: 300  Bit Score: 70.76  E-value: 2.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259  18 GADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNttvpIAAEVLKKAGVYDKRRLFGI-T 96
Cdd:cd00300   66 DADIVVITAGAPRKPGETRLDLINRNAPILRSVITNLKKYGPDAIILVVSNPVD----ILTYVAQKLSGLPKNRVIGSgT 141

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 189168259  97 TLDVIRSETFVAELKDKDPGDIRVPVIGGHsGVTILPLLSQV 138
Cdd:cd00300  142 LLDSARFRSLLAEKLDVDPQSVHAYVLGEH-GDSQVVAWSTA 182
HicDH_like cd05291
L-2-hydroxyisocapronate dehydrogenases and some bacterial L-lactate dehydrogenases; ...
 15-146 3.73e-15

L-2-hydroxyisocapronate dehydrogenases and some bacterial L-lactate dehydrogenases; L-2-hydroxyisocapronate dehydrogenase (HicDH) catalyzes the conversion of a variety of 2-oxo carboxylic acids with medium-sized aliphatic or aromatic side chains. This subfamily is composed of HicDHs and some bacterial L-lactate dehydrogenases (LDH). LDHs catalyze the last step of glycolysis in which pyruvate is converted to L-lactate. Bacterial LDHs can be non-allosteric or may be activated by an allosteric effector such as fructose-1,6-bisphosphate. Members of this subfamily with known structures such as the HicDH of Lactobacillus confusus, the non-allosteric LDH of Lactobacillus pentosus, and the allosteric LDH of Bacillus stearothermophilus, show that they exist as homotetramers. The HicDH-like subfamily is part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133427 [Multi-domain]  Cd Length: 306  Bit Score: 70.19  E-value: 3.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259  15 ALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNttvpIAAEVLKKAGVYDKRRLFG 94
Cdd:cd05291   65 DCKDADIVVITAGAPQKPGETRLDLLEKNAKIMKSIVPKIKASGFDGIFLVASNPVD----VITYVVQKLSGLPKNRVIG 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 189168259  95 I-TTLDVIRSETFVAELKDKDPGDIRVPVIGGH--------SGVTIL--PLLSQVEGVEFTDE 146
Cdd:cd05291  141 TgTSLDTARLRRALAEKLNVDPRSVHAYVLGEHgdsqfvawSTVTVGgkPLLDLLKEGKLSEL 203
LDH_2 cd05292
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
 1-126 1.19e-14

A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes catalyzing the last step of glycolysis in which pyruvate is converted to L-lactate. This subgroup is composed predominantly of bacterial LDHs and a few fungal LDHs. Bacterial LDHs may be non-allosteric or may be activated by an allosteric effector such as fructose-1,6-bisphosphate. LDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133428 [Multi-domain]  Cd Length: 308  Bit Score: 69.06  E-value: 1.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259   1 PVSIkgYAG--EDptpaLEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVN--TTVpi 76
Cdd:cd05292   54 PVRI--YAGdyAD----CKGADVVVITAGANQKPGETRLDLLKRNVAIFKEIIPQILKYAPDAILLVVTNPVDvlTYV-- 125

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189168259  77 aaeVLKKAGvYDKRRLFGI-TTLDVIRSETFVAELKDKDPGDIRVPVIGGH 126
Cdd:cd05292  126 ---AYKLSG-LPPNRVIGSgTVLDTARFRYLLGEHLGVDPRSVHAYIIGEH 172
Ldh_1_C pfam02866
lactate/malate dehydrogenase, alpha/beta C-terminal domain; L-lactate dehydrogenases are ...
 96-146 1.69e-13

lactate/malate dehydrogenase, alpha/beta C-terminal domain; L-lactate dehydrogenases are metabolic enzymes which catalyze the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis. L-2-hydroxyisocaproate dehydrogenases are also members of the family. Malate dehydrogenases catalyze the interconversion of malate to oxaloacetate. The enzyme participates in the citric acid cycle. L-lactate dehydrogenase is also found as a lens crystallin in bird and crocodile eyes.


Pssm-ID: 397136  Cd Length: 173  Bit Score: 63.92  E-value: 1.69e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189168259   96 TTLDVIRSETFVAELKDKDPGDIRVPVIGGHSG----------VTILPLLSQVEG-VEFTDE 146
Cdd:pfam02866   1 TTLDINRARTFLAEKAGVDPRVVNVPVIGGHSGtefpdwshanVTIIPLQSQVKEnLKDSEW 62
MDH cd00704
Malate dehydrogenase; Malate dehydrogenase (MDH) is one of the key enzymes in the citric acid ...
 8-137 8.33e-13

Malate dehydrogenase; Malate dehydrogenase (MDH) is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. MDHs belong to the NAD-dependent, lactate dehydrogenase (LDH)-like, 2-hydroxycarboxylate dehydrogenase family, which also includes the GH4 family of glycoside hydrolases. They are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133420 [Multi-domain]  Cd Length: 323  Bit Score: 63.83  E-value: 8.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259   8 AGEDPTPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKI-AVTCPTACVGIITNPVNTTvpiAAEVLKKAGV 86
Cdd:cd00704   66 ITTDPEEAFKDVDVAILVGAFPRKPGMERADLLRKNAKIFKEQGEALnKVAKPTVKVLVVGNPANTN---ALIALKNAPN 142

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 189168259  87 YDKRRLFGITTLDVIRSETFVAELKDKDPGDIR-VPVIGGHSGvTILPLLSQ 137
Cdd:cd00704  143 LPPKNFTALTRLDHNRAKAQVARKLGVRVSDVKnVIIWGNHSN-TQVPDLSN 193
LDH_3 cd05290
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
 15-138 1.07e-12

A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes catalyzing the last step of glycolysis in which pyruvate is converted to L-lactate. This subgroup is composed of some bacterial LDHs from firmicutes, gammaproteobacteria, and actinobacteria. Vertebrate LDHs are non-allosteric, but some bacterial LDHs are activated by an allosteric effector such as fructose-1,6-bisphosphate. LDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenase, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133426 [Multi-domain]  Cd Length: 307  Bit Score: 63.50  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259  15 ALEGADVVLISAGVARKPG--MDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNTTVPIAAEVLKkagvYDKRRL 92
Cdd:cd05290   65 DCADADIIVITAGPSIDPGntDDRLDLAQTNAKIIREIMGNITKVTKEAVIILITNPLDIAVYIAATEFD----YPANKV 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 189168259  93 FGI-TTLDVIRSETFVAELKDKDPGDIRVPVIGGHsGVTILPLLSQV 138
Cdd:cd05290  141 IGTgTMLDTARLRRIVADKYGVDPKNVTGYVLGEH-GSHAFPVWSLV 186
ldh PRK00066
L-lactate dehydrogenase; Reviewed
 17-138 3.35e-11

L-lactate dehydrogenase; Reviewed


Pssm-ID: 178836 [Multi-domain]  Cd Length: 315  Bit Score: 59.52  E-value: 3.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259  17 EGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNttvpIAAEVLKKAGVYDKRRLFGI- 95
Cdd:PRK00066  72 KDADLVVITAGAPQKPGETRLDLVEKNLKIFKSIVGEVMASGFDGIFLVASNPVD----ILTYATWKLSGFPKERVIGSg 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 189168259  96 TTLDVIRSETFVAELKDKDPGDIRVPVIGGHsGVTILPLLSQV 138
Cdd:PRK00066 148 TSLDSARFRYMLSEKLDVDPRSVHAYIIGEH-GDTEFPVWSHA 189
PRK05442 PRK05442
malate dehydrogenase; Provisional
 8-127 2.07e-10

malate dehydrogenase; Provisional


Pssm-ID: 235468 [Multi-domain]  Cd Length: 326  Bit Score: 57.11  E-value: 2.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259   8 AGEDPTPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKI-AVTCPTACVGIITNPVNTTVPIAAevlKKAGV 86
Cdd:PRK05442  70 ITDDPNVAFKDADVALLVGARPRGPGMERKDLLEANGAIFTAQGKALnEVAARDVKVLVVGNPANTNALIAM---KNAPD 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 189168259  87 YDKRRLFGITTLDVIRSETFVAELKDKDPGDI-RVPVIGGHS 127
Cdd:PRK05442 147 LPAENFTAMTRLDHNRALSQLAAKAGVPVADIkKMTVWGNHS 188
MDH_chloroplast-like cd01338
Chloroplast-like malate dehydrogenases; MDH is one of the key enzymes in the citric acid cycle, ...
 8-127 1.12e-09

Chloroplast-like malate dehydrogenases; MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. Members of this subfamily are bacterial MDHs, and plant MDHs localized to the chloroplasts. MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133423 [Multi-domain]  Cd Length: 322  Bit Score: 54.90  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259   8 AGEDPTPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKI-AVTCPTACVGIITNPVNTTVPIAAevlKKAGV 86
Cdd:cd01338   68 ITDDPNVAFKDADWALLVGAKPRGPGMERADLLKANGKIFTAQGKALnDVASRDVKVLVVGNPCNTNALIAM---KNAPD 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 189168259  87 YDKRRLFGITTLDVIRSETFVAELKDKDPGDI-RVPVIGGHS 127
Cdd:cd01338  145 IPPDNFTAMTRLDHNRAKSQLAKKAGVPVTDVkNMVIWGNHS 186
LDH_protist TIGR01756
lactate dehydrogenase; This model represents a family of protist lactate dehydrogenases which ...
 3-145 1.43e-09

lactate dehydrogenase; This model represents a family of protist lactate dehydrogenases which have aparrently evolved from a recent protist malate dehydrogenase ancestor. Lactate dehydrogenase converts the hydroxyl at C-2 of lactate to a carbonyl in the product, pyruvate. The preference of this enzyme for NAD or NADP has not been determined. A critical residue in malate dehydrogenase, arginine-91 (T. vaginalis numbering) has been mutated to a leucine, eliminating the positive charge which complemeted the carboxylate in malate which is absent in lactate. Several other more subtle changes are proposed to make the active site smaller to accomadate the less bulky lactate molecule.


Pssm-ID: 130817  Cd Length: 313  Bit Score: 54.89  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259    3 SIKGYAGED-PTPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTC-PTACVGIITNPVNTTVPIAaeV 80
Cdd:TIGR01756  44 NLAGTIVTTkLEEAFKDIDCAFLVASVPLKPGEVRADLLTKNTPIFKATGEALSEYAkPTVKVLVIGNPVNTNCLVA--M 121

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189168259   81 LKKAGVYDKrRLFGITTLDVIRSETFVAELKDKDPGDIRVPVIGGHSGVTILPLLSQvegVEFTD 145
Cdd:TIGR01756 122 LHAPKLSAE-NFSSLCMLDHNRAVSRIASKLKVPVDHIYHVVVWGNHAESMVADLTH---AEFTK 182
MDH_cytoplasmic_cytosolic cd01336
Cytoplasmic and cytosolic Malate dehydrogenases; MDH is one of the key enzymes in the citric ...
 8-128 7.83e-09

Cytoplasmic and cytosolic Malate dehydrogenases; MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. Members of this subfamily are eukaryotic MDHs localized to the cytoplasm and cytosol. MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133421 [Multi-domain]  Cd Length: 325  Bit Score: 52.63  E-value: 7.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259   8 AGEDPTPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIA-VTCPTACVGIITNPVNTTVPIAaevLKKAGV 86
Cdd:cd01336   68 ATTDPEEAFKDVDVAILVGAMPRKEGMERKDLLKANVKIFKEQGEALDkYAKKNVKVLVVGNPANTNALIL---LKYAPS 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 189168259  87 YDKRRLFGITTLDVIRSETFVAELKDKDPGDIRVPVI-GGHSG 128
Cdd:cd01336  145 IPKENFTALTRLDHNRAKSQIALKLGVPVSDVKNVIIwGNHSS 187
MDH_euk_cyt TIGR01758
malate dehydrogenase, NAD-dependent; This model represents the NAD-dependent cytosolic malate ...
 11-137 3.62e-08

malate dehydrogenase, NAD-dependent; This model represents the NAD-dependent cytosolic malate dehydrogenase from eukaryotes. The enzyme from pig has been studied by X-ray crystallography


Pssm-ID: 130819 [Multi-domain]  Cd Length: 324  Bit Score: 50.61  E-value: 3.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259   11 DPTPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKI-AVTCPTACVGIITNPVNTTvpiaAEVLKKAGVYDK 89
Cdd:TIGR01758  68 DPAVAFTDVDVAILVGAFPRKEGMERRDLLSKNVKIFKEQGRALdKLAKKDCKVLVVGNPANTN----ALVLSNYAPSIP 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 189168259   90 RRLF-GITTLDVIRSETFVAELKDKDPGDIRVPVI-GGHSGvTILPLLSQ 137
Cdd:TIGR01758 144 PKNFsALTRLDHNRALAQVAERAGVPVSDVKNVIIwGNHSS-TQYPDVNH 192
PLN00112 PLN00112
malate dehydrogenase (NADP); Provisional
 2-99 4.68e-07

malate dehydrogenase (NADP); Provisional


Pssm-ID: 215060 [Multi-domain]  Cd Length: 444  Bit Score: 47.52  E-value: 4.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259   2 VSIkgyaGEDPTPALEGADVVLISAGVARKPGMDRADLFNVNAGIV----KSLAEKIAVTCPTACVGiitNPVNTTVPIA 77
Cdd:PLN00112 164 VSI----GIDPYEVFQDAEWALLIGAKPRGPGMERADLLDINGQIFaeqgKALNEVASRNVKVIVVG---NPCNTNALIC 236

                         90       100
                 ....*....|....*....|..
gi 189168259  78 aevLKKAGVYDKRRLFGITTLD 99
Cdd:PLN00112 237 ---LKNAPNIPAKNFHALTRLD 255
Malate-DH_plant TIGR01757
malate dehydrogenase, NADP-dependent; This model represents the NADP-dependent malate ...
 9-127 5.06e-07

malate dehydrogenase, NADP-dependent; This model represents the NADP-dependent malate dehydrogenase found in plants, mosses and green algae and localized to the chloroplast. Malate dehydrogenase converts oxaloacetate into malate, a critical step in the C4 cycle which allows circumvention of the effects of photorespiration. Malate is subsequenctly transported from the chloroplast to the cytoplasm (and then to the bundle sheath cells in C4 plants). The plant and moss enzymes are light regulated via cysteine disulfide bonds. The enzyme from Sorghum has been crystallized.


Pssm-ID: 130818 [Multi-domain]  Cd Length: 387  Bit Score: 47.66  E-value: 5.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259    9 GEDPTPALEGADVVLISAGVARKPGMDRADLFNVNAGIV----KSLAEKIAVTCPTACVGiitNPVNTTVPIAaevLKKA 84
Cdd:TIGR01757 111 GIDPYEVFEDADWALLIGAKPRGPGMERADLLDINGQIFadqgKALNAVASKNCKVLVVG---NPCNTNALIA---MKNA 184

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 189168259   85 GVYDKRRLFGITTLDVIRSETFVAELKDKDPGDI-RVPVIGGHS 127
Cdd:TIGR01757 185 PNIPRKNFHALTRLDENRAKCQLALKSGKFYTSVsNVTIWGNHS 228
PLN00135 PLN00135
malate dehydrogenase
 8-127 9.13e-07

malate dehydrogenase


Pssm-ID: 177744 [Multi-domain]  Cd Length: 309  Bit Score: 46.69  E-value: 9.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259   8 AGEDPTPALEGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTAC-VGIITNPVNTTvpiaAEVLKK-AG 85
Cdd:PLN00135  48 ATTDVVEACKGVNIAVMVGGFPRKEGMERKDVMSKNVSIYKSQASALEKHAAPDCkVLVVANPANTN----ALILKEfAP 123

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 189168259  86 VYDKRRLFGITTLDVIRSETFVAELKDKDPGDIRVPVI-GGHS 127
Cdd:PLN00135 124 SIPEKNITCLTRLDHNRALGQISERLGVPVSDVKNVIIwGNHS 166
LDH_1 cd05293
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
 18-131 3.90e-06

A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes catalyzing the last step of glycolysis in which pyruvate is converted to L-lactate. This subgroup is composed of eukaryotic LDHs. Vertebrate LDHs are non-allosteric. This is in contrast to some bacterial LDHs that are activated by an allosteric effector such as fructose-1,6-bisphosphate. LDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133429 [Multi-domain]  Cd Length: 312  Bit Score: 44.90  E-value: 3.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259  18 GADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNttvpIAAEVLKKAGVYDKRRLFGI-T 96
Cdd:cd05293   71 NSKVVIVTAGARQNEGESRLDLVQRNVDIFKGIIPKLVKYSPNAILLVVSNPVD----IMTYVAWKLSGLPKHRVIGSgC 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 189168259  97 TLDVIRSETFVAELKDKDPGDIRVPVIGGH--------SGVTI 131
Cdd:cd05293  147 NLDSARFRYLIAERLGVAPSSVHGWIIGEHgdssvpvwSGVNV 189
PLN02602 PLN02602
lactate dehydrogenase
 17-138 1.16e-05

lactate dehydrogenase


Pssm-ID: 178212 [Multi-domain]  Cd Length: 350  Bit Score: 43.61  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189168259  17 EGADVVLISAGVARKPGMDRADLFNVNAGIVKSLAEKIAVTCPTACVGIITNPVNTTVPIAaevLKKAGVYDKRRLFGIT 96
Cdd:PLN02602 104 AGSDLCIVTAGARQIPGESRLNLLQRNVALFRKIIPELAKYSPDTILLIVSNPVDVLTYVA---WKLSGFPANRVIGSGT 180

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 189168259  97 TLDVIRSETFVAELKDKDPGDIRVPVIGGHsGVTILPLLSQV 138
Cdd:PLN02602 181 NLDSSRFRFLIADHLDVNAQDVQAYIVGEH-GDSSVALWSSV 221
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH