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Conserved domains on  [gi|17554310|ref|NP_498457|]
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Malate dehydrogenase, mitochondrial [Caenorhabditis elegans]

Protein Classification

malate dehydrogenase( domain architecture ID 10102004)

malate dehydrogenase specifically oxidizes malate to oxaloacetate

CATH:  3.40.50.720
EC:  1.1.1.37
Gene Ontology:  GO:0030060|GO:0006108

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MDH_glyoxysomal_mitochondrial cd01337
Glyoxysomal and mitochondrial malate dehydrogenases; MDH is one of the key enzymes in the ...
30-338 0e+00

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: 550.55  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  30 KVALLGAAGGIGQPLGLLLKQDPLVAHLALYDVVNTPGVAADLSHIDSNAKVTAHTGPKELYAAVENADVIVIPAGVPRK 109
Cdd:cd01337   2 KVAVLGAAGGIGQPLSLLLKLNPLVSELALYDIVNTPGVAADLSHINTPAKVTGYLGPEELKKALKGADVVVIPAGVPRK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 110 PGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNSTVPIASEVLKKAGVYDPKRVFGVTTLDVVRSQAFVSELK 189
Cdd:cd01337  82 PGMTRDDLFNINAGIVRDLATAVAKACPKALILIISNPVNSTVPIAAEVLKKAGVYDPKRLFGVTTLDVVRANTFVAELL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 190 GHDASKTVVPVVGGHAGITIIPLLSQVKPSTKFSEEEISKLTPRIQDAGTEVVNAKAGAGSATLSMALAGARFANALVRG 269
Cdd:cd01337 162 GLDPAKVNVPVIGGHSGVTILPLLSQCQPPFTFDQEEIEALTHRIQFGGDEVVKAKAGAGSATLSMAYAGARFANSLLRG 241
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 270 IKGEKNV-QCAYVASDaVKGVEYFSTPVELGPNGVEKILGVGKVSAYEQKLIDASVPELNKNIAKGVAFV 338
Cdd:cd01337 242 LKGEKGViECAYVESD-VTEAPFFATPVELGKNGVEKNLGLGKLNDYEKKLLEAALPELKKNIEKGVDFV 310
 
Name Accession Description Interval E-value
MDH_glyoxysomal_mitochondrial cd01337
Glyoxysomal and mitochondrial malate dehydrogenases; MDH is one of the key enzymes in the ...
30-338 0e+00

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: 550.55  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  30 KVALLGAAGGIGQPLGLLLKQDPLVAHLALYDVVNTPGVAADLSHIDSNAKVTAHTGPKELYAAVENADVIVIPAGVPRK 109
Cdd:cd01337   2 KVAVLGAAGGIGQPLSLLLKLNPLVSELALYDIVNTPGVAADLSHINTPAKVTGYLGPEELKKALKGADVVVIPAGVPRK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 110 PGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNSTVPIASEVLKKAGVYDPKRVFGVTTLDVVRSQAFVSELK 189
Cdd:cd01337  82 PGMTRDDLFNINAGIVRDLATAVAKACPKALILIISNPVNSTVPIAAEVLKKAGVYDPKRLFGVTTLDVVRANTFVAELL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 190 GHDASKTVVPVVGGHAGITIIPLLSQVKPSTKFSEEEISKLTPRIQDAGTEVVNAKAGAGSATLSMALAGARFANALVRG 269
Cdd:cd01337 162 GLDPAKVNVPVIGGHSGVTILPLLSQCQPPFTFDQEEIEALTHRIQFGGDEVVKAKAGAGSATLSMAYAGARFANSLLRG 241
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 270 IKGEKNV-QCAYVASDaVKGVEYFSTPVELGPNGVEKILGVGKVSAYEQKLIDASVPELNKNIAKGVAFV 338
Cdd:cd01337 242 LKGEKGViECAYVESD-VTEAPFFATPVELGKNGVEKNLGLGKLNDYEKKLLEAALPELKKNIEKGVDFV 310
PLN00106 PLN00106
malate dehydrogenase
15-333 4.27e-175

malate dehydrogenase


Pssm-ID: 215058 [Multi-domain]  Cd Length: 323  Bit Score: 488.31  E-value: 4.27e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   15 SGLRAVSVRHSSQAPKVALLGAAGGIGQPLGLLLKQDPLVAHLALYDVVNTPGVAADLSHIDSNAKVTAHTGPKELYAAV 94
Cdd:PLN00106   5 SSLRACRAKGGAPGFKVAVLGAAGGIGQPLSLLMKMNPLVSELHLYDIANTPGVAADVSHINTPAQVRGFLGDDQLGDAL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   95 ENADVIVIPAGVPRKPGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNSTVPIASEVLKKAGVYDPKRVFGVT 174
Cdd:PLN00106  85 KGADLVIIPAGVPRKPGMTRDDLFNINAGIVKTLCEAVAKHCPNALVNIISNPVNSTVPIAAEVLKKAGVYDPKKLFGVT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  175 TLDVVRSQAFVSELKGHDASKTVVPVVGGHAGITIIPLLSQVKPSTKFSEEEISKLTPRIQDAGTEVVNAKAGAGSATLS 254
Cdd:PLN00106 165 TLDVVRANTFVAEKKGLDPADVDVPVVGGHAGITILPLLSQATPKVSFTDEEIEALTKRIQNGGTEVVEAKAGAGSATLS 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  255 MALAGARFANALVRGIKGEKNV-QCAYVASDaVKGVEYFSTPVELGPNGVEKILGVGKVSAYEQKLIDASVPELNKNIAK 333
Cdd:PLN00106 245 MAYAAARFADACLRGLNGEADVvECSYVQSE-VTELPFFASKVRLGRNGVEEVLGLGPLSEYEQKGLEALKPELKASIEK 323
MDH_euk_gproteo TIGR01772
malate dehydrogenase, NAD-dependent; This model represents the NAD-dependent malate ...
30-339 4.26e-160

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: 449.93  E-value: 4.26e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310    30 KVALLGAAGGIGQPLGLLLKQDPLVAHLALYDVVNTPGVAADLSHIDSNAKVTAHTGPKELYAAVENADVIVIPAGVPRK 109
Cdd:TIGR01772   1 KVAVLGAAGGIGQPLSLLLKLQPYVSELSLYDIAGAAGVAADLSHIPTAASVKGFSGEEGLENALKGADVVVIPAGVPRK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   110 PGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNSTVPIASEVLKKAGVYDPKRVFGVTTLDVVRSQAFVSELK 189
Cdd:TIGR01772  81 PGMTRDDLFNVNAGIVKDLVAAVAESCPKAMILVITNPVNSTVPIAAEVLKKKGVYDPNKLFGVTTLDIVRANTFVAELK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   190 GHDASKTVVPVVGGHAGITIIPLLSQVKPSTKFSEEEISKLTPRIQDAGTEVVNAKAGAGSATLSMALAGARFANALVRG 269
Cdd:TIGR01772 161 GKDPMEVNVPVIGGHSGETIIPLISQCPGKVLFTEDQLEALIHRIQNAGTEVVKAKAGAGSATLSMAFAGARFVLSLVRG 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17554310   270 IKGEKNV-QCAYVASDAVKGVEYFSTPVELGPNGVEKILGVGKVSAYEQKLIDASVPELNKNIAKGVAFVK 339
Cdd:TIGR01772 241 LKGEEGVvECAYVESDGVTEATFFATPLLLGKNGVEKRLGIGKLSSFEEKMLNGALPELKKNIKKGEEFVA 311
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ...
30-332 6.85e-51

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: 170.97  E-value: 6.85e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  30 KVALLGAaGGIGQPLGLLLKQDPLVAHLALYDVVNTP--GVAADLSH----IDSNAKVTAHTgpkelYAAVENADVIVIP 103
Cdd:COG0039   2 KVAIIGA-GNVGSTLAFRLASGGLADELVLIDINEGKaeGEALDLADafplLGFDVKITAGD-----YEDLADADVVVIT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 104 AGVPRKPGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNstvpIASEVLKKAGVYDPKRVFGV-TTLDVVRSQ 182
Cdd:COG0039  76 AGAPRKPGMSRLDLLEANAKIFKSVGEAIKKYAPDAIVLVVTNPVD----VMTYIAQKASGLPKERVIGMgTVLDSARFR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 183 AFVSELKGHDASKTVVPVVGGHaGITIIPLLSQV----KPSTKF---SEEEISKLTPRIQDAGTEVVNAKagaGSATLSM 255
Cdd:COG0039 152 SFLAEKLGVSPRDVHAYVLGEH-GDSMVPLWSHAtvggIPLTELikeTDEDLDEIIERVRKGGAEIIEGK---GSTYYAI 227
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17554310 256 ALAGARFANALVRgikGEKNVQCAYVASDAVKGVE--YFSTPVELGPNGVEKILGVgKVSAYEQKLIDASVPELNKNIA 332
Cdd:COG0039 228 AAAAARIVEAILR---DEKRVLPVSVYLDGEYGIEdvYLGVPVVIGRNGVEKIVEL-ELTDEERAKLDASAEELKEEID 302
Ldh_1_C pfam02866
lactate/malate dehydrogenase, alpha/beta C-terminal domain; L-lactate dehydrogenases are ...
174-338 8.65e-50

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: 164.07  E-value: 8.65e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   174 TTLDVVRSQAFVSELKGHDASKTVVPVVGGHAG----------ITIIPLLSQVKPSTKFSEEEISKLTPRIQDAGTEVVN 243
Cdd:pfam02866   1 TTLDINRARTFLAEKAGVDPRVVNVPVIGGHSGtefpdwshanVTIIPLQSQVKENLKDSEWELEELTHRVQNAGYEVIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   244 AKagAGSATLSMALAGARFANALVRGIKGEKNV---QCAYVasdAVKGVEYFSTPVELGPNGVEKILGVGKVSAYEQKLI 320
Cdd:pfam02866  81 AK--AGSATLSMAVAGARFIRAILRGEGGVLSVgvyEDGYY---GVPDDIYFSFPVVLGKDGVEKVLEIGPLNDFEREKM 155
                         170
                  ....*....|....*...
gi 17554310   321 DASVPELNKNIAKGVAFV 338
Cdd:pfam02866 156 EKSAAELKKEIEKGFAFV 173
 
Name Accession Description Interval E-value
MDH_glyoxysomal_mitochondrial cd01337
Glyoxysomal and mitochondrial malate dehydrogenases; MDH is one of the key enzymes in the ...
30-338 0e+00

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: 550.55  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  30 KVALLGAAGGIGQPLGLLLKQDPLVAHLALYDVVNTPGVAADLSHIDSNAKVTAHTGPKELYAAVENADVIVIPAGVPRK 109
Cdd:cd01337   2 KVAVLGAAGGIGQPLSLLLKLNPLVSELALYDIVNTPGVAADLSHINTPAKVTGYLGPEELKKALKGADVVVIPAGVPRK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 110 PGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNSTVPIASEVLKKAGVYDPKRVFGVTTLDVVRSQAFVSELK 189
Cdd:cd01337  82 PGMTRDDLFNINAGIVRDLATAVAKACPKALILIISNPVNSTVPIAAEVLKKAGVYDPKRLFGVTTLDVVRANTFVAELL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 190 GHDASKTVVPVVGGHAGITIIPLLSQVKPSTKFSEEEISKLTPRIQDAGTEVVNAKAGAGSATLSMALAGARFANALVRG 269
Cdd:cd01337 162 GLDPAKVNVPVIGGHSGVTILPLLSQCQPPFTFDQEEIEALTHRIQFGGDEVVKAKAGAGSATLSMAYAGARFANSLLRG 241
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 270 IKGEKNV-QCAYVASDaVKGVEYFSTPVELGPNGVEKILGVGKVSAYEQKLIDASVPELNKNIAKGVAFV 338
Cdd:cd01337 242 LKGEKGViECAYVESD-VTEAPFFATPVELGKNGVEKNLGLGKLNDYEKKLLEAALPELKKNIEKGVDFV 310
PLN00106 PLN00106
malate dehydrogenase
15-333 4.27e-175

malate dehydrogenase


Pssm-ID: 215058 [Multi-domain]  Cd Length: 323  Bit Score: 488.31  E-value: 4.27e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   15 SGLRAVSVRHSSQAPKVALLGAAGGIGQPLGLLLKQDPLVAHLALYDVVNTPGVAADLSHIDSNAKVTAHTGPKELYAAV 94
Cdd:PLN00106   5 SSLRACRAKGGAPGFKVAVLGAAGGIGQPLSLLMKMNPLVSELHLYDIANTPGVAADVSHINTPAQVRGFLGDDQLGDAL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   95 ENADVIVIPAGVPRKPGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNSTVPIASEVLKKAGVYDPKRVFGVT 174
Cdd:PLN00106  85 KGADLVIIPAGVPRKPGMTRDDLFNINAGIVKTLCEAVAKHCPNALVNIISNPVNSTVPIAAEVLKKAGVYDPKKLFGVT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  175 TLDVVRSQAFVSELKGHDASKTVVPVVGGHAGITIIPLLSQVKPSTKFSEEEISKLTPRIQDAGTEVVNAKAGAGSATLS 254
Cdd:PLN00106 165 TLDVVRANTFVAEKKGLDPADVDVPVVGGHAGITILPLLSQATPKVSFTDEEIEALTKRIQNGGTEVVEAKAGAGSATLS 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  255 MALAGARFANALVRGIKGEKNV-QCAYVASDaVKGVEYFSTPVELGPNGVEKILGVGKVSAYEQKLIDASVPELNKNIAK 333
Cdd:PLN00106 245 MAYAAARFADACLRGLNGEADVvECSYVQSE-VTELPFFASKVRLGRNGVEEVLGLGPLSEYEQKGLEALKPELKASIEK 323
MDH_euk_gproteo TIGR01772
malate dehydrogenase, NAD-dependent; This model represents the NAD-dependent malate ...
30-339 4.26e-160

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: 449.93  E-value: 4.26e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310    30 KVALLGAAGGIGQPLGLLLKQDPLVAHLALYDVVNTPGVAADLSHIDSNAKVTAHTGPKELYAAVENADVIVIPAGVPRK 109
Cdd:TIGR01772   1 KVAVLGAAGGIGQPLSLLLKLQPYVSELSLYDIAGAAGVAADLSHIPTAASVKGFSGEEGLENALKGADVVVIPAGVPRK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   110 PGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNSTVPIASEVLKKAGVYDPKRVFGVTTLDVVRSQAFVSELK 189
Cdd:TIGR01772  81 PGMTRDDLFNVNAGIVKDLVAAVAESCPKAMILVITNPVNSTVPIAAEVLKKKGVYDPNKLFGVTTLDIVRANTFVAELK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   190 GHDASKTVVPVVGGHAGITIIPLLSQVKPSTKFSEEEISKLTPRIQDAGTEVVNAKAGAGSATLSMALAGARFANALVRG 269
Cdd:TIGR01772 161 GKDPMEVNVPVIGGHSGETIIPLISQCPGKVLFTEDQLEALIHRIQNAGTEVVKAKAGAGSATLSMAFAGARFVLSLVRG 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17554310   270 IKGEKNV-QCAYVASDAVKGVEYFSTPVELGPNGVEKILGVGKVSAYEQKLIDASVPELNKNIAKGVAFVK 339
Cdd:TIGR01772 241 LKGEEGVvECAYVESDGVTEATFFATPLLLGKNGVEKRLGIGKLSSFEEKMLNGALPELKKNIKKGEEFVA 311
PTZ00325 PTZ00325
malate dehydrogenase; Provisional
23-338 2.60e-148

malate dehydrogenase; Provisional


Pssm-ID: 240360 [Multi-domain]  Cd Length: 321  Bit Score: 420.61  E-value: 2.60e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   23 RHSSQAP--KVALLGAAGGIGQPLGLLLKQDPLVAHLALYDVVNTPGVAADLSHIDSNAKVTAHTGPKELYAAVENADVI 100
Cdd:PTZ00325   1 MRPSALKmfKVAVLGAAGGIGQPLSLLLKQNPHVSELSLYDIVGAPGVAADLSHIDTPAKVTGYADGELWEKALRGADLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  101 VIPAGVPRKPGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNSTVPIASEVLKKAGVYDPKRVFGVTTLDVVR 180
Cdd:PTZ00325  81 LICAGVPRKPGMTRDDLFNTNAPIVRDLVAAVASSAPKAIVGIVSNPVNSTVPIAAETLKKAGVYDPRKLFGVTTLDVVR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  181 SQAFVSELKGHDASKTVVPVVGGHAGITIIPLLSQVKPStkFSEEEISKLTPRIQDAGTEVVNAKAGAGSATLSMALAGA 260
Cdd:PTZ00325 161 ARKFVAEALGMNPYDVNVPVVGGHSGVTIVPLLSQTGLS--LPEEQVEQITHRVQVGGDEVVKAKEGAGSATLSMAYAAA 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17554310  261 RFANALVRGIKGEKN-VQCAYVASDAVKGVEYFSTPVELGPNGVEKILGVGKVSAYEQKLIDASVPELNKNIAKGVAFV 338
Cdd:PTZ00325 239 EWSTSVLKALRGDKGiVECAFVESDMRPECPFFSSPVELGKEGVERVLPIGPLNAYEEELLEAAVPDLKKNIEKGLEFA 317
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ...
30-332 6.85e-51

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: 170.97  E-value: 6.85e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  30 KVALLGAaGGIGQPLGLLLKQDPLVAHLALYDVVNTP--GVAADLSH----IDSNAKVTAHTgpkelYAAVENADVIVIP 103
Cdd:COG0039   2 KVAIIGA-GNVGSTLAFRLASGGLADELVLIDINEGKaeGEALDLADafplLGFDVKITAGD-----YEDLADADVVVIT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 104 AGVPRKPGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNstvpIASEVLKKAGVYDPKRVFGV-TTLDVVRSQ 182
Cdd:COG0039  76 AGAPRKPGMSRLDLLEANAKIFKSVGEAIKKYAPDAIVLVVTNPVD----VMTYIAQKASGLPKERVIGMgTVLDSARFR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 183 AFVSELKGHDASKTVVPVVGGHaGITIIPLLSQV----KPSTKF---SEEEISKLTPRIQDAGTEVVNAKagaGSATLSM 255
Cdd:COG0039 152 SFLAEKLGVSPRDVHAYVLGEH-GDSMVPLWSHAtvggIPLTELikeTDEDLDEIIERVRKGGAEIIEGK---GSTYYAI 227
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17554310 256 ALAGARFANALVRgikGEKNVQCAYVASDAVKGVE--YFSTPVELGPNGVEKILGVgKVSAYEQKLIDASVPELNKNIA 332
Cdd:COG0039 228 AAAAARIVEAILR---DEKRVLPVSVYLDGEYGIEdvYLGVPVVIGRNGVEKIVEL-ELTDEERAKLDASAEELKEEID 302
Ldh_1_C pfam02866
lactate/malate dehydrogenase, alpha/beta C-terminal domain; L-lactate dehydrogenases are ...
174-338 8.65e-50

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: 164.07  E-value: 8.65e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   174 TTLDVVRSQAFVSELKGHDASKTVVPVVGGHAG----------ITIIPLLSQVKPSTKFSEEEISKLTPRIQDAGTEVVN 243
Cdd:pfam02866   1 TTLDINRARTFLAEKAGVDPRVVNVPVIGGHSGtefpdwshanVTIIPLQSQVKENLKDSEWELEELTHRVQNAGYEVIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   244 AKagAGSATLSMALAGARFANALVRGIKGEKNV---QCAYVasdAVKGVEYFSTPVELGPNGVEKILGVGKVSAYEQKLI 320
Cdd:pfam02866  81 AK--AGSATLSMAVAGARFIRAILRGEGGVLSVgvyEDGYY---GVPDDIYFSFPVVLGKDGVEKVLEIGPLNDFEREKM 155
                         170
                  ....*....|....*...
gi 17554310   321 DASVPELNKNIAKGVAFV 338
Cdd:pfam02866 156 EKSAAELKKEIEKGFAFV 173
Ldh_1_N pfam00056
lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic ...
30-172 1.44e-48

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: 159.69  E-value: 1.44e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310    30 KVALLGAAGGIGQPLGLLLKQDPLVAHLALYDVV--NTPGVAADLSHIDSNAKVTAHTGPKeLYAAVENADVIVIPAGVP 107
Cdd:pfam00056   2 KVAVVGAAGGVGQSLAFLLANKGLADELVLYDIVkeKLEGVAMDLSHGSTFLLVPGIVGGG-DYEDLKDADVVVITAGVP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17554310   108 RKPGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNstvpIASEVLKKAGVYDPKRVFG 172
Cdd:pfam00056  81 RKPGMTRLDLLNVNAKIFKSIGPALAKYAPNAIVLVVSNPVD----ILTYVAWKASGFPPNRVFG 141
LDH-like_MDH cd01339
L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an ...
31-332 5.41e-46

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: 158.41  E-value: 5.41e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  31 VALLGAaGGIGQPLGLLLKQDPLvAHLALYDVV-NTP-GVAADLSH----IDSNAKVTAHTGpkelYAAVENADVIVIPA 104
Cdd:cd01339   1 ISIIGA-GNVGATLAQLLALKEL-GDVVLLDIVeGLPqGKALDISQaapiLGSDTKVTGTND----YEDIAGSDVVVITA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 105 GVPRKPGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNSTVpiasEVLKKAGVYDPKRVFGV-TTLDVVRSQA 183
Cdd:cd01339  75 GIPRKPGMSRDDLLGTNAKIVKEVAENIKKYAPNAIVIVVTNPLDVMT----YVAYKASGFPRNRVIGMaGVLDSARFRY 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 184 FVSELKGHDASKTVVPVVGGHaGITIIPLLSQV----KPSTKF-SEEEISKLTPRIQDAGTEVVNAKaGAGSATLSMALA 258
Cdd:cd01339 151 FIAEELGVSVKDVQAMVLGGH-GDTMVPLPRYStvggIPLTELiTKEEIDEIVERTRNGGAEIVNLL-KTGSAYYAPAAA 228
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17554310 259 GARFANALVrgiKGEKNVQ--CAYVASDA-VKGVeYFSTPVELGPNGVEKILGVgKVSAYEQKLIDASVPELNKNIA 332
Cdd:cd01339 229 IAEMVEAIL---KDKKRVLpcSAYLEGEYgIKDI-FVGVPVVLGKNGVEKIIEL-DLTDEEKEAFDKSVESVKELID 300
PRK06223 PRK06223
malate dehydrogenase; Reviewed
29-333 6.92e-46

malate dehydrogenase; Reviewed


Pssm-ID: 180477 [Multi-domain]  Cd Length: 307  Bit Score: 158.37  E-value: 6.92e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   29 PKVALLGAaGGIGQPLGLLLKQDPLvAHLALYDVV-NTP-GVAADLSH----IDSNAKVTAHTGpkelYAAVENADVIVI 102
Cdd:PRK06223   3 KKISIIGA-GNVGATLAHLLALKEL-GDVVLFDIVeGVPqGKALDIAEaapvEGFDTKITGTND----YEDIAGSDVVVI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  103 PAGVPRKPGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNSTVpiasEVLKKAGVYDPKRVFGVTT-LDVVRS 181
Cdd:PRK06223  77 TAGVPRKPGMSRDDLLGINAKIMKDVAEGIKKYAPDAIVIVVTNPVDAMT----YVALKESGFPKNRVIGMAGvLDSARF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  182 QAFVSELKGHDASKTVVPVVGGHaGITIIPLLSQ-----VKPSTKFSEEEISKLTPRIQDAGTEVVNAKaGAGSATLSMA 256
Cdd:PRK06223 153 RTFIAEELNVSVKDVTAFVLGGH-GDSMVPLVRYstvggIPLEDLLSKEKLDEIVERTRKGGAEIVGLL-KTGSAYYAPA 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  257 LAGArfanALVRGI-KGEKNV--QCAYVasDAVKGVE--YFSTPVELGPNGVEKILGVgKVSAYEQKLIDASVPELNKNI 331
Cdd:PRK06223 231 ASIA----EMVEAIlKDKKRVlpCSAYL--EGEYGVKdvYVGVPVKLGKNGVEKIIEL-ELDDEEKAAFDKSVEAVKKLI 303

                 ..
gi 17554310  332 AK 333
Cdd:PRK06223 304 EA 305
LDH_MDH_like cd00650
NAD-dependent, lactate dehydrogenase-like, 2-hydroxycarboxylate dehydrogenase family; Members ...
31-331 1.53e-39

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: 140.53  E-value: 1.53e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  31 VALLGAAGGIGQPL--GLLLKQDPLVAHLALYDVVN--TPGVAADLSHIDSNAKVTAHTGPKELYAAVENADVIVIPAGV 106
Cdd:cd00650   1 IAVIGAGGNVGPALafGLADGSVLLAIELVLYDIDEekLKGVAMDLQDAVEPLADIKVSITDDPYEAFKDADVVIITAGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 107 PRKPGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNstvpIASEVLKKAGVYDPKRVFGVTTLDVVRSQAFVS 186
Cdd:cd00650  81 GRKPGMGRLDLLKRNVPIVKEIGDNIEKYSPDAWIIVVSNPVD----IITYLVWRYSGLPKEKVIGLGTLDPIRFRRILA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 187 ELKGHDASKTVVPVVGGHAGiTIIPLLSQVKpstkfseeeiskltpriqdagtevvnakagagsatlsMALAGARFANAL 266
Cdd:cd00650 157 EKLGVDPDDVKVYILGEHGG-SQVPDWSTVR-------------------------------------IATSIADLIRSL 198
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17554310 267 VRgikGEKNVQCAYVASDAVKGVE---YFSTPVELGPNGVEKILGVGKvSAYEQKLIDASVPELNKNI 331
Cdd:cd00650 199 LN---DEGEILPVGVRNNGQIGIPddvVVSVPCIVGKNGVEEPIEVGL-TDFELEKLQKSADTLKKEL 262
PTZ00117 PTZ00117
malate dehydrogenase; Provisional
29-332 1.87e-33

malate dehydrogenase; Provisional


Pssm-ID: 173409 [Multi-domain]  Cd Length: 319  Bit Score: 125.60  E-value: 1.87e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   29 PKVALLGAaGGIGQPLGLLLKQDPLvAHLALYDVVN--TPGVAADLSH----IDSNAKVTAHTGpkelYAAVENADVIVI 102
Cdd:PTZ00117   6 KKISMIGA-GQIGSTVALLILQKNL-GDVVLYDVIKgvPQGKALDLKHfstlVGSNINILGTNN----YEDIKDSDVVVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  103 PAGVPRKPGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNSTVpiasEVLKKAGVYDPKRVFGVT-TLDVVRS 181
Cdd:PTZ00117  80 TAGVQRKEEMTREDLLTINGKIMKSVAESVKKYCPNAFVICVTNPLDCMV----KVFQEKSGIPSNKICGMAgVLDSSRF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  182 QAFVSELKGHDASKTVVPVVGGHaGITIIPLLSQVK----PSTKF------SEEEISKLTPRIQDAGTEVVNAkAGAGSA 251
Cdd:PTZ00117 156 RCNLAEKLGVSPGDVSAVVIGGH-GDLMVPLPRYCTvngiPLSDFvkkgaiTEKEINEIIKKTRNMGGEIVKL-LKKGSA 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  252 TLSMALAGARFANALvrgIKGEKNVQCAYVASDAVKGVE--YFSTPVELGPNGVEKILGVgKVSAYEQKLID---ASVPE 326
Cdd:PTZ00117 234 FFAPAAAIVAMIEAY---LKDEKRVLVCSVYLNGQYNCKnlFVGVPVVIGGKGIEKVIEL-ELNAEEKELFDksiESIQE 309

                 ....*.
gi 17554310  327 LNKNIA 332
Cdd:PTZ00117 310 LTQKAK 315
PTZ00082 PTZ00082
L-lactate dehydrogenase; Provisional
25-328 6.04e-33

L-lactate dehydrogenase; Provisional


Pssm-ID: 173376 [Multi-domain]  Cd Length: 321  Bit Score: 124.42  E-value: 6.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   25 SSQAPKVALLGAaGGIGQPLGLLLKQDPLvAHLALYDVV-NTP-GVAADLSHI----DSNAKVTAHTGpkelYAAVENAD 98
Cdd:PTZ00082   3 MIKRRKISLIGS-GNIGGVMAYLIVLKNL-GDVVLFDIVkNIPqGKALDISHSnviaGSNSKVIGTNN----YEDIAGSD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   99 VIVIPAGVPRKPGMT-----RDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNSTVPIaseVLKKAGVyDPKRVFGV 173
Cdd:PTZ00082  77 VVIVTAGLTKRPGKSdkewnRDDLLPLNAKIMDEVAEGIKKYCPNAFVIVITNPLDVMVKL---LQEHSGL-PKNKVCGM 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  174 T-TLDVVRSQAFVSELKGHDASKTVVPVVGGHaGITIIPLLSQVK----PSTKF------SEEEISKLTPRIQDAGTEVV 242
Cdd:PTZ00082 153 AgVLDSSRLRTYIAEKLGVNPRDVHASVIGAH-GDKMVPLPRYVTvggiPLSEFikkgliTQEEIDEIVERTRNTGKEIV 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  243 NAkAGAGSATLSMALAGARFANALVRGIKgeKNVQCAYVASD--AVKGVeYFSTPVELGPNGVEKILGVgKVSAYEQKLI 320
Cdd:PTZ00082 232 DL-LGTGSAYFAPAAAAIEMAEAYLKDKK--RVLPCSAYLEGqyGHKDI-YMGTPAVIGANGVEKIIEL-DLTPEEQKKF 306

                 ....*...
gi 17554310  321 DASVPELN 328
Cdd:PTZ00082 307 DESIKEVK 314
LDH_like cd00300
L-lactate dehydrogenase-like enzymes; Members of this subfamily are tetrameric NAD-dependent ...
31-331 1.61e-32

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: 122.76  E-value: 1.61e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  31 VALLGAaGGIGQPLGLLLKQDPLVAHLALYDVVN--TPGVAADLSHIDSNAKVTAHTGPkELYAAVENADVIVIPAGVPR 108
Cdd:cd00300   1 ITIIGA-GNVGAAVAFALIAKGLASELVLVDVNEekAKGDALDLSHASAFLATGTIVRG-GDYADAADADIVVITAGAPR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 109 KPGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNstvpIASEVLKKAGVYDPKRVFGV-TTLDVVRSQAFVSE 187
Cdd:cd00300  79 KPGETRLDLINRNAPILRSVITNLKKYGPDAIILVVSNPVD----ILTYVAQKLSGLPKNRVIGSgTLLDSARFRSLLAE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 188 LKGHDASKTVVPVVGGHaGITIIPLLSQVK-------PSTKFSEEEISKLTPRIQDAGTEVVNAKagaGSATLSMALAGA 260
Cdd:cd00300 155 KLDVDPQSVHAYVLGEH-GDSQVVAWSTATvgglpleELAPFTKLDLEAIEEEVRTSGYEIIRLK---GATNYGIATAIA 230
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17554310 261 RFANALVRGIKGEKNVQcAYVasDAVKGVE--YFSTPVELGPNGVEKILGVgKVSAYEQKLIDASVPELNKNI 331
Cdd:cd00300 231 DIVKSILLDERRVLPVS-AVQ--EGQYGIEdvALSVPAVVGREGVVRILEI-PLTEDEEAKLQKSAEALKEVL 299
MalateDH_bact TIGR01763
malate dehydrogenase, NAD-dependent; This enzyme converts malate into oxaloacetate in the ...
30-331 2.35e-32

malate dehydrogenase, NAD-dependent; This enzyme converts malate into oxaloacetate in the citric acid cycle. The critical residues which discriminate malate dehydrogenase from lactate dehydrogenase have been characterized, and have been used to set the cutoffs for this model. Sequences showing [aflimv][ap]R[rk]pgM[st] and [ltv][ilm]gGhgd were kept above trusted, while those in which the capitalized residues in the patterns were found to be Q, E and E were kept below the noise cutoff. Some sequences in the grey zone have been annotated as malate dehydrogenases, but none have been characterized. Phylogenetically, a clade of sequences from eukaryotes such as Toxoplasma and Plasmodium which include a characterized lactate dehydrogenase and show abiguous critical residue patterns appears to be more closely related to these bacterial sequences than other eukaryotic sequences. These are relatively long branch and have been excluded from the model. All other sequences falling below trusted appear to be phylogenetically outside of the clade including the trusted hits. The annotation of Botryococcus braunii as lactate dehydrogenase appears top be in error. This was initially annotated as MDH by Swiss-Prot and then changed. The rationale for either of these annotations is not traceable. [Energy metabolism, TCA cycle]


Pssm-ID: 273792 [Multi-domain]  Cd Length: 305  Bit Score: 122.67  E-value: 2.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310    30 KVALLGAaGGIGQPLGLLLKQDPLvAHLALYDVVNTP--GVAADLSHIDS----NAKVTAHTGpkelYAAVENADVIVIP 103
Cdd:TIGR01763   3 KISVIGA-GFVGATTAFRLAEKEL-ADLVLLDVVEGIpqGKALDMYEASPvggfDTKVTGTNN----YADTANSDIVVIT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   104 AGVPRKPGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNSTVPIASEvlkKAGVydPK-RVFGVT-TLDVVRS 181
Cdd:TIGR01763  77 AGLPRKPGMSREDLLSMNAGIVREVTGRIMEHSPNPIIVVVSNPLDAMTYVAWQ---KSGF--PKeRVIGQAgVLDSARF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   182 QAFVSELKGHDASKTVVPVVGGHaGITIIPL-----LSQVKPSTKFSEEEISKLTPRIQDAGTEVVNAkAGAGSATLSMA 256
Cdd:TIGR01763 152 RTFIAMELGVSVQDVTACVLGGH-GDAMVPLvrystVAGIPVADLISAERIAEIVERTRKGGGEIVNL-LKQGSAYYAPA 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17554310   257 LAGARFANALVrgiKGEKNVQCAYVASDAVKGVE--YFSTPVELGPNGVEKILGVgKVSAYEQKLIDASVPELNKNI 331
Cdd:TIGR01763 230 ASVVEMVEAIL---KDRKRVLPCAAYLDGQYGIDgiYVGVPVILGKNGVEHIYEL-KLDQSELALLNKSAKIVDENC 302
L-LDH-NAD TIGR01771
L-lactate dehydrogenase; This model represents the NAD-dependent L-lactate dehydrogenases from ...
53-324 1.76e-29

L-lactate dehydrogenase; This model represents the NAD-dependent L-lactate dehydrogenases from bacteria and eukaryotes. This enzyme function as as the final step in anaerobic glycolysis. Although lactate dehydrogenases have in some cases been mistaken for malate 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 malate dehydrogenases. [Energy metabolism, Anaerobic, Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 273796 [Multi-domain]  Cd Length: 299  Bit Score: 114.60  E-value: 1.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310    53 LVAHLALYDVVN--TPGVAADLSH----IDSNAKVTAHTgpkelYAAVENADVIVIPAGVPRKPGMTRDDLFNTNAGIVR 126
Cdd:TIGR01771  20 IADEIVLIDINKdkAEGEAMDLQHaasfLPTPKKIRSGD-----YSDCKDADLVVITAGAPQKPGETRLELVGRNVRIMK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   127 DLAAVIAKASPKALIAIITNPVNstvpIASEVLKKAGVYDPKRVFGV-TTLDVVRSQAFVSELKGHDASKTVVPVVGGH- 204
Cdd:TIGR01771  95 SIVPEVVKSGFDGIFLVATNPVD----ILTYVAWKLSGFPKNRVIGSgTVLDTARLRYLLAEKLGVDPQSVHAYIIGEHg 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   205 ---------AGITIIPLLSQVKPSTKFSEEEISKLTPRIQDAGTEVVNAKagaGSATLSMALAGARFANALvrgIKGEKN 275
Cdd:TIGR01771 171 dsevpvwssATIGGVPLLDYLKAKGTETDLDLEEIEKEVRDAAYEIINRK---GATYYGIGMAVARIVEAI---LHDENR 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 17554310   276 VQCAYVASDAVKGVE--YFSTPVELGPNGVEKILGVgKVSAYEQKLIDASV 324
Cdd:TIGR01771 245 VLPVSAYLDGEYGIKdvYIGVPAVLGRNGVEEIIEL-PLSDEEKEAFQKSA 294
HicDH_like cd05291
L-2-hydroxyisocapronate dehydrogenases and some bacterial L-lactate dehydrogenases; ...
30-333 1.50e-28

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: 112.18  E-value: 1.50e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  30 KVALLGAaGGIGQPLGLLLKQDPLVAHLALYDVVNTP--GVAADLSH----IDSNAKVTAHTgpkelYAAVENADVIVIP 103
Cdd:cd05291   2 KVVIIGA-GHVGSSFAYSLVNQGIADELVLIDINEEKaeGEALDLEDalafLPSPVKIKAGD-----YSDCKDADIVVIT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 104 AGVPRKPGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNStvpIASEVLKKAGvYDPKRVFGV-TTLDVVRSQ 182
Cdd:cd05291  76 AGAPQKPGETRLDLLEKNAKIMKSIVPKIKASGFDGIFLVASNPVDV---ITYVVQKLSG-LPKNRVIGTgTSLDTARLR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 183 AFVSELKGHDASKTVVPVVGGHaGITIIPLLSQV----KP------STKFSEEEISKLTPRIQDAGTEVVNAKagaGSAT 252
Cdd:cd05291 152 RALAEKLNVDPRSVHAYVLGEH-GDSQFVAWSTVtvggKPlldllkEGKLSELDLDEIEEDVRKAGYEIINGK---GATY 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 253 LSMALAGARFANALvrgIKGEKNVQCAYVASDAVKGVE--YFSTPVELGPNGVEKILGVgKVSAYEQKLIDASVPELNKN 330
Cdd:cd05291 228 YGIATALARIVKAI---LNDENAILPVSAYLDGEYGEKdvYIGVPAIIGRNGVEEVIEL-DLTEEEQEKFEKSADIIKEN 303

                ...
gi 17554310 331 IAK 333
Cdd:cd05291 304 IKK 306
LDH-like_MDH_nadp cd05294
A lactate dehydrogenases-like structure with malate dehydrogenase enzymatic activity; The ...
30-309 4.06e-28

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: 111.34  E-value: 4.06e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  30 KVALLGAAGGIGQPLGLLLKQDPLVAHLALY----DVVNTPGVAAD----LSHIDSNAKVTAHTGpkelYAAVENADVIV 101
Cdd:cd05294   2 KVSIIGASGRVGSATALLLAKEDVVKEINLIsrpkSLEKLKGLRLDiydaLAAAGIDAEIKISSD----LSDVAGSDIVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 102 IPAGVPRKPGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNSTVPIAsevLKKAGvYDPKRVFGVTT-LDVVR 180
Cdd:cd05294  78 ITAGVPRKEGMSRLDLAKKNAKIVKKYAKQIAEFAPDTKILVVTNPVDVMTYKA---LKESG-FDKNRVFGLGThLDSLR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 181 SQAFVSELKGHDASKTVVPVVGGHaGITIIPLLSQVK----PSTKFSEEE---ISKLTPRIQDAGTEVVNAKAGA----G 249
Cdd:cd05294 154 FKVAIAKHFNVHISEVHTRIIGEH-GDSMVPLISSTSiggiPIKRFPEYKdfdVEKIVETVKNAGQNIISLKGGSeygpA 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17554310 250 SATLSmalagarfanaLVRGI-KGEKNVQ--CAYVAS--DAVKGVeYFSTPVELGPNGVEKILGV 309
Cdd:cd05294 233 SAISN-----------LVRTIaNDERRILtvSTYLEGeiDGIRDV-CIGVPVKLGKNGIEEIVPI 285
ldh PRK00066
L-lactate dehydrogenase; Reviewed
30-333 2.58e-24

L-lactate dehydrogenase; Reviewed


Pssm-ID: 178836 [Multi-domain]  Cd Length: 315  Bit Score: 100.74  E-value: 2.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   30 KVALLGAaGGIGQPLGLLLKQDPLVAHLALYDVV--NTPGVAADLSHIdsnakvTAHTGPKELYAA----VENADVIVIP 103
Cdd:PRK00066   8 KVVLVGD-GAVGSSYAYALVNQGIADELVIIDINkeKAEGDAMDLSHA------VPFTSPTKIYAGdysdCKDADLVVIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  104 AGVPRKPGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNstvpIASEVLKKAGVYDPKRVFGV-TTLDVVRSQ 182
Cdd:PRK00066  81 AGAPQKPGETRLDLVEKNLKIFKSIVGEVMASGFDGIFLVASNPVD----ILTYATWKLSGFPKERVIGSgTSLDSARFR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  183 AFVSELKGHDASK-----------TVVPVVgGHAGITIIPLLSQVKPSTKFSEEEISKLTPRIQDAGTEVVNAKaGAGSA 251
Cdd:PRK00066 157 YMLSEKLDVDPRSvhayiigehgdTEFPVW-SHANVAGVPLEEYLEENEQYDEEDLDEIFENVRDAAYEIIEKK-GATYY 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  252 TLSMALA---GARFAN--------ALVRGIKGEKNVqcayvasdavkgveYFSTPVELGPNGVEKILGVgKVSAYEQKLI 320
Cdd:PRK00066 235 GIAMALAritKAILNNenavlpvsAYLEGQYGEEDV--------------YIGVPAVVNRNGIREIVEL-PLNDDEKQKF 299
                        330
                 ....*....|...
gi 17554310  321 DASVPELNKNIAK 333
Cdd:PRK00066 300 AHSADVLKEIMDE 312
LDH_2 cd05292
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
30-332 2.33e-22

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: 95.25  E-value: 2.33e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  30 KVALLGAaGGIGQPLGLLLKQDPLVAHLALYDVvNTP---GVAADLSHidsnakVTAHTGPKELYAA----VENADVIVI 102
Cdd:cd05292   2 KVAIVGA-GFVGSTTAYALLLRGLASEIVLVDI-NKAkaeGEAMDLAH------GTPFVKPVRIYAGdyadCKGADVVVI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 103 PAGVPRKPGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNstvpIASEVLKKAGVYDPKRVFGV-TTLDVVRS 181
Cdd:cd05292  74 TAGANQKPGETRLDLLKRNVAIFKEIIPQILKYAPDAILLVVTNPVD----VLTYVAYKLSGLPPNRVIGSgTVLDTARF 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 182 QAFVSELKGHDASKTVVPVVGGH----------AGITIIPLLS-QVKPSTKFSEEEISKLTPRIQDAGTEVVNAKagaGS 250
Cdd:cd05292 150 RYLLGEHLGVDPRSVHAYIIGEHgdsevavwssANIGGVPLDEfCKLCGRPFDEEVREEIFEEVRNAAYEIIERK---GA 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 251 ATLSMALAGARFANALVRgikGEKNVQCAYVASDAVKGVE--YFSTPVELGPNGVEKILGVgKVSAYEQKLIDASVPELN 328
Cdd:cd05292 227 TYYAIGLALARIVEAILR---DENSVLTVSSLLDGQYGIKdvALSLPCIVGRSGVERVLPP-PLSEEEEEALRASAEVLK 302

                ....
gi 17554310 329 KNIA 332
Cdd:cd05292 303 EAIE 306
LDH_1 cd05293
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
26-323 1.81e-18

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: 84.58  E-value: 1.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  26 SQAPKVALLGAaGGIGQPLGLLLKQDPLVAHLALYDVVN--TPGVAADLSH---IDSNAKVTAHTGpkelYAAVENADVI 100
Cdd:cd05293   1 KPRNKVTVVGV-GQVGMACAISILAKGLADELVLVDVVEdkLKGEAMDLQHgsaFLKNPKIEADKD----YSVTANSKVV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 101 VIPAGVPRKPGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNstvpIASEVLKKAGVYDPKRVFGV-TTLDVV 179
Cdd:cd05293  76 IVTAGARQNEGESRLDLVQRNVDIFKGIIPKLVKYSPNAILLVVSNPVD----IMTYVAWKLSGLPKHRVIGSgCNLDSA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 180 RSQAFVSELKGHDASKTVVPVVGGH--------AGITI--IPLLSQVK-PSTKFSEEEISKLTPRIQDAGTEVVNAKaga 248
Cdd:cd05293 152 RFRYLIAERLGVAPSSVHGWIIGEHgdssvpvwSGVNVagVRLQDLNPdIGTDKDPEKWKEVHKQVVDSAYEVIKLK--- 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 249 GSATLSMALAGARFANALVRGIKgeknvQCAYVASDA--VKGVE---YFSTPVELGPNGVEKILGVgKVSAYEQKLIDAS 323
Cdd:cd05293 229 GYTSWAIGLSVADLVDAILRNTG-----RVHSVSTLVkgLHGIEdevFLSLPCILGENGITHVIKQ-PLTEEEQEKLQKS 302
MDH cd00704
Malate dehydrogenase; Malate dehydrogenase (MDH) is one of the key enzymes in the citric acid ...
30-327 5.43e-18

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: 83.09  E-value: 5.43e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  30 KVALLGAAGGIGQPL------GLLLKQDPLVaHLALYDvvNTP------GVAADLshIDSN----AKVTAHTGPKElyaA 93
Cdd:cd00704   2 HVLITGAAGQIGYNLlfliasGELFGDDQPV-ILHLLD--IPPamkaleGVVMEL--QDCAfpllKGVVITTDPEE---A 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  94 VENADVIVIPAGVPRKPGMTRDDLFNTNAGIVRDLAAVIAK-ASPKALIAIITNPVNSTVPIAsevLKKAGVYDPKRVFG 172
Cdd:cd00704  74 FKDVDVAILVGAFPRKPGMERADLLRKNAKIFKEQGEALNKvAKPTVKVLVVGNPANTNALIA---LKNAPNLPPKNFTA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 173 VTTLDVVRSQAFVSELKGHDASKTV-VPVVGGHAGiTIIPLLSQVK----PSTKFSEEEISK------LTPRIQDAGTEV 241
Cdd:cd00704 151 LTRLDHNRAKAQVARKLGVRVSDVKnVIIWGNHSN-TQVPDLSNAVvygpGGTEWVLDLLDEewlndeFVKTVQKRGAAI 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 242 VNAKaGAGSAtLSMALAGARFANALVRGIKGEKNVQCAYVASDAVKGVE---YFSTPVELgPNGVEKILGVGKVSAYEQK 318
Cdd:cd00704 230 IKKR-GASSA-ASAAKAIADHVKDWLFGTPPGEIVSMGVYSPGNPYGIPpgiVFSFPCTC-KGGGWHVVEDLKLNDWLRE 306

                ....*....
gi 17554310 319 LIDASVPEL 327
Cdd:cd00704 307 KLKATEEEL 315
LDH_3 cd05290
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
53-307 2.22e-17

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: 81.22  E-value: 2.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  53 LVAHLALYDVvnTPGVAA----DLSHIDS-----NAKVTAHTgpkelYAAVENADVIVIPAGVPRKPGMT--RDDLFNTN 121
Cdd:cd05290  23 LFSEIVLIDV--NEGVAEgealDFHHATAltystNTKIRAGD-----YDDCADADIIVITAGPSIDPGNTddRLDLAQTN 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 122 AGIVRDLAAVIAKASPKALIAIITNPVNSTVPIASEVLKkagvYDPKRVFGV-TTLDVVRSQAFVSELKGHDaSKTVVPV 200
Cdd:cd05290  96 AKIIREIMGNITKVTKEAVIILITNPLDIAVYIAATEFD----YPANKVIGTgTMLDTARLRRIVADKYGVD-PKNVTGY 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 201 VGGHAGITIIPLLSQV--------KPSTKFSEEEISK--LTPRIQDAGTEVVNAKaGAGSATLSMAlagarfANALVRGI 270
Cdd:cd05290 171 VLGEHGSHAFPVWSLVniaglpldELEALFGKEPIDKdeLLEEVVQAAYDVFNRK-GWTNAGIAKS------ASRLIKAI 243
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 17554310 271 K-GEKNVQCAYVASDAVKGVE--YFSTPVELGPNGVEKIL 307
Cdd:cd05290 244 LlDERSILPVCTLLSGEYGLSdvALSLPTVIGAKGIERVL 283
MDH_chloroplast-like cd01338
Chloroplast-like malate dehydrogenases; MDH is one of the key enzymes in the citric acid cycle, ...
30-327 2.01e-15

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: 75.70  E-value: 2.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  30 KVALLGAAGGIGQPL------GLLLKQDPLVAhLALYDVVNT----PGVAADLShiDSN----AKVTAHTGPKElyaAVE 95
Cdd:cd01338   4 RVAVTGAAGQIGYSLlfriasGEMFGPDQPVI-LQLLELPQAlkalEGVAMELE--DCAfpllAEIVITDDPNV---AFK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  96 NADVIVIPAGVPRKPGMTRDDLFNTNAGIVRDLAAVIAK-ASPKALIAIITNPVNSTVPIAsevLKKAGVYDPKRVFGVT 174
Cdd:cd01338  78 DADWALLVGAKPRGPGMERADLLKANGKIFTAQGKALNDvASRDVKVLVVGNPCNTNALIA---MKNAPDIPPDNFTAMT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 175 TLDVVRSQAFVselkghdASKTVVPV-------VGGHAGITIIPLLSQVKPSTKFSEEEI-------SKLTPRIQDAGTE 240
Cdd:cd01338 155 RLDHNRAKSQL-------AKKAGVPVtdvknmvIWGNHSPTQYPDFTNATIGGKPAAEVIndrawleDEFIPTVQKRGAA 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 241 VVNAKaGAGSAtlsmalagARFANALVRGIK------GEKNVQCAYVASDAVKGVE---YFSTPVELGPNGVEKILGVgK 311
Cdd:cd01338 228 IIKAR-GASSA--------ASAANAAIDHMRdwvlgtPEGDWFSMAVPSDGSYGIPeglIFSFPVRSKGGGYEIVEGL-E 297
                       330
                ....*....|....*.
gi 17554310 312 VSAYEQKLIDASVPEL 327
Cdd:cd01338 298 IDDFAREKIDATLAEL 313
PLN02602 PLN02602
lactate dehydrogenase
5-309 7.03e-14

lactate dehydrogenase


Pssm-ID: 178212 [Multi-domain]  Cd Length: 350  Bit Score: 71.73  E-value: 7.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310    5 AKTLVQAAANSGLRAVSVRHSsqapKVALLGAaGGIGQPLG-LLLKQDpLVAHLALYDVV--NTPGVAADLSHIDS---N 78
Cdd:PLN02602  18 SQAFFKPIHNSSPPSPTRRHT----KVSVVGV-GNVGMAIAqTILTQD-LADELALVDVNpdKLRGEMLDLQHAAAflpR 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   79 AKVTAHTGpkelYAAVENADVIVIPAGVPRKPGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNstvpIASEV 158
Cdd:PLN02602  92 TKILASTD----YAVTAGSDLCIVTAGARQIPGESRLNLLQRNVALFRKIIPELAKYSPDTILLIVSNPVD----VLTYV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  159 LKKAGVYDPKRVFGV-TTLDVVRSQAFVSELKGHDASKTVVPVVGGHaGITIIPLLSQV------------KPSTKFSEE 225
Cdd:PLN02602 164 AWKLSGFPANRVIGSgTNLDSSRFRFLIADHLDVNAQDVQAYIVGEH-GDSSVALWSSVsvggvpvlsfleKQQIAYEKE 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  226 EISKLTPRIQDAGTEVVNAKagaGSATLSMALAGARFANALVRgikGEKNVQCAYVASDAVKGVE----YFSTPVELGPN 301
Cdd:PLN02602 243 TLEEIHRAVVDSAYEVIKLK---GYTSWAIGYSVASLVRSLLR---DQRRIHPVSVLAKGFHGIDegdvFLSLPAQLGRN 316

                 ....*...
gi 17554310  302 GVekiLGV 309
Cdd:PLN02602 317 GV---LGV 321
MDH_euk_cyt TIGR01758
malate dehydrogenase, NAD-dependent; This model represents the NAD-dependent cytosolic malate ...
30-327 2.20e-11

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: 64.10  E-value: 2.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310    30 KVALLGAAGGIGQPL------GLLLKQD-PLVAHL----ALYDVVNtpGVAADLshIDSN----AKVTAHTGPKElyaAV 94
Cdd:TIGR01758   1 RVVVTGAAGQIGYALlpmiarGRMLGKDqPIILHLldipPAMKVLE--GVVMEL--MDCAfpllDGVVPTHDPAV---AF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310    95 ENADVIVIPAGVPRKPGMTRDDLFNTNAGIVRDLAAVIAK-ASPKALIAIITNPVNSTVPIASEVlkkAGVYDPKRVFGV 173
Cdd:TIGR01758  74 TDVDVAILVGAFPRKEGMERRDLLSKNVKIFKEQGRALDKlAKKDCKVLVVGNPANTNALVLSNY---APSIPPKNFSAL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   174 TTLDVVRSQAFVSELKG-HDASKTVVPVVGGHAGiTIIPLLSQVKPSTKFSEEEISKL-----------TPRIQDAGTEV 241
Cdd:TIGR01758 151 TRLDHNRALAQVAERAGvPVSDVKNVIIWGNHSS-TQYPDVNHATVTKGGKQKPVREAikddayldgefITTVQQRGAAI 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   242 VNAKagAGSATLSMALAGARFANALVRGIKGEKNVQCAyVASD-----AVKGVeYFSTPVELgPNGVEKILGVGKVSAYE 316
Cdd:TIGR01758 230 IRAR--KLSSALSAAKAAVDQMHDWVLGTPEGTFVSMG-VYSDgspygVPKGL-IFSFPVTC-KNGEWKIVEGLCVDDSS 304
                         330
                  ....*....|.
gi 17554310   317 QKLIDASVPEL 327
Cdd:TIGR01758 305 RKKLALTAKEL 315
MDH_cytoplasmic_cytosolic cd01336
Cytoplasmic and cytosolic Malate dehydrogenases; MDH is one of the key enzymes in the citric ...
30-327 4.26e-10

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: 59.95  E-value: 4.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  30 KVALLGAAGGIGQPL------GLLLKQDPLVAhLALYDVvnTP------GVAADLshIDSN----AKVTAHTGPKElyaA 93
Cdd:cd01336   4 RVLVTGAAGQIAYSLlpmiakGDVFGPDQPVI-LHLLDI--PPalkaleGVVMEL--QDCAfpllKSVVATTDPEE---A 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  94 VENADVIVIPAGVPRKPGMTRDDLFNTNAGIVRDLAAVIAK-ASPKALIAIITNPVNSTVPIASevlKKAGVYDPKRVFG 172
Cdd:cd01336  76 FKDVDVAILVGAMPRKEGMERKDLLKANVKIFKEQGEALDKyAKKNVKVLVVGNPANTNALILL---KYAPSIPKENFTA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 173 VTTLDVVRSQAFVSELKG--------------HdaSKTVVPVVgGHAGITI----IPLLSQVKPSTKFSEEEIskltPRI 234
Cdd:cd01336 153 LTRLDHNRAKSQIALKLGvpvsdvknviiwgnH--SSTQYPDV-NHATVELngkgKPAREAVKDDAWLNGEFI----STV 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310 235 QDAGTEVVNAKAgagsatLSMALAGARFANALVR----GIKGEKNVQCAyVASDAVKGVE---YFSTPVELgPNGVEKIL 307
Cdd:cd01336 226 QKRGAAVIKARK------LSSAMSAAKAICDHVHdwwfGTPEGEFVSMG-VYSDGSYGVPeglIFSFPVTC-KNGKWKIV 297
                       330       340
                ....*....|....*....|
gi 17554310 308 GVGKVSAYEQKLIDASVPEL 327
Cdd:cd01336 298 QGLSIDDFSREKIDATAKEL 317
PRK05442 PRK05442
malate dehydrogenase; Provisional
26-327 3.72e-09

malate dehydrogenase; Provisional


Pssm-ID: 235468 [Multi-domain]  Cd Length: 326  Bit Score: 57.11  E-value: 3.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   26 SQAP-KVALLGAAGGIGQPL------GLLLKQDPLVAhLALYDVvnTP------GVAADLShiDSN----AKVTAHTGPK 88
Cdd:PRK05442   1 MKAPvRVAVTGAAGQIGYSLlfriasGDMLGKDQPVI-LQLLEI--PPalkaleGVVMELD--DCAfpllAGVVITDDPN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   89 ElyaAVENADVIVIPAGVPRKPGMTRDDLFNTNAGIVRDLAAVIAK-ASPKALIAIITNPVNSTVPIAsevLKKAGVYDP 167
Cdd:PRK05442  76 V---AFKDADVALLVGARPRGPGMERKDLLEANGAIFTAQGKALNEvAARDVKVLVVGNPANTNALIA---MKNAPDLPA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  168 KRVFGVTTLDVVRSQAFVselkghdASKTVVPV-------VGG-----------HAGITIIPLLSQVKPSTKFSEEEIsk 229
Cdd:PRK05442 150 ENFTAMTRLDHNRALSQL-------AAKAGVPVadikkmtVWGnhsatqypdfrHATIDGKPAAEVINDQAWLEDTFI-- 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  230 ltPRIQDAGTEVVNAKaGAGSATlSMALAGARFANALVRGIKGEKNVQCAyVASDAVKGVE---YFSTPVELGPNGVEKI 306
Cdd:PRK05442 221 --PTVQKRGAAIIEAR-GASSAA-SAANAAIDHVRDWVLGTPEGDWVSMG-VPSDGSYGIPeglIFGFPVTCENGEYEIV 295
                        330       340
                 ....*....|....*....|.
gi 17554310  307 LGVgKVSAYEQKLIDASVPEL 327
Cdd:PRK05442 296 QGL-EIDDFSREKIDATLAEL 315
PLN00135 PLN00135
malate dehydrogenase
81-327 5.34e-06

malate dehydrogenase


Pssm-ID: 177744 [Multi-domain]  Cd Length: 309  Bit Score: 47.46  E-value: 5.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   81 VTAHTGPKElyaAVENADVIVIPAGVPRKPGMTRDDLFNTNAGIVRDLAAVIAK-ASPKALIAIITNPVNSTVPIASEVl 159
Cdd:PLN00135  46 VVATTDVVE---ACKGVNIAVMVGGFPRKEGMERKDVMSKNVSIYKSQASALEKhAAPDCKVLVVANPANTNALILKEF- 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  160 kkAGVYDPKRVFGVTTLDVVRSQAFVSELKGHDASKTVVPVVGGHAGITIIPLLSQVKPSTKFSEEEISKLT-------- 231
Cdd:PLN00135 122 --APSIPEKNITCLTRLDHNRALGQISERLGVPVSDVKNVIIWGNHSSTQYPDVNHATVKTPSGEKPVRELVaddawlng 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  232 ---PRIQDAGTEVVnaKAGAGSATLSMALAGARFANALVRGIKGEKNVQCAyVASDAVKGVE---YFSTPVELGpNGVEK 305
Cdd:PLN00135 200 efiTTVQQRGAAII--KARKLSSALSAASSACDHIRDWVLGTPEGTWVSMG-VYSDGSYGVPpglIYSFPVTCE-KGEWS 275
                        250       260
                 ....*....|....*....|..
gi 17554310  306 ILGVGKVSAYEQKLIDASVPEL 327
Cdd:PLN00135 276 IVQGLSIDEFSRKKMDATAKEL 297
LDH_protist TIGR01756
lactate dehydrogenase; This model represents a family of protist lactate dehydrogenases which ...
79-216 1.53e-05

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: 46.03  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310    79 AKVTAHTGPKElyaAVENADVIVIPAGVPRKPGMTRDDLFNTNAGIVRDLAAVIAK-ASPKALIAIITNPVNSTVPIAse 157
Cdd:TIGR01756  46 AGTIVTTKLEE---AFKDIDCAFLVASVPLKPGEVRADLLTKNTPIFKATGEALSEyAKPTVKVLVIGNPVNTNCLVA-- 120
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17554310   158 vLKKAGVYDPKRVFGVTTLDVVRSqafVSELkghdASKTVVPV-------VGGHAGITIIPLLSQV 216
Cdd:TIGR01756 121 -MLHAPKLSAENFSSLCMLDHNRA---VSRI----ASKLKVPVdhiyhvvVWGNHAESMVADLTHA 178
Malate-DH_plant TIGR01757
malate dehydrogenase, NADP-dependent; This model represents the NADP-dependent malate ...
30-258 2.51e-05

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: 45.73  E-value: 2.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310    30 KVALLGAAGGIGQPLGLLL-------KQDPLVAHL--------ALydvvntPGVAADLShiDSN----AKVTAHTGPKEL 90
Cdd:TIGR01757  46 NVAVSGAAGMISNHLLFMLasgevfgQDQPIALKLlgserskeAL------EGVAMELE--DSLypllREVSIGIDPYEV 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310    91 YaavENADVIVIPAGVPRKPGMTRDDLFNTNAGIVRDLA-AVIAKASPKALIAIITNPVNSTVPIAsevLKKAGVYDPKR 169
Cdd:TIGR01757 118 F---EDADWALLIGAKPRGPGMERADLLDINGQIFADQGkALNAVASKNCKVLVVGNPCNTNALIA---MKNAPNIPRKN 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   170 VFGVTTLDVVRSQAFVSELKGHDASK-TVVPVVGGH----------AGITIIPLLSQVKpSTKFSEEEiskLTPRIQDAG 238
Cdd:TIGR01757 192 FHALTRLDENRAKCQLALKSGKFYTSvSNVTIWGNHsttqvpdfvnAKIGGRPAKEVIK-DTKWLEEE---FTPTVQKRG 267
                         250       260
                  ....*....|....*....|..
gi 17554310   239 TEVVN--AKAGAGSATLSMALA 258
Cdd:TIGR01757 268 GALIKkwGRSSAASTAVSIADA 289
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
30-141 2.78e-04

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 42.27  E-value: 2.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  30 KVALLGAAGGIGQPLGLLLKQDPlvahlalYDVV---NTPGVAADLSHIDsnaKVTAHTG----PKELYAAVENADVIVI 102
Cdd:COG0451   1 RILVTGGAGFIGSHLARRLLARG-------HEVVgldRSPPGAANLAALP---GVEFVRGdlrdPEALAAALAGVDAVVH 70
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 17554310 103 PAGVPRKPGMTRDDLFNTNAGIVRDLAAVIAKASPKALI 141
Cdd:COG0451  71 LAAPAGVGEEDPDETLEVNVEGTLNLLEAARAAGVKRFV 109
PLN00112 PLN00112
malate dehydrogenase (NADP); Provisional
80-258 6.36e-04

malate dehydrogenase (NADP); Provisional


Pssm-ID: 215060 [Multi-domain]  Cd Length: 444  Bit Score: 41.35  E-value: 6.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   80 KVTAHTGPKELYAAVENADVIvipAGVPRKPGMTRDDLFNTNAGIVRDLA-AVIAKASPKALIAIITNPVNSTVPIAsev 158
Cdd:PLN00112 163 EVSIGIDPYEVFQDAEWALLI---GAKPRGPGMERADLLDINGQIFAEQGkALNEVASRNVKVIVVGNPCNTNALIC--- 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310  159 LKKAGVYDPKRVFGVTTLDVVRSQAFVSeLKGHDASKTV--VPVVGGH----------AGITIIPlLSQVKPSTKFSEEE 226
Cdd:PLN00112 237 LKNAPNIPAKNFHALTRLDENRAKCQLA-LKAGVFYDKVsnVTIWGNHsttqvpdflnAKINGLP-VKEVITDHKWLEEE 314
                        170       180       190
                 ....*....|....*....|....*....|....
gi 17554310  227 iskLTPRIQDAGTEVVN--AKAGAGSATLSMALA 258
Cdd:PLN00112 315 ---FTPKVQKRGGVLIKkwGRSSAASTAVSIADA 345
PRK14193 PRK14193
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
30-125 7.11e-03

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 237637 [Multi-domain]  Cd Length: 284  Bit Score: 37.69  E-value: 7.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554310   30 KVALLGAAGGIGQPLGLLLKQDPLvahlalydvvntpgvaadlshidsNAKVT-AHTGPKELYAAVENADVIVIPAGVpr 108
Cdd:PRK14193 160 HVVVIGRGVTVGRPIGLLLTRRSE------------------------NATVTlCHTGTRDLAAHTRRADIIVAAAGV-- 213
                         90
                 ....*....|....*..
gi 17554310  109 kPGMTRDDLFNTNAGIV 125
Cdd:PRK14193 214 -AHLVTADMVKPGAAVL 229
 
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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