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Conserved domains on  [gi|18858959|ref|NP_571321|]
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L-lactate dehydrogenase A chain [Danio rerio]

Protein Classification

LDH_1 domain-containing protein (domain architecture ID 10143083)

LDH_1 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LDH_1 cd05293
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
19-330 0e+00

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  Cd Length: 312  Bit Score: 559.91  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  19 GPTNKVTVVGVGMVGMAAAVSILLKDLTDELALVDVMEDKLKGEAMDLQHGSLFLKTHKIVADKDYSVTANSKVVVVTAG 98
Cdd:cd05293   1 KPRNKVTVVGVGQVGMACAISILAKGLADELVLVDVVEDKLKGEAMDLQHGSAFLKNPKIEADKDYSVTANSKVVIVTAG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  99 ARQQEGESRLNLVQRNVNIFKFIIPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEK 178
Cdd:cd05293  81 ARQNEGESRLDLVQRNVDIFKGIIPKLVKYSPNAILLVVSNPVDIMTYVAWKLSGLPKHRVIGSGCNLDSARFRYLIAER 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 179 LGIHPSSCHGWVVGEHGDSSVPVWSGVNVAGVSLQALNPDLGTDKDKEDWKSVHKMVVDSAYEVIKLKGYTSWAIGMSVA 258
Cdd:cd05293 161 LGVAPSSVHGWIIGEHGDSSVPVWSGVNVAGVRLQDLNPDIGTDKDPEKWKEVHKQVVDSAYEVIKLKGYTSWAIGLSVA 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18858959 259 DLCESILKNMHKCHPVSTLVKGMHGVNEEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETLWGVQKE 330
Cdd:cd05293 241 DLVDAILRNTGRVHSVSTLVKGLHGIEDEVFLSLPCILGENGITHVIKQPLTEEEQEKLQKSADTLWEVQKQ 312
 
Name Accession Description Interval E-value
LDH_1 cd05293
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
19-330 0e+00

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  Cd Length: 312  Bit Score: 559.91  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  19 GPTNKVTVVGVGMVGMAAAVSILLKDLTDELALVDVMEDKLKGEAMDLQHGSLFLKTHKIVADKDYSVTANSKVVVVTAG 98
Cdd:cd05293   1 KPRNKVTVVGVGQVGMACAISILAKGLADELVLVDVVEDKLKGEAMDLQHGSAFLKNPKIEADKDYSVTANSKVVIVTAG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  99 ARQQEGESRLNLVQRNVNIFKFIIPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEK 178
Cdd:cd05293  81 ARQNEGESRLDLVQRNVDIFKGIIPKLVKYSPNAILLVVSNPVDIMTYVAWKLSGLPKHRVIGSGCNLDSARFRYLIAER 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 179 LGIHPSSCHGWVVGEHGDSSVPVWSGVNVAGVSLQALNPDLGTDKDKEDWKSVHKMVVDSAYEVIKLKGYTSWAIGMSVA 258
Cdd:cd05293 161 LGVAPSSVHGWIIGEHGDSSVPVWSGVNVAGVRLQDLNPDIGTDKDPEKWKEVHKQVVDSAYEVIKLKGYTSWAIGLSVA 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18858959 259 DLCESILKNMHKCHPVSTLVKGMHGVNEEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETLWGVQKE 330
Cdd:cd05293 241 DLVDAILRNTGRVHSVSTLVKGLHGIEDEVFLSLPCILGENGITHVIKQPLTEEEQEKLQKSADTLWEVQKQ 312
L-LDH-NAD TIGR01771
L-lactate dehydrogenase; This model represents the NAD-dependent L-lactate dehydrogenases from ...
39-325 8.83e-157

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  Cd Length: 299  Bit Score: 445.11  E-value: 8.83e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959    39 SILLKDLTDELALVDVMEDKLKGEAMDLQHGSLFLKTHKIVADKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIF 118
Cdd:TIGR01771  14 ALLNQGIADEIVLIDINKDKAEGEAMDLQHAASFLPTPKKIRSGDYSDCKDADLVVITAGAPQKPGETRLELVGRNVRIM 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   119 KFIIPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVVGEHGDSS 198
Cdd:TIGR01771  94 KSIVPEVVKSGFDGIFLVATNPVDILTYVAWKLSGFPKNRVIGSGTVLDTARLRYLLAEKLGVDPQSVHAYIIGEHGDSE 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   199 VPVWSGVNVAGVSLQALNPDLGTDKDKEDWKsVHKMVVDSAYEVIKLKGYTSWAIGMSVADLCESILKNMHKCHPVSTLV 278
Cdd:TIGR01771 174 VPVWSSATIGGVPLLDYLKAKGTETDLDLEE-IEKEVRDAAYEIINRKGATYYGIGMAVARIVEAILHDENRVLPVSAYL 252
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 18858959   279 KGMHGVNeEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETLW 325
Cdd:TIGR01771 253 DGEYGIK-DVYIGVPAVLGRNGVEEIIELPLSDEEKEAFQKSAETLK 298
PLN02602 PLN02602
lactate dehydrogenase
39-333 8.45e-149

lactate dehydrogenase


Pssm-ID: 178212  Cd Length: 350  Bit Score: 426.88  E-value: 8.45e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   39 SILLKDLTDELALVDVMEDKLKGEAMDLQHGSLFLKTHKIVADKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIF 118
Cdd:PLN02602  55 TILTQDLADELALVDVNPDKLRGEMLDLQHAAAFLPRTKILASTDYAVTAGSDLCIVTAGARQIPGESRLNLLQRNVALF 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  119 KFIIPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVVGEHGDSS 198
Cdd:PLN02602 135 RKIIPELAKYSPDTILLIVSNPVDVLTYVAWKLSGFPANRVIGSGTNLDSSRFRFLIADHLDVNAQDVQAYIVGEHGDSS 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  199 VPVWSGVNVAGVSLQALNPDLGTDKDKEDWKSVHKMVVDSAYEVIKLKGYTSWAIGMSVADLCESILKNMHKCHPVSTLV 278
Cdd:PLN02602 215 VALWSSVSVGGVPVLSFLEKQQIAYEKETLEEIHRAVVDSAYEVIKLKGYTSWAIGYSVASLVRSLLRDQRRIHPVSVLA 294
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18858959  279 KGMHGVNE-EVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETLWGVQKELTL 333
Cdd:PLN02602 295 KGFHGIDEgDVFLSLPAQLGRNGVLGVVNVHLTDEEAERLRKSAKTLWEVQSQLGL 350
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion];
39-324 1.45e-103

Malate/lactate dehydrogenase [Energy production and conversion];


Pssm-ID: 223117  Cd Length: 313  Bit Score: 310.25  E-value: 1.45e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  39 SILLKDLTDELALVDVMEDKLKGEAMDLQHGSLFLKTH-KIVADKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNI 117
Cdd:COG0039  18 LLLLQGLGSELVLIDINEEKAEGVALDLSHAAAPLGSDvKITGDGDYEDLKGADIVVITAGVPRKPGMTRLDLLEKNAKI 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 118 FKFIIPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVVGEHGDS 197
Cdd:COG0039  98 VKDIAKAIAKYAPDAIVLVVTNPVDILTYIAMKFSGFPKNRVIGSGTVLDSARFRTFLAEKLGVSPKDVHAYVIGEHGDT 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 198 SVPVWSGVNVAGVSLqalnPDLGTDKDKEDWKSVHKMVVDSAYEVIKLKGY-TSWAIGMSVADLCESILKNMHKCHPVST 276
Cdd:COG0039 178 MVPLWSQATVGGKPL----EELLKEDTEEDLEELIERVRNAGAEIIEAKGAgTYYGPAAALARMVEAILRDEKRVLPVSV 253
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 18858959 277 LVKGMHGVnEEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETL 324
Cdd:COG0039 254 YLDGEYGV-EDVYFGVPAVLGKNGVEEILELLLSDDEQEKLDKSAEEL 300
Ldh_1_N pfam00056
lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic ...
39-161 2.26e-58

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: 306549  Cd Length: 140  Bit Score: 187.80  E-value: 2.26e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959    39 SILLKDLTDELALVDVMEDKLKGEAMDLQHGSLFLKTHKIVADKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIF 118
Cdd:pfam00056  18 LLANQGLADELVLYDIAKDKLEGVAMDLSHGSTFLPVPGIVGGGDYEDLKDADVVVITAGVPRKPGMTRLDLLNVNAGIF 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 18858959   119 KFIIPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIG 161
Cdd:pfam00056  98 KSIGPAVAKYAPNAIVLVVSNPVDILTYVAWKASGFPPNRVFG 140
 
Name Accession Description Interval E-value
LDH_1 cd05293
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
19-330 0e+00

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  Cd Length: 312  Bit Score: 559.91  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  19 GPTNKVTVVGVGMVGMAAAVSILLKDLTDELALVDVMEDKLKGEAMDLQHGSLFLKTHKIVADKDYSVTANSKVVVVTAG 98
Cdd:cd05293   1 KPRNKVTVVGVGQVGMACAISILAKGLADELVLVDVVEDKLKGEAMDLQHGSAFLKNPKIEADKDYSVTANSKVVIVTAG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  99 ARQQEGESRLNLVQRNVNIFKFIIPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEK 178
Cdd:cd05293  81 ARQNEGESRLDLVQRNVDIFKGIIPKLVKYSPNAILLVVSNPVDIMTYVAWKLSGLPKHRVIGSGCNLDSARFRYLIAER 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 179 LGIHPSSCHGWVVGEHGDSSVPVWSGVNVAGVSLQALNPDLGTDKDKEDWKSVHKMVVDSAYEVIKLKGYTSWAIGMSVA 258
Cdd:cd05293 161 LGVAPSSVHGWIIGEHGDSSVPVWSGVNVAGVRLQDLNPDIGTDKDPEKWKEVHKQVVDSAYEVIKLKGYTSWAIGLSVA 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18858959 259 DLCESILKNMHKCHPVSTLVKGMHGVNEEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETLWGVQKE 330
Cdd:cd05293 241 DLVDAILRNTGRVHSVSTLVKGLHGIEDEVFLSLPCILGENGITHVIKQPLTEEEQEKLQKSADTLWEVQKQ 312
L-LDH-NAD TIGR01771
L-lactate dehydrogenase; This model represents the NAD-dependent L-lactate dehydrogenases from ...
39-325 8.83e-157

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  Cd Length: 299  Bit Score: 445.11  E-value: 8.83e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959    39 SILLKDLTDELALVDVMEDKLKGEAMDLQHGSLFLKTHKIVADKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIF 118
Cdd:TIGR01771  14 ALLNQGIADEIVLIDINKDKAEGEAMDLQHAASFLPTPKKIRSGDYSDCKDADLVVITAGAPQKPGETRLELVGRNVRIM 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   119 KFIIPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVVGEHGDSS 198
Cdd:TIGR01771  94 KSIVPEVVKSGFDGIFLVATNPVDILTYVAWKLSGFPKNRVIGSGTVLDTARLRYLLAEKLGVDPQSVHAYIIGEHGDSE 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   199 VPVWSGVNVAGVSLQALNPDLGTDKDKEDWKsVHKMVVDSAYEVIKLKGYTSWAIGMSVADLCESILKNMHKCHPVSTLV 278
Cdd:TIGR01771 174 VPVWSSATIGGVPLLDYLKAKGTETDLDLEE-IEKEVRDAAYEIINRKGATYYGIGMAVARIVEAILHDENRVLPVSAYL 252
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 18858959   279 KGMHGVNeEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETLW 325
Cdd:TIGR01771 253 DGEYGIK-DVYIGVPAVLGRNGVEEIIELPLSDEEKEAFQKSAETLK 298
PLN02602 PLN02602
lactate dehydrogenase
39-333 8.45e-149

lactate dehydrogenase


Pssm-ID: 178212  Cd Length: 350  Bit Score: 426.88  E-value: 8.45e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   39 SILLKDLTDELALVDVMEDKLKGEAMDLQHGSLFLKTHKIVADKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIF 118
Cdd:PLN02602  55 TILTQDLADELALVDVNPDKLRGEMLDLQHAAAFLPRTKILASTDYAVTAGSDLCIVTAGARQIPGESRLNLLQRNVALF 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  119 KFIIPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVVGEHGDSS 198
Cdd:PLN02602 135 RKIIPELAKYSPDTILLIVSNPVDVLTYVAWKLSGFPANRVIGSGTNLDSSRFRFLIADHLDVNAQDVQAYIVGEHGDSS 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  199 VPVWSGVNVAGVSLQALNPDLGTDKDKEDWKSVHKMVVDSAYEVIKLKGYTSWAIGMSVADLCESILKNMHKCHPVSTLV 278
Cdd:PLN02602 215 VALWSSVSVGGVPVLSFLEKQQIAYEKETLEEIHRAVVDSAYEVIKLKGYTSWAIGYSVASLVRSLLRDQRRIHPVSVLA 294
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18858959  279 KGMHGVNE-EVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETLWGVQKELTL 333
Cdd:PLN02602 295 KGFHGIDEgDVFLSLPAQLGRNGVLGVVNVHLTDEEAERLRKSAKTLWEVQSQLGL 350
LDH_like cd00300
L-lactate dehydrogenase-like enzymes; Members of this subfamily are tetrameric NAD-dependent ...
39-329 6.61e-139

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  Cd Length: 300  Bit Score: 399.72  E-value: 6.61e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  39 SILLKDLTDELALVDVMEDKLKGEAMDLQHGSLFLKTHKIVADKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIF 118
Cdd:cd00300  16 ALIAKGLASELVLVDVNEEKAKGDALDLSHASAFLATGTIVRGGDYADAADADIVVITAGAPRKPGETRLDLINRNAPIL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 119 KFIIPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVVGEHGDSS 198
Cdd:cd00300  96 RSVITNLKKYGPDAIILVVSNPVDILTYVAQKLSGLPKNRVIGSGTLLDSARFRSLLAEKLDVDPQSVHAYVLGEHGDSQ 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 199 VPVWSGVNVAGVSLQALNPDlgtdkDKEDWKSVHKMVVDSAYEVIKLKGYTSWAIGMSVADLCESILKNMHKCHPVSTLV 278
Cdd:cd00300 176 VVAWSTATVGGLPLEELAPF-----TKLDLEAIEEEVRTSGYEIIRLKGATNYGIATAIADIVKSILLDERRVLPVSAVQ 250
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 18858959 279 KGMHGVnEEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETLWGVQK 329
Cdd:cd00300 251 EGQYGI-EDVALSVPAVVGREGVVRILEIPLTEDEEAKLQKSAEALKEVLN 300
LDH_2 cd05292
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
39-331 4.54e-136

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  Cd Length: 308  Bit Score: 393.01  E-value: 4.54e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  39 SILLKDLTDELALVDVMEDKLKGEAMDLQHGSLFLKTHKIVADkDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIF 118
Cdd:cd05292  18 ALLLRGLASEIVLVDINKAKAEGEAMDLAHGTPFVKPVRIYAG-DYADCKGADVVVITAGANQKPGETRLDLLKRNVAIF 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 119 KFIIPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVVGEHGDSS 198
Cdd:cd05292  97 KEIIPQILKYAPDAILLVVTNPVDVLTYVAYKLSGLPPNRVIGSGTVLDTARFRYLLGEHLGVDPRSVHAYIIGEHGDSE 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 199 VPVWSGVNVAGVSLQALNPDLGTDKDKEDWKSVHKMVVDSAYEVIKLKGYTSWAIGMSVADLCESILKNMHKCHPVSTLV 278
Cdd:cd05292 177 VAVWSSANIGGVPLDEFCKLCGRPFDEEVREEIFEEVRNAAYEIIERKGATYYAIGLALARIVEAILRDENSVLTVSSLL 256
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 18858959 279 KGMHGVnEEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETLWGVQKEL 331
Cdd:cd05292 257 DGQYGI-KDVALSLPCIVGRSGVERVLPPPLSEEEEEALRASAEVLKEAIESL 308
ldh PRK00066
L-lactate dehydrogenase; Reviewed
45-331 2.49e-112

L-lactate dehydrogenase; Reviewed


Pssm-ID: 178836  Cd Length: 315  Bit Score: 332.63  E-value: 2.49e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   45 LTDELALVDVMEDKLKGEAMDLQHGSLFLKTHKIVAdKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIFKFIIPN 124
Cdd:PRK00066  30 IADELVIIDINKEKAEGDAMDLSHAVPFTSPTKIYA-GDYSDCKDADLVVITAGAPQKPGETRLDLVEKNLKIFKSIVGE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  125 IIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVVGEHGDSSVPVWSG 204
Cdd:PRK00066 109 VMASGFDGIFLVASNPVDILTYATWKLSGFPKERVIGSGTSLDSARFRYMLSEKLDVDPRSVHAYIIGEHGDTEFPVWSH 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  205 VNVAGVSLQALNPDLGTDKDKEDWKSVHKmVVDSAYEVIKLKGYTSWAIGMSVADLCESILKNMHKCHPVSTLVKGMHGV 284
Cdd:PRK00066 189 ANVAGVPLEEYLEENEQYDEEDLDEIFEN-VRDAAYEIIEKKGATYYGIAMALARITKAILNNENAVLPVSAYLEGQYGE 267
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 18858959  285 NeEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETLWGVQKEL 331
Cdd:PRK00066 268 E-DVYIGVPAVVNRNGIREIVELPLNDDEKQKFAHSADVLKEIMDEA 313
HicDH_like cd05291
L-2-hydroxyisocapronate dehydrogenases and some bacterial L-lactate dehydrogenases; ...
39-324 7.35e-109

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  Cd Length: 306  Bit Score: 323.26  E-value: 7.35e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  39 SILLKDLTDELALVDVMEDKLKGEAMDLQHGSLFLKTHKIVADKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIF 118
Cdd:cd05291  18 SLVNQGIADELVLIDINEEKAEGEALDLEDALAFLPSPVKIKAGDYSDCKDADIVVITAGAPQKPGETRLDLLEKNAKIM 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 119 KFIIPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVVGEHGDSS 198
Cdd:cd05291  98 KSIVPKIKASGFDGIFLVASNPVDVITYVVQKLSGLPKNRVIGTGTSLDTARLRRALAEKLNVDPRSVHAYVLGEHGDSQ 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 199 VPVWSGVNVAGVSL-QALNPDLGTDKDKEDwksVHKMVVDSAYEVIKLKGYTSWAIGMSVADLCESILKNMHKCHPVSTL 277
Cdd:cd05291 178 FVAWSTVTVGGKPLlDLLKEGKLSELDLDE---IEEDVRKAGYEIINGKGATYYGIATALARIVKAILNDENAILPVSAY 254
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 18858959 278 VKGMHGvNEEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETL 324
Cdd:cd05291 255 LDGEYG-EKDVYIGVPAIIGRNGVEEVIELDLTEEEQEKFEKSADII 300
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion];
39-324 1.45e-103

Malate/lactate dehydrogenase [Energy production and conversion];


Pssm-ID: 223117  Cd Length: 313  Bit Score: 310.25  E-value: 1.45e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  39 SILLKDLTDELALVDVMEDKLKGEAMDLQHGSLFLKTH-KIVADKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNI 117
Cdd:COG0039  18 LLLLQGLGSELVLIDINEEKAEGVALDLSHAAAPLGSDvKITGDGDYEDLKGADIVVITAGVPRKPGMTRLDLLEKNAKI 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 118 FKFIIPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVVGEHGDS 197
Cdd:COG0039  98 VKDIAKAIAKYAPDAIVLVVTNPVDILTYIAMKFSGFPKNRVIGSGTVLDSARFRTFLAEKLGVSPKDVHAYVIGEHGDT 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 198 SVPVWSGVNVAGVSLqalnPDLGTDKDKEDWKSVHKMVVDSAYEVIKLKGY-TSWAIGMSVADLCESILKNMHKCHPVST 276
Cdd:COG0039 178 MVPLWSQATVGGKPL----EELLKEDTEEDLEELIERVRNAGAEIIEAKGAgTYYGPAAALARMVEAILRDEKRVLPVSV 253
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 18858959 277 LVKGMHGVnEEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETL 324
Cdd:COG0039 254 YLDGEYGV-EDVYFGVPAVLGKNGVEEILELLLSDDEQEKLDKSAEEL 300
PRK06223 PRK06223
malate dehydrogenase; Reviewed
40-331 2.15e-89

malate dehydrogenase; Reviewed


Pssm-ID: 180477  Cd Length: 307  Bit Score: 273.54  E-value: 2.15e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   40 ILLKDLtDELALVDVMEDKLKGEAMDLQHGSLFLKTH-KIVADKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIF 118
Cdd:PRK06223  21 LALKEL-GDVVLFDIVEGVPQGKALDIAEAAPVEGFDtKITGTNDYEDIAGSDVVVITAGVPRKPGMSRDDLLGINAKIM 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  119 KFIIPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVVGEHGDSS 198
Cdd:PRK06223 100 KDVAEGIKKYAPDAIVIVVTNPVDAMTYVALKESGFPKNRVIGMAGVLDSARFRTFIAEELNVSVKDVTAFVLGGHGDSM 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  199 VPVWSGVNVAGVSLqalnPDLGTDKDKEDwksVHKMVVDSAYEVIKL--KGYTSWAIGMSVADLCESILKNMHKCHPVST 276
Cdd:PRK06223 180 VPLVRYSTVGGIPL----EDLLSKEKLDE---IVERTRKGGAEIVGLlkTGSAYYAPAASIAEMVEAILKDKKRVLPCSA 252
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18858959  277 LVKGMHGVnEEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETLWGVQKEL 331
Cdd:PRK06223 253 YLEGEYGV-KDVYVGVPVKLGKNGVEKIIELELDDEEKAAFDKSVEAVKKLIEAL 306
LDH-like_MDH cd01339
L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an ...
40-324 2.11e-84

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  Cd Length: 300  Bit Score: 260.48  E-value: 2.11e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  40 ILLKDLtDELALVDVMEDKLKGEAMDLQH-GSLFLKTHKIVADKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIF 118
Cdd:cd01339  17 LALKEL-GDVVLLDIVEGLPQGKALDISQaAPILGSDTKVTGTNDYEDIAGSDVVVITAGIPRKPGMSRDDLLGTNAKIV 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 119 KFIIPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVVGEHGDSS 198
Cdd:cd01339  96 KEVAENIKKYAPNAIVIVVTNPLDVMTYVAYKASGFPRNRVIGMAGVLDSARFRYFIAEELGVSVKDVQAMVLGGHGDTM 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 199 VPVWSGVNVAGVSLQALNPdlgtdkdKEDWKSVHKMVVDSAYEVIKLKGYTS--WAIGMSVADLCESILKNMHKCHPVST 276
Cdd:cd01339 176 VPLPRYSTVGGIPLTELIT-------KEEIDEIVERTRNGGAEIVNLLKTGSayYAPAAAIAEMVEAILKDKKRVLPCSA 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 18858959 277 LVKGMHGVNeEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETL 324
Cdd:cd01339 249 YLEGEYGIK-DIFVGVPVVLGKNGVEKIIELDLTDEEKEAFDKSVESV 295
LDH_MDH_like cd00650
NAD-dependent, lactate dehydrogenase-like, 2-hydroxycarboxylate dehydrogenase family; Members ...
44-329 9.25e-78

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  Cd Length: 263  Bit Score: 242.22  E-value: 9.25e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  44 DLTDELALVDVMEDKLKGEAMDLQHGSLFLKTHKIVADKD-YSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIFKFII 122
Cdd:cd00650  24 LLAIELVLYDIDEEKLKGVAMDLQDAVEPLADIKVSITDDpYEAFKDADVVIITAGVGRKPGMGRLDLLKRNVPIVKEIG 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 123 PNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTnLDSARFRYLMGEKLGIHPSSCHGWVVGEHGDSSVPVW 202
Cdd:cd00650 104 DNIEKYSPDAWIIVVSNPVDIITYLVWRYSGLPKEKVIGLGT-LDPIRFRRILAEKLGVDPDDVKVYILGEHGGSQVPDW 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 203 SGVNvagvslqalnpdlgtdkdkedwksvhkmvvdsayeviklkgytswaIGMSVADLCESILKNMHKCHPVSTLVKGMH 282
Cdd:cd00650 183 STVR----------------------------------------------IATSIADLIRSLLNDEGEILPVGVRNNGQI 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 18858959 283 GVNEEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETLWGVQK 329
Cdd:cd00650 217 GIPDDVVVSVPCIVGKNGVEEPIEVGLTDFELEKLQKSADTLKKELE 263
LDH_3 cd05290
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
45-324 2.17e-75

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  Cd Length: 307  Bit Score: 237.61  E-value: 2.17e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  45 LTDELALVDVMEDKLKGEAMDLQHG-SLFLKTHKIVADKDYSVTANSKVVVVTAGA--RQQEGESRLNLVQRNVNIFKFI 121
Cdd:cd05290  23 LFSEIVLIDVNEGVAEGEALDFHHAtALTYSTNTKIRAGDYDDCADADIIVITAGPsiDPGNTDDRLDLAQTNAKIIREI 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 122 IPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVVGEHGDSSVPV 201
Cdd:cd05290 103 MGNITKVTKEAVIILITNPLDIAVYIAATEFDYPANKVIGTGTMLDTARLRRIVADKYGVDPKNVTGYVLGEHGSHAFPV 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 202 WSGVNVAGVSLQALNPDLGTDK-DKEDwksVHKMVVDSAYEVIKLKGYTSWAIGMSVADLCESILKNMHKCHPVSTLVKG 280
Cdd:cd05290 183 WSLVNIAGLPLDELEALFGKEPiDKDE---LLEEVVQAAYDVFNRKGWTNAGIAKSASRLIKAILLDERSILPVCTLLSG 259
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 18858959 281 MHGVnEEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETL 324
Cdd:cd05290 260 EYGL-SDVALSLPTVIGAKGIERVLEIPLDEWELEKLHKSAKAI 302
Ldh_1_N pfam00056
lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic ...
39-161 2.26e-58

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: 306549  Cd Length: 140  Bit Score: 187.80  E-value: 2.26e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959    39 SILLKDLTDELALVDVMEDKLKGEAMDLQHGSLFLKTHKIVADKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIF 118
Cdd:pfam00056  18 LLANQGLADELVLYDIAKDKLEGVAMDLSHGSTFLPVPGIVGGGDYEDLKDADVVVITAGVPRKPGMTRLDLLNVNAGIF 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 18858959   119 KFIIPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIG 161
Cdd:pfam00056  98 KSIGPAVAKYAPNAIVLVVSNPVDILTYVAWKASGFPPNRVFG 140
MalateDH_bact TIGR01763
malate dehydrogenase, NAD-dependent; This enzyme converts malate into oxaloacetate in the ...
43-331 3.35e-54

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  Cd Length: 305  Bit Score: 182.38  E-value: 3.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959    43 KDLTDeLALVDVMEDKLKGEAMDL-QHGSLFLKTHKIVADKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIFKFI 121
Cdd:TIGR01763  23 KELAD-LVLLDVVEGIPQGKALDMyEASPVGGFDTKVTGTNNYADTANSDIVVITAGLPRKPGMSREDLLSMNAGIVREV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   122 IPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVVGEHGDSSVPV 201
Cdd:TIGR01763 102 TGRIMEHSPNPIIVVVSNPLDAMTYVAWQKSGFPKERVIGQAGVLDSARFRTFIAMELGVSVQDVTACVLGGHGDAMVPL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   202 WSGVNVAGVSLQALNPdlgtdkdKEDWKSVHKMVVDSAYEVIKL--KGYTSWAIGMSVADLCESILKNMHKCHPVSTLVK 279
Cdd:TIGR01763 182 VRYSTVAGIPVADLIS-------AERIAEIVERTRKGGGEIVNLlkQGSAYYAPAASVVEMVEAILKDRKRVLPCAAYLD 254
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 18858959   280 GMHGVNeEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETLWGVQKEL 331
Cdd:TIGR01763 255 GQYGID-GIYVGVPVILGKNGVEHIYELKLDQSELALLNKSAKIVDENCKML 305
PTZ00082 PTZ00082
L-lactate dehydrogenase; Provisional
40-320 8.67e-53

L-lactate dehydrogenase; Provisional


Pssm-ID: 173376  Cd Length: 321  Bit Score: 179.11  E-value: 8.67e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   40 ILLKDLTDeLALVDVMEDKLKGEAMDLQHG-SLFLKTHKIVADKDYSVTANSKVVVVTAGARQQEGES-----RLNLVQR 113
Cdd:PTZ00082  25 IVLKNLGD-VVLFDIVKNIPQGKALDISHSnVIAGSNSKVIGTNNYEDIAGSDVVIVTAGLTKRPGKSdkewnRDDLLPL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  114 NVNIFKFIIPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVVGE 193
Cdd:PTZ00082 104 NAKIMDEVAEGIKKYCPNAFVIVITNPLDVMVKLLQEHSGLPKNKVCGMAGVLDSSRLRTYIAEKLGVNPRDVHASVIGA 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  194 HGDSSVPVWSGVNVAGVSLQAL-NPDLGTDKDKEDwksVHKMVVDSAYEVIKLKGYTS--WAIGMSVADLCESILKNMHK 270
Cdd:PTZ00082 184 HGDKMVPLPRYVTVGGIPLSEFiKKGLITQEEIDE---IVERTRNTGKEIVDLLGTGSayFAPAAAAIEMAEAYLKDKKR 260
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 18858959  271 CHPVSTLVKGMHGVNeEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKS 320
Cdd:PTZ00082 261 VLPCSAYLEGQYGHK-DIYMGTPAVIGANGVEKIIELDLTPEEQKKFDES 309
LDH-like_MDH_nadp cd05294
A lactate dehydrogenases-like structure with malate dehydrogenase enzymatic activity; The ...
57-331 4.37e-50

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  Cd Length: 309  Bit Score: 171.82  E-value: 4.37e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  57 DKLKGEAMDLqHGSLFLKTH--KIVADKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIFKFIIPNIIKYSPNCIL 134
Cdd:cd05294  39 EKLKGLRLDI-YDALAAAGIdaEIKISSDLSDVAGSDIVIITAGVPRKEGMSRLDLAKKNAKIVKKYAKQIAEFAPDTKI 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 135 LVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVVGEHGDSSVPVWSGVNVAGVSLQA 214
Cdd:cd05294 118 LVVTNPVDVMTYKALKESGFDKNRVFGLGTHLDSLRFKVAIAKHFNVHISEVHTRIIGEHGDSMVPLISSTSIGGIPIKR 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 215 LnpdlgTDKDKEDWKSVHKMVVDSAYEVIKLKGYTSWAIGMSVADLCESILKNMHKCHPVSTLVKG-MHGVnEEVFLSVP 293
Cdd:cd05294 198 F-----PEYKDFDVEKIVETVKNAGQNIISLKGGSEYGPASAISNLVRTIANDERRILTVSTYLEGeIDGI-RDVCIGVP 271
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 18858959 294 CILGNNGLTDVVHMTLKPEEEKQLVKSAETLWGVQKEL 331
Cdd:cd05294 272 VKLGKNGIEEIVPIEMDDDEREAFRKSAEIVKKYTREV 309
PTZ00117 PTZ00117
malate dehydrogenase; Provisional
40-322 4.07e-48

malate dehydrogenase; Provisional


Pssm-ID: 173409  Cd Length: 319  Bit Score: 166.82  E-value: 4.07e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   40 ILLKDLTDeLALVDVMEDKLKGEAMDLQHGSLFLKTH-KIVADKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIF 118
Cdd:PTZ00117  24 ILQKNLGD-VVLYDVIKGVPQGKALDLKHFSTLVGSNiNILGTNNYEDIKDSDVVVITAGVQRKEEMTREDLLTINGKIM 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  119 KFIIPNIIKYSPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVVGEHGDSS 198
Cdd:PTZ00117 103 KSVAESVKKYCPNAFVICVTNPLDCMVKVFQEKSGIPSNKICGMAGVLDSSRFRCNLAEKLGVSPGDVSAVVIGGHGDLM 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  199 VPVWSGVNVAGVSLQALNPD-LGTDKDKEDwksVHKMVVDSAYEVIKL--KGYTSWAIGMSVADLCESILKNMHKCHPVS 275
Cdd:PTZ00117 183 VPLPRYCTVNGIPLSDFVKKgAITEKEINE---IIKKTRNMGGEIVKLlkKGSAFFAPAAAIVAMIEAYLKDEKRVLVCS 259
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 18858959  276 TLVKGMHGVNeEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAE 322
Cdd:PTZ00117 260 VYLNGQYNCK-NLFVGVPVVIGGKGIEKVIELELNAEEKELFDKSIE 305
Ldh_1_C pfam02866
lactate/malate dehydrogenase, alpha/beta C-terminal domain; L-lactate dehydrogenases are ...
164-324 5.11e-30

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: 280941  Cd Length: 173  Bit Score: 114.37  E-value: 5.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   164 TNLDSARFRYLMGEKLGIHPSSCHGWVVGEHGDSSVPVWSGVNVAGVSLQALNPDLGTDKDKEDWKSVHKmVVDSAYEVI 243
Cdd:pfam02866   1 TTLDINRAKTFLAEKAGVDPRVVNVPVIGGHSGTEFPDWSHAKVTIIPLESQVKENVKDSEWELEELTPR-VQNRGYEII 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   244 KLK-GYTSWAIGMSVADLCESILKNMHKCHPVSTLVKGMHGVNEEVFLSVPCILGNNGLTDVVH-MTLKPEEEKQLVKSA 321
Cdd:pfam02866  80 KAKaGSATLSMAVAGARFVRSILRGTGGVLSMGVYEDGYYGIPDDIYFSFPVTLGKDGVEKILEiLPLNDFEREKMEKSA 159

                  ...
gi 18858959   322 ETL 324
Cdd:pfam02866 160 AEL 162
PTZ00325 PTZ00325
malate dehydrogenase; Provisional
39-321 1.46e-17

malate dehydrogenase; Provisional


Pssm-ID: 240360  Cd Length: 321  Bit Score: 81.63  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   39 SILLKD--LTDELALVDVMedKLKGEAMDLQHGSLFLKTHKIVADKDYSVTA-NSKVVVVTAGARQQEGESRLNLVQRNV 115
Cdd:PTZ00325  25 SLLLKQnpHVSELSLYDIV--GAPGVAADLSHIDTPAKVTGYADGELWEKALrGADLVLICAGVPRKPGMTRDDLFNTNA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  116 NIFKFIIPNIIKYSPNCILLVVSNPVDILTYVAW----KLSGLPRNRVIGSgTNLDSARFRYLMGEKLGIHPSSCHGWVV 191
Cdd:PTZ00325 103 PIVRDLVAAVASSAPKAIVGIVSNPVNSTVPIAAetlkKAGVYDPRKLFGV-TTLDVVRARKFVAEALGMNPYDVNVPVV 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  192 GEHGDSS-VPVWSGvnvAGVSLQalnpdlgtdkdKEDWKSVHKMVVDSAYEVIKLK-GYTSWAIGM--SVADLCESILKN 267
Cdd:PTZ00325 182 GGHSGVTiVPLLSQ---TGLSLP-----------EEQVEQITHRVQVGGDEVVKAKeGAGSATLSMayAAAEWSTSVLKA 247
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  268 MH------KCHPVSTLVKgmhgvNEEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSA 321
Cdd:PTZ00325 248 LRgdkgivECAFVESDMR-----PECPFFSSPVELGKEGVERVLPIGPLNAYEEELLEAA 302
MDH cd00704
Malate dehydrogenase; Malate dehydrogenase (MDH) is one of the key enzymes in the citric acid ...
48-324 6.44e-14

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  Cd Length: 323  Bit Score: 71.15  E-value: 6.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  48 ELALVDVM--EDKLKGEAMDLQHGSLFLKTHKIVADKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIFKFIIPNI 125
Cdd:cd00704  33 ILHLLDIPpaMKALEGVVMELQDCAFPLLKGVVITTDPEEAFKDVDVAILVGAFPRKPGMERADLLRKNAKIFKEQGEAL 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 126 IKY-SPNCILLVVSNPVDILTYVAWKLSGLPRNRVIGSGTNLDSARFRYLMGEKLGIHPSSCHG-WVVGEHGDSSVPvws 203
Cdd:cd00704 113 NKVaKPTVKVLVVGNPANTNALIALKNAPNLPPKNFTALTRLDHNRAKAQVARKLGVRVSDVKNvIIWGNHSNTQVP--- 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 204 GVNVAGVSLQALnPDLGTDKDKEDW--KSVHKMVVDSAYEVIKLKGYTSwaiGMSVAdlcESILKNMHK-CHP------V 274
Cdd:cd00704 190 DLSNAVVYGPGG-TEWVLDLLDEEWlnDEFVKTVQKRGAAIIKKRGASS---AASAA---KAIADHVKDwLFGtppgeiV 262
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 18858959 275 STLV---KGMHGVNEEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETL 324
Cdd:cd00704 263 SMGVyspGNPYGIPPGIVFSFPCTCKGGGWHVVEDLKLNDWLREKLKATEEEL 315
MDH_glyoxysomal_mitochondrial cd01337
Glyoxysomal and mitochondrial malate dehydrogenases; MDH is one of the key enzymes in the ...
39-324 1.12e-13

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  Cd Length: 310  Bit Score: 70.21  E-value: 1.12e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  39 SILLK--DLTDELALVDVMEdkLKGEAMDLQHGSLFLKTHKIVADKD-YSVTANSKVVVVTAGARQQEGESRLNLVQRNV 115
Cdd:cd01337  17 SLLLKlnPLVSELALYDIVN--TPGVAADLSHINTPAKVTGYLGPEElKKALKGADVVVIPAGVPRKPGMTRDDLFNINA 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 116 NIFKFIIPNIIKYSPNCILLVVSNPVDILTYVA---WKLSGL--PRnRVIGSgTNLDSARFRYLMGEKLGIHPSSCHGWV 190
Cdd:cd01337  95 GIVRDLATAVAKACPKALILIISNPVNSTVPIAaevLKKAGVydPK-RLFGV-TTLDVVRANTFVAELLGLDPAKVNVPV 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 191 VGEH-GDSSVPVWSgvnvagvslQALNPDLGTDKDKEdwKSVHKmVVDSAYEVIKLK-GYTSWAIGMSVA--DLCESILK 266
Cdd:cd01337 173 IGGHsGVTILPLLS---------QCQPPFTFDQEEIE--ALTHR-IQFGGDEVVKAKaGAGSATLSMAYAgaRFANSLLR 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18858959 267 NMH--KCHPVSTLVKGmhGVNEEVFLSVPCILGNNGLTDVVHM-TLKPEEEKQLVKSAETL 324
Cdd:cd01337 241 GLKgeKGVIECAYVES--DVTEAPFFATPVELGKNGVEKNLGLgKLNDYEKKLLEAALPEL 299
MDH_euk_gproteo TIGR01772
malate dehydrogenase, NAD-dependent; This model represents the NAD-dependent malate ...
39-324 3.71e-13

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  Cd Length: 312  Bit Score: 68.97  E-value: 3.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959    39 SILLKD--LTDELALVDVMEdkLKGEAMDLQHGSLFLKTHKIVADKDYSVTA-NSKVVVVTAGARQQEGESRLNLVQRNV 115
Cdd:TIGR01772  16 SLLLKLqpYVSELSLYDIAG--AAGVAADLSHIPTAASVKGFSGEEGLENALkGADVVVIPAGVPRKPGMTRDDLFNVNA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   116 NIFKFIIPNIIKYSPNCILLVVSNPVDILTYVAW----KLSGLPRNRVIGSgTNLDSARFRYLMGEKLGIHPSSCHGWVV 191
Cdd:TIGR01772  94 GIVKDLVAAVAESCPKAMILVITNPVNSTVPIAAevlkKKGVYDPNKLFGV-TTLDIVRANTFVAELKGKDPMEVNVPVI 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   192 GEH-GDSSVPVWSGVNvagvslqalNPDLGTDKDKEDWksVHKmVVDSAYEVIKLK---GYTSWAIGMSVADLCESILKN 267
Cdd:TIGR01772 173 GGHsGETIIPLISQCP---------GKVLFTEDQLEAL--IHR-IQNAGTEVVKAKagaGSATLSMAFAGARFVLSLVRG 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   268 MH--KCHPVSTLVKGmHGVNEEVFLSVPCILGNNGLTDVVHM-TLKPEEEKQLVKSAETL 324
Cdd:TIGR01772 241 LKgeEGVVECAYVES-DGVTEATFFATPLLLGKNGVEKRLGIgKLSSFEEKMLNGALPEL 299
MalateDH-SF1 TIGR01759
malate dehydrogenase; This model represents a family of malate dehydrogenases in bacteria and ...
43-305 1.88e-09

malate dehydrogenase; This model represents a family of malate dehydrogenases in bacteria and eukaryotes which utilize either NAD or NADP depending on the species and context. MDH interconverts malate and oxaloacetate and is a part of the citric acid cycle as well as the C4 cycle in certain photosynthetic organisms.


Pssm-ID: 130820  Cd Length: 323  Bit Score: 58.11  E-value: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959    43 KDLTDELALVDV--MEDKLKGEAMDLQHGSLFLKTHKIVADKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIFKF 120
Cdd:TIGR01759  31 KDQPVVLHLLDIppAMKALEGVAMELEDCAFPLLAGVVATTDPEEAFKDVDAALLVGAFPRKPGMERADLLSKNGKIFKE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   121 IIPNIIKY-SPNCILLVVSNPVDILTYVAWKLS-GLPRNRViGSGTNLDSARFRYLMGEKLGIHPSSCHG-WVVGEHGDS 197
Cdd:TIGR01759 111 QGKALNKVaKKDVKVLVVGNPANTNALIASKNApDIPPKNF-SAMTRLDHNRAKYQLAAKAGVPVSDVKNvIIWGNHSNT 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   198 SVPVWSGVNVAGVSLQALNPDlgtdkdkEDW--KSVHKMVVDSAYEVIKLKGYTSWAigmSVADlceSILKNMHKCHP-- 273
Cdd:TIGR01759 190 QVPDFTHATVDGRPVKEVIKD-------DKWleGEFIPTVQQRGAAVIEARGASSAA---SAAN---AAIDHVRDWVTgt 256
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 18858959   274 -----VST--LVKGMH-GVNEEVFLSVPCILGNNGLTDVV 305
Cdd:TIGR01759 257 pegdwVSMgvYSDGNPyGIPEGIIFSFPVTCKGDGEWEIV 296
MDH_euk_cyt TIGR01758
malate dehydrogenase, NAD-dependent; This model represents the NAD-dependent cytosolic malate ...
40-324 3.88e-07

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  Cd Length: 324  Bit Score: 51.00  E-value: 3.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959    40 ILLKDLTDELALVDV--MEDKLKGEAMDLQHGSLFLkTHKIVADKDYSVT-ANSKVVVVTAGARQQEGESRLNLVQRNVN 116
Cdd:TIGR01758  24 MLGKDQPIILHLLDIppAMKVLEGVVMELMDCAFPL-LDGVVPTHDPAVAfTDVDVAILVGAFPRKEGMERRDLLSKNVK 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   117 IFKFIIPNIIKY-SPNCILLVVSNPVDILTYVAWKLS-GLPRNRvIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVV-GE 193
Cdd:TIGR01758 103 IFKEQGRALDKLaKKDCKVLVVGNPANTNALVLSNYApSIPPKN-FSALTRLDHNRALAQVAERAGVPVSDVKNVIIwGN 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   194 HGDSSVPVWSGVNVAGVSLQALNPDLGTDkdkEDW--KSVHKMVVDSAYEVIKLKGYTSwaiGMSVAdlcESILKNMHKC 271
Cdd:TIGR01758 182 HSSTQYPDVNHATVTKGGKQKPVREAIKD---DAYldGEFITTVQQRGAAIIRARKLSS---ALSAA---KAAVDQMHDW 252
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18858959   272 ---HPVSTLVK-------GMHGVNEEVFLSVPCILGNNGLTDVVHMTLKPEEEKQLVKSAETL 324
Cdd:TIGR01758 253 vlgTPEGTFVSmgvysdgSPYGVPKGLIFSFPVTCKNGEWKIVEGLCVDDSSRKKLALTAKEL 315
MDH_cytoplasmic_cytosolic cd01336
Cytoplasmic and cytosolic Malate dehydrogenases; MDH is one of the key enzymes in the citric ...
48-304 7.59e-07

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  Cd Length: 325  Bit Score: 49.93  E-value: 7.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  48 ELALVDV--MEDKLKGEAMDLQHGSLFLkTHKIVADKDYSVTANSKVVVVTAGAR-QQEGESRLNLVQRNVNIFKFIIPN 124
Cdd:cd01336  35 ILHLLDIppALKALEGVVMELQDCAFPL-LKSVVATTDPEEAFKDVDVAILVGAMpRKEGMERKDLLKANVKIFKEQGEA 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 125 IIKY-SPNCILLVVSNPVDILTYVAWKL-SGLPRnRVIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVV-GEHGDSSVPv 201
Cdd:cd01336 114 LDKYaKKNVKVLVVGNPANTNALILLKYaPSIPK-ENFTALTRLDHNRAKSQIALKLGVPVSDVKNVIIwGNHSSTQYP- 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 202 wsGVNVAGVSLQALnpdlgtdkdkedWKSVHKMVVDSAY--------------EVIKLKGYTSwaiGMSVAdlcESILKN 267
Cdd:cd01336 192 --DVNHATVELNGK------------GKPAREAVKDDAWlngefistvqkrgaAVIKARKLSS---AMSAA---KAICDH 251
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 18858959 268 MHKCHP-------VSTLV--KGMHGVNEEVFLSVPCILGNNGLTDV 304
Cdd:cd01336 252 VHDWWFgtpegefVSMGVysDGSYGVPEGLIFSFPVTCKNGKWKIV 297
PRK05086 PRK05086
malate dehydrogenase; Provisional
48-324 4.65e-06

malate dehydrogenase; Provisional


Pssm-ID: 235340  Cd Length: 312  Bit Score: 47.30  E-value: 4.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   48 ELALVDVMEdKLKGEAMDLQHGSLFLKTHKIVADKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIFKFIIPNIIK 127
Cdd:PRK05086  29 ELSLYDIAP-VTPGVAVDLSHIPTAVKIKGFSGEDPTPALEGADVVLISAGVARKPGMDRSDLFNVNAGIVKNLVEKVAK 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  128 YSPNCILLVVSNPVDILTYVA---WKLSGL-PRNRVIGSgTNLDSARFRYLMGEKLGIHPSSCHGWVVGEH-GDSSVPVW 202
Cdd:PRK05086 108 TCPKACIGIITNPVNTTVAIAaevLKKAGVyDKNKLFGV-TTLDVIRSETFVAELKGKQPGEVEVPVIGGHsGVTILPLL 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  203 SgvNVAGVSLqalnpdlgTDkdkEDWKSVHKMVVDSAYEVIKLK---GYTSWAIGMSVADLCESilknmhkchpvstLVK 279
Cdd:PRK05086 187 S--QVPGVSF--------TE---QEVADLTKRIQNAGTEVVEAKaggGSATLSMGQAAARFGLS-------------LVR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18858959  280 GMHGVNEEV-------------FLSVPCILGNNGLTDVVHM-TLKPEEEKQLVKSAETL 324
Cdd:PRK05086 241 ALQGEQGVVecayvegdgkyarFFAQPVLLGKNGVEERLPIgTLSAFEQNALEGMLDTL 299
LDH_protist TIGR01756
lactate dehydrogenase; This model represents a family of protist lactate dehydrogenases which ...
57-324 8.11e-06

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: 46.80  E-value: 8.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959    57 DKLKGEAMDLQHGSLFLKTHKIVADKDYSVTANSKVVVVTAGARQQEGESRLNLVQRNVNIFKFIIPNIIKYS-PNCILL 135
Cdd:TIGR01756  28 NRLEALAMELEDCAFPNLAGTIVTTKLEEAFKDIDCAFLVASVPLKPGEVRADLLTKNTPIFKATGEALSEYAkPTVKVL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   136 VVSNPVDILTYVAW----KLSglPRNrvIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVV-GEHGDSSVPVWSGVNVA-G 209
Cdd:TIGR01756 108 VIGNPVNTNCLVAMlhapKLS--AEN--FSSLCMLDHNRAVSRIASKLKVPVDHIYHVVVwGNHAESMVADLTHAEFTkN 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   210 VSLQALNPDLGTDKDKEDWksvHKMVVDSAYEVIKLKGYTSwAIGMSVADLCEsILKNMHKCHPVSTLVKGM-------H 282
Cdd:TIGR01756 184 GKHQKVFDELCRDYPEPDF---FEVIAQRAWKILEMRGFTS-AASPVKASLQH-MKAWLFGTRPGEVLSMGIpvpegnpY 258
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 18858959   283 GVNEEVFLSVPCILGNNGLTDVVH-MTLKPEEEKQLVKSAETL 324
Cdd:TIGR01756 259 GIKPGVIFSFPCTVDEDGKVHVVEnFELNPWLKTKLAQTEKDL 301
PLN00106 PLN00106
malate dehydrogenase
92-194 1.27e-05

malate dehydrogenase


Pssm-ID: 215058  Cd Length: 323  Bit Score: 46.10  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   92 VVVVTAGARQQEGESRLNLVQRNVNIFKFIIPNIIKYSPNCILLVVSNPVDILTYVA---WKLSGL--PRnRVIGSgTNL 166
Cdd:PLN00106  89 LVIIPAGVPRKPGMTRDDLFNINAGIVKTLCEAVAKHCPNALVNIISNPVNSTVPIAaevLKKAGVydPK-KLFGV-TTL 166
                         90       100
                 ....*....|....*....|....*...
gi 18858959  167 DSARFRYLMGEKLGIHPSSCHGWVVGEH 194
Cdd:PLN00106 167 DVVRANTFVAEKKGLDPADVDVPVVGGH 194
MDH_choloroplast_like cd01338
Chloroplast-like malate dehydrogenases; MDH is one of the key enzymes in the citric acid cycle, ...
48-304 2.19e-04

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 choloroplasts. 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  Cd Length: 322  Bit Score: 42.19  E-value: 2.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  48 ELALVDV--MEDKLKGEAMDLQHgSLFLKTHKIVADKDYSVTANSKVVVVTAGAR-QQEGESRLNLVQRNVNIFKFIIPN 124
Cdd:cd01338  35 ILQLLELpqALKALEGVAMELED-CAFPLLAEIVITDDPNVAFKDADWALLVGAKpRGPGMERADLLKANGKIFTAQGKA 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 125 IIKY-SPNCILLVVSNPVDILTYVAWKLS-GLPRNRvIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVV-GEHGDSSVPV 201
Cdd:cd01338 114 LNDVaSRDVKVLVVGNPCNTNALIAMKNApDIPPDN-FTAMTRLDHNRAKSQLAKKAGVPVTDVKNMVIwGNHSPTQYPD 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959 202 WSGVNVAGVSLqalnPDLGTDkdkEDW--KSVHKMVVDSAYEVIKLKGYTSWAigmSVADlceSILKNMH---------K 270
Cdd:cd01338 193 FTNATIGGKPA----AEVIND---RAWleDEFIPTVQKRGAAIIKARGASSAA---SAAN---AAIDHMRdwvlgtpegD 259
                       250       260       270
                ....*....|....*....|....*....|....
gi 18858959 271 CHPVSTLVKGMHGVNEEVFLSVPCILGNNGLTDV 304
Cdd:cd01338 260 WFSMAVPSDGSYGIPEGLIFSFPVRSKGGGYEIV 293
PLN00135 PLN00135
malate dehydrogenase
49-211 6.69e-04

malate dehydrogenase


Pssm-ID: 177744  Cd Length: 309  Bit Score: 40.53  E-value: 6.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959   49 LALVDV--MEDKLKGEAMDLQHGSLFLkTHKIVADKDY-SVTANSKVVVVTAGARQQEGESRLNLVQRNVNIFKFIIPNI 125
Cdd:PLN00135  16 LHMLDIppAAEALNGVKMELIDAAFPL-LKGVVATTDVvEACKGVNIAVMVGGFPRKEGMERKDVMSKNVSIYKSQASAL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858959  126 IKY-SPNCILLVVSNPVD----ILTYVAwklSGLPRNRvIGSGTNLDSARFRYLMGEKLGIHPSSCHGWVV-GEHGDSSV 199
Cdd:PLN00135  95 EKHaAPDCKVLVVANPANtnalILKEFA---PSIPEKN-ITCLTRLDHNRALGQISERLGVPVSDVKNVIIwGNHSSTQY 170
                        170
                 ....*....|..
gi 18858959  200 PvwsGVNVAGVS 211
Cdd:PLN00135 171 P---DVNHATVK 179
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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