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Conserved domains on  [gi|442630559|ref|NP_001261474|]
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lactate dehydrogenase, isoform B [Drosophila melanogaster]

Protein Classification

L-lactate dehydrogenase( domain architecture ID 10143083)

L-lactate dehydrogenase catalyzes the last step of glycolysis in which pyruvate is converted to L-lactate

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 ...
18-329 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 [Multi-domain]  Cd Length: 312  Bit Score: 546.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  18 SSGHKVTIVGIGQVGMASAFSILAQNVSKEVCLIDVCADKLQGELMDLQHGSNFLKNPQITASTDFAASANSRLCIVTAG 97
Cdd:cd05293    1 KPRNKVTVVGVGQVGMACAISILAKGLADELVLVDVVEDKLKGEAMDLQHGSAFLKNPKIEADKDYSVTANSKVVIVTAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  98 VRQKEGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMSQR 177
Cdd:cd05293   81 ARQNEGESRLDLVQRNVDIFKGIIPKLVKYSPNAILLVVSNPVDIMTYVAWKLSGLPKHRVIGSGCNLDSARFRYLIAER 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 178 LGVAPTSCHGWIIGEHGDSSVPVWSGVNIAGVRLRELNPILGTGEDPEKWNELHKQVVDSAYEVIKLKGYTSWAIGLSTA 257
Cdd:cd05293  161 LGVAPSSVHGWIIGEHGDSSVPVWSGVNVAGVRLQDLNPDIGTDKDPEKWKEVHKQVVDSAYEVIKLKGYTSWAIGLSVA 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442630559 258 SLASAILRNTSSVAAVSTSVLGEHGIDKDVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSANIMSDVQAG 329
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 ...
18-329 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 [Multi-domain]  Cd Length: 312  Bit Score: 546.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  18 SSGHKVTIVGIGQVGMASAFSILAQNVSKEVCLIDVCADKLQGELMDLQHGSNFLKNPQITASTDFAASANSRLCIVTAG 97
Cdd:cd05293    1 KPRNKVTVVGVGQVGMACAISILAKGLADELVLVDVVEDKLKGEAMDLQHGSAFLKNPKIEADKDYSVTANSKVVIVTAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  98 VRQKEGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMSQR 177
Cdd:cd05293   81 ARQNEGESRLDLVQRNVDIFKGIIPKLVKYSPNAILLVVSNPVDIMTYVAWKLSGLPKHRVIGSGCNLDSARFRYLIAER 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 178 LGVAPTSCHGWIIGEHGDSSVPVWSGVNIAGVRLRELNPILGTGEDPEKWNELHKQVVDSAYEVIKLKGYTSWAIGLSTA 257
Cdd:cd05293  161 LGVAPSSVHGWIIGEHGDSSVPVWSGVNVAGVRLQDLNPDIGTDKDPEKWKEVHKQVVDSAYEVIKLKGYTSWAIGLSVA 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442630559 258 SLASAILRNTSSVAAVSTSVLGEHGIDKDVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSANIMSDVQAG 329
Cdd:cd05293  241 DLVDAILRNTGRVHSVSTLVKGLHGIEDEVFLSLPCILGENGITHVIKQPLTEEEQEKLQKSADTLWEVQKQ 312
PLN02602 PLN02602
lactate dehydrogenase
21-331 1.56e-145

lactate dehydrogenase


Pssm-ID: 178212 [Multi-domain]  Cd Length: 350  Bit Score: 414.17  E-value: 1.56e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  21 HKVTIVGIGQVGMASAFSILAQNVSKEVCLIDVCADKLQGELMDLQHGSNFLKNPQITASTDFAASANSRLCIVTAGVRQ 100
Cdd:PLN02602  38 TKVSVVGVGNVGMAIAQTILTQDLADELALVDVNPDKLRGEMLDLQHAAAFLPRTKILASTDYAVTAGSDLCIVTAGARQ 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 101 KEGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMSQRLGV 180
Cdd:PLN02602 118 IPGESRLNLLQRNVALFRKIIPELAKYSPDTILLIVSNPVDVLTYVAWKLSGFPANRVIGSGTNLDSSRFRFLIADHLDV 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 181 APTSCHGWIIGEHGDSSVPVWSGVNIAGVrlrelnPILGTGE------DPEKWNELHKQVVDSAYEVIKLKGYTSWAIGL 254
Cdd:PLN02602 198 NAQDVQAYIVGEHGDSSVALWSSVSVGGV------PVLSFLEkqqiayEKETLEEIHRAVVDSAYEVIKLKGYTSWAIGY 271
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442630559 255 STASLASAILRNTSSVAAVSTSVLGEHGIDK-DVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSANIMSDVQAGLK 331
Cdd:PLN02602 272 SVASLVRSLLRDQRRIHPVSVLAKGFHGIDEgDVFLSLPAQLGRNGVLGVVNVHLTDEEAERLRKSAKTLWEVQSQLG 349
L-LDH-NAD TIGR01771
L-lactate dehydrogenase; This model represents the NAD-dependent L-lactate dehydrogenases from ...
25-323 1.47e-140

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: 399.65  E-value: 1.47e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559   25 IVGIGQVGMASAFSILAQNVSKEVCLIDVCADKLQGELMDLQHGSNFLKNPQITASTDFAASANSRLCIVTAGVRQKEGE 104
Cdd:TIGR01771   1 IIGAGNVGSSTAFALLNQGIADEIVLIDINKDKAEGEAMDLQHAASFLPTPKKIRSGDYSDCKDADLVVITAGAPQKPGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  105 SRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMSQRLGVAPTS 184
Cdd:TIGR01771  81 TRLELVGRNVRIMKSIVPEVVKSGFDGIFLVATNPVDILTYVAWKLSGFPKNRVIGSGTVLDTARLRYLLAEKLGVDPQS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  185 CHGWIIGEHGDSSVPVWSGVNIAGVRLRELNPILGTGEDPEKWnELHKQVVDSAYEVIKLKGYTSWAIGLSTASLASAIL 264
Cdd:TIGR01771 161 VHAYIIGEHGDSEVPVWSSATIGGVPLLDYLKAKGTETDLDLE-EIEKEVRDAAYEIINRKGATYYGIGMAVARIVEAIL 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 442630559  265 RNTSSVAAVSTSVLGEHGIdKDVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSANIM 323
Cdd:TIGR01771 240 HDENRVLPVSAYLDGEYGI-KDVYIGVPAVLGRNGVEEIIELPLSDEEKEAFQKSAETL 297
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ...
22-328 3.10e-128

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: 368.58  E-value: 3.10e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  22 KVTIVGIGQVGMASAFSILAQNVSKEVCLIDVCADKLQGELMDLQHGSNFLKNPQITASTDFAASANSRLCIVTAGVRQK 101
Cdd:COG0039    2 KVAIIGAGNVGSTLAFRLASGGLADELVLIDINEGKAEGEALDLADAFPLLGFDVKITAGDYEDLADADVVVITAGAPRK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 102 EGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMSQRLGVA 181
Cdd:COG0039   82 PGMSRLDLLEANAKIFKSVGEAIKKYAPDAIVLVVTNPVDVMTYIAQKASGLPKERVIGMGTVLDSARFRSFLAEKLGVS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 182 PTSCHGWIIGEHGDSSVPVWSGVNIAGVRLRELnpilgTGEDPEKWNELHKQVVDSAYEVIKLKGYTSWAIGLSTASLAS 261
Cdd:COG0039  162 PRDVHAYVLGEHGDSMVPLWSHATVGGIPLTEL-----IKETDEDLDEIIERVRKGGAEIIEGKGSTYYAIAAAAARIVE 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442630559 262 AILRNTSSVAAVSTSVLGEHGIdKDVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSANIMSDVQA 328
Cdd:COG0039  237 AILRDEKRVLPVSVYLDGEYGI-EDVYLGVPVVIGRNGVEKIVELELTDEERAKLDASAEELKEEID 302
Ldh_1_N pfam00056
lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic ...
22-160 5.21e-51

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: 165.86  E-value: 5.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559   22 KVTIVG-IGQVGMASAFSILAQNVSKEVCLIDVCADKLQGELMDLQHGSNFLKNPQITASTDFAASANSRLCIVTAGVRQ 100
Cdd:pfam00056   2 KVAVVGaAGGVGQSLAFLLANKGLADELVLYDIVKEKLEGVAMDLSHGSTFLLVPGIVGGGDYEDLKDADVVVITAGVPR 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  101 KEGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIG 160
Cdd:pfam00056  82 KPGMTRLDLLNVNAKIFKSIGPALAKYAPNAIVLVVSNPVDILTYVAWKASGFPPNRVFG 141
 
Name Accession Description Interval E-value
LDH_1 cd05293
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
18-329 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 [Multi-domain]  Cd Length: 312  Bit Score: 546.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  18 SSGHKVTIVGIGQVGMASAFSILAQNVSKEVCLIDVCADKLQGELMDLQHGSNFLKNPQITASTDFAASANSRLCIVTAG 97
Cdd:cd05293    1 KPRNKVTVVGVGQVGMACAISILAKGLADELVLVDVVEDKLKGEAMDLQHGSAFLKNPKIEADKDYSVTANSKVVIVTAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  98 VRQKEGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMSQR 177
Cdd:cd05293   81 ARQNEGESRLDLVQRNVDIFKGIIPKLVKYSPNAILLVVSNPVDIMTYVAWKLSGLPKHRVIGSGCNLDSARFRYLIAER 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 178 LGVAPTSCHGWIIGEHGDSSVPVWSGVNIAGVRLRELNPILGTGEDPEKWNELHKQVVDSAYEVIKLKGYTSWAIGLSTA 257
Cdd:cd05293  161 LGVAPSSVHGWIIGEHGDSSVPVWSGVNVAGVRLQDLNPDIGTDKDPEKWKEVHKQVVDSAYEVIKLKGYTSWAIGLSVA 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442630559 258 SLASAILRNTSSVAAVSTSVLGEHGIDKDVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSANIMSDVQAG 329
Cdd:cd05293  241 DLVDAILRNTGRVHSVSTLVKGLHGIEDEVFLSLPCILGENGITHVIKQPLTEEEQEKLQKSADTLWEVQKQ 312
PLN02602 PLN02602
lactate dehydrogenase
21-331 1.56e-145

lactate dehydrogenase


Pssm-ID: 178212 [Multi-domain]  Cd Length: 350  Bit Score: 414.17  E-value: 1.56e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  21 HKVTIVGIGQVGMASAFSILAQNVSKEVCLIDVCADKLQGELMDLQHGSNFLKNPQITASTDFAASANSRLCIVTAGVRQ 100
Cdd:PLN02602  38 TKVSVVGVGNVGMAIAQTILTQDLADELALVDVNPDKLRGEMLDLQHAAAFLPRTKILASTDYAVTAGSDLCIVTAGARQ 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 101 KEGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMSQRLGV 180
Cdd:PLN02602 118 IPGESRLNLLQRNVALFRKIIPELAKYSPDTILLIVSNPVDVLTYVAWKLSGFPANRVIGSGTNLDSSRFRFLIADHLDV 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 181 APTSCHGWIIGEHGDSSVPVWSGVNIAGVrlrelnPILGTGE------DPEKWNELHKQVVDSAYEVIKLKGYTSWAIGL 254
Cdd:PLN02602 198 NAQDVQAYIVGEHGDSSVALWSSVSVGGV------PVLSFLEkqqiayEKETLEEIHRAVVDSAYEVIKLKGYTSWAIGY 271
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442630559 255 STASLASAILRNTSSVAAVSTSVLGEHGIDK-DVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSANIMSDVQAGLK 331
Cdd:PLN02602 272 SVASLVRSLLRDQRRIHPVSVLAKGFHGIDEgDVFLSLPAQLGRNGVLGVVNVHLTDEEAERLRKSAKTLWEVQSQLG 349
L-LDH-NAD TIGR01771
L-lactate dehydrogenase; This model represents the NAD-dependent L-lactate dehydrogenases from ...
25-323 1.47e-140

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: 399.65  E-value: 1.47e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559   25 IVGIGQVGMASAFSILAQNVSKEVCLIDVCADKLQGELMDLQHGSNFLKNPQITASTDFAASANSRLCIVTAGVRQKEGE 104
Cdd:TIGR01771   1 IIGAGNVGSSTAFALLNQGIADEIVLIDINKDKAEGEAMDLQHAASFLPTPKKIRSGDYSDCKDADLVVITAGAPQKPGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  105 SRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMSQRLGVAPTS 184
Cdd:TIGR01771  81 TRLELVGRNVRIMKSIVPEVVKSGFDGIFLVATNPVDILTYVAWKLSGFPKNRVIGSGTVLDTARLRYLLAEKLGVDPQS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  185 CHGWIIGEHGDSSVPVWSGVNIAGVRLRELNPILGTGEDPEKWnELHKQVVDSAYEVIKLKGYTSWAIGLSTASLASAIL 264
Cdd:TIGR01771 161 VHAYIIGEHGDSEVPVWSSATIGGVPLLDYLKAKGTETDLDLE-EIEKEVRDAAYEIINRKGATYYGIGMAVARIVEAIL 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 442630559  265 RNTSSVAAVSTSVLGEHGIdKDVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSANIM 323
Cdd:TIGR01771 240 HDENRVLPVSAYLDGEYGI-KDVYIGVPAVLGRNGVEEIIELPLSDEEKEAFQKSAETL 297
LDH_2 cd05292
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
22-330 2.25e-139

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: 396.86  E-value: 2.25e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  22 KVTIVGIGQVGMASAFSILAQNVSKEVCLIDVCADKLQGELMDLQHGSNFLKnPQITASTDFAASANSRLCIVTAGVRQK 101
Cdd:cd05292    2 KVAIVGAGFVGSTTAYALLLRGLASEIVLVDINKAKAEGEAMDLAHGTPFVK-PVRIYAGDYADCKGADVVVITAGANQK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 102 EGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMSQRLGVA 181
Cdd:cd05292   81 PGETRLDLLKRNVAIFKEIIPQILKYAPDAILLVVTNPVDVLTYVAYKLSGLPPNRVIGSGTVLDTARFRYLLGEHLGVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 182 PTSCHGWIIGEHGDSSVPVWSGVNIAGVRLRELNPILGTGEDPEKWNELHKQVVDSAYEVIKLKGYTSWAIGLSTASLAS 261
Cdd:cd05292  161 PRSVHAYIIGEHGDSEVAVWSSANIGGVPLDEFCKLCGRPFDEEVREEIFEEVRNAAYEIIERKGATYYAIGLALARIVE 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442630559 262 AILRNTSSVAAVSTSVLGEHGIdKDVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSANIMSDVQAGL 330
Cdd:cd05292  241 AILRDENSVLTVSSLLDGQYGI-KDVALSLPCIVGRSGVERVLPPPLSEEEEEALRASAEVLKEAIESL 308
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ...
22-328 3.10e-128

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: 368.58  E-value: 3.10e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  22 KVTIVGIGQVGMASAFSILAQNVSKEVCLIDVCADKLQGELMDLQHGSNFLKNPQITASTDFAASANSRLCIVTAGVRQK 101
Cdd:COG0039    2 KVAIIGAGNVGSTLAFRLASGGLADELVLIDINEGKAEGEALDLADAFPLLGFDVKITAGDYEDLADADVVVITAGAPRK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 102 EGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMSQRLGVA 181
Cdd:COG0039   82 PGMSRLDLLEANAKIFKSVGEAIKKYAPDAIVLVVTNPVDVMTYIAQKASGLPKERVIGMGTVLDSARFRSFLAEKLGVS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 182 PTSCHGWIIGEHGDSSVPVWSGVNIAGVRLRELnpilgTGEDPEKWNELHKQVVDSAYEVIKLKGYTSWAIGLSTASLAS 261
Cdd:COG0039  162 PRDVHAYVLGEHGDSMVPLWSHATVGGIPLTEL-----IKETDEDLDEIIERVRKGGAEIIEGKGSTYYAIAAAAARIVE 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442630559 262 AILRNTSSVAAVSTSVLGEHGIdKDVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSANIMSDVQA 328
Cdd:COG0039  237 AILRDEKRVLPVSVYLDGEYGI-EDVYLGVPVVIGRNGVEKIVELELTDEERAKLDASAEELKEEID 302
LDH_like cd00300
L-lactate dehydrogenase-like enzymes; Members of this subfamily are tetrameric NAD-dependent ...
23-327 1.82e-125

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: 361.20  E-value: 1.82e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  23 VTIVGIGQVGMASAFSILAQNVSKEVCLIDVCADKLQGELMDLQHGSNFLKNPQITASTDFAASANSRLCIVTAGVRQKE 102
Cdd:cd00300    1 ITIIGAGNVGAAVAFALIAKGLASELVLVDVNEEKAKGDALDLSHASAFLATGTIVRGGDYADAADADIVVITAGAPRKP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 103 GESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMSQRLGVAP 182
Cdd:cd00300   81 GETRLDLINRNAPILRSVITNLKKYGPDAIILVVSNPVDILTYVAQKLSGLPKNRVIGSGTLLDSARFRSLLAEKLDVDP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 183 TSCHGWIIGEHGDSSVPVWSGVNIAGVRLRELNPilgtgEDPEKWNELHKQVVDSAYEVIKLKGYTSWAIGLSTASLASA 262
Cdd:cd00300  161 QSVHAYVLGEHGDSQVVAWSTATVGGLPLEELAP-----FTKLDLEAIEEEVRTSGYEIIRLKGATNYGIATAIADIVKS 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442630559 263 ILRNTSSVAAVSTSVLGEHGIDkDVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSANIMSDVQ 327
Cdd:cd00300  236 ILLDERRVLPVSAVQEGQYGIE-DVALSVPAVVGREGVVRILEIPLTEDEEAKLQKSAEALKEVL 299
ldh PRK00066
L-lactate dehydrogenase; Reviewed
19-330 2.92e-116

L-lactate dehydrogenase; Reviewed


Pssm-ID: 178836 [Multi-domain]  Cd Length: 315  Bit Score: 338.41  E-value: 2.92e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  19 SGHKVTIVGIGQVGMASAFSILAQNVSKEVCLIDVCADKLQGELMDLQHGSNFLKNPQITAStDFAASANSRLCIVTAGV 98
Cdd:PRK00066   5 QHNKVVLVGDGAVGSSYAYALVNQGIADELVIIDINKEKAEGDAMDLSHAVPFTSPTKIYAG-DYSDCKDADLVVITAGA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  99 RQKEGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMSQRL 178
Cdd:PRK00066  84 PQKPGETRLDLVEKNLKIFKSIVGEVMASGFDGIFLVASNPVDILTYATWKLSGFPKERVIGSGTSLDSARFRYMLSEKL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 179 GVAPTSCHGWIIGEHGDSSVPVWSGVNIAGVRLRELNPILGTGEDPEKwNELHKQVVDSAYEVIKLKGYTSWAIGLSTAS 258
Cdd:PRK00066 164 DVDPRSVHAYIIGEHGDTEFPVWSHANVAGVPLEEYLEENEQYDEEDL-DEIFENVRDAAYEIIEKKGATYYGIAMALAR 242
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442630559 259 LASAILRNTSSVAAVSTSVLGEHGIDkDVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSANIMSDVQAGL 330
Cdd:PRK00066 243 ITKAILNNENAVLPVSAYLEGQYGEE-DVYIGVPAVVNRNGIREIVELPLNDDEKQKFAHSADVLKEIMDEA 313
HicDH_like cd05291
L-2-hydroxyisocapronate dehydrogenases and some bacterial L-lactate dehydrogenases; ...
21-328 6.88e-116

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: 337.13  E-value: 6.88e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  21 HKVTIVGIGQVGMASAFSILAQNVSKEVCLIDVCADKLQGELMDLQHGSNFLKNPQITASTDFAASANSRLCIVTAGVRQ 100
Cdd:cd05291    1 RKVVIIGAGHVGSSFAYSLVNQGIADELVLIDINEEKAEGEALDLEDALAFLPSPVKIKAGDYSDCKDADIVVITAGAPQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 101 KEGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMSQRLGV 180
Cdd:cd05291   81 KPGETRLDLLEKNAKIMKSIVPKIKASGFDGIFLVASNPVDVITYVVQKLSGLPKNRVIGTGTSLDTARLRRALAEKLNV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 181 APTSCHGWIIGEHGDSSVPVWSGVNIAGVRLRELnpILGTGEDPEKWNELHKQVVDSAYEVIKLKGYTSWAIGLSTASLA 260
Cdd:cd05291  161 DPRSVHAYVLGEHGDSQFVAWSTVTVGGKPLLDL--LKEGKLSELDLDEIEEDVRKAGYEIINGKGATYYGIATALARIV 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442630559 261 SAILRNTSSVAAVSTSVLGEHGIdKDVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSANIMSDVQA 328
Cdd:cd05291  239 KAILNDENAILPVSAYLDGEYGE-KDVYIGVPAIIGRNGVEEVIELDLTEEEQEKFEKSADIIKENIK 305
PRK06223 PRK06223
malate dehydrogenase; Reviewed
22-331 2.61e-94

malate dehydrogenase; Reviewed


Pssm-ID: 180477 [Multi-domain]  Cd Length: 307  Bit Score: 282.40  E-value: 2.61e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  22 KVTIVGIGQVGMASAFsILAQNVSKEVCLIDVCADKLQGELMDLQHGSNFLK-NPQITASTDFAASANSRLCIVTAGVRQ 100
Cdd:PRK06223   4 KISIIGAGNVGATLAH-LLALKELGDVVLFDIVEGVPQGKALDIAEAAPVEGfDTKITGTNDYEDIAGSDVVVITAGVPR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 101 KEGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMSQRLGV 180
Cdd:PRK06223  83 KPGMSRDDLLGINAKIMKDVAEGIKKYAPDAIVIVVTNPVDAMTYVALKESGFPKNRVIGMAGVLDSARFRTFIAEELNV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 181 APTSCHGWIIGEHGDSSVPVWSGVNIAGVRLRELNPilgtgedPEKWNELHKQVVDSAYEVIKL--KGYTSWAIGLSTAS 258
Cdd:PRK06223 163 SVKDVTAFVLGGHGDSMVPLVRYSTVGGIPLEDLLS-------KEKLDEIVERTRKGGAEIVGLlkTGSAYYAPAASIAE 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442630559 259 LASAILRNTSSVAAVSTSVLGEHGIdKDVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSANIMSDVQAGLK 331
Cdd:PRK06223 236 MVEAILKDKKRVLPCSAYLEGEYGV-KDVYVGVPVKLGKNGVEKIIELELDDEEKAAFDKSVEAVKKLIEALK 307
LDH-like_MDH cd01339
L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an ...
23-325 2.08e-87

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: 264.72  E-value: 2.08e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  23 VTIVGIGQVGMASAFSILAQNVSkEVCLIDVCADKLQGELMDLQHGSN-FLKNPQITASTDFAASANSRLCIVTAGVRQK 101
Cdd:cd01339    1 ISIIGAGNVGATLAQLLALKELG-DVVLLDIVEGLPQGKALDISQAAPiLGSDTKVTGTNDYEDIAGSDVVVITAGIPRK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 102 EGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMSQRLGVA 181
Cdd:cd01339   80 PGMSRDDLLGTNAKIVKEVAENIKKYAPNAIVIVVTNPLDVMTYVAYKASGFPRNRVIGMAGVLDSARFRYFIAEELGVS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 182 PTSCHGWIIGEHGDSSVPVWSGVNIAGVRLRELnpilgtgEDPEKWNELHKQVVDSAYEVIKLKGYTS--WAIGLSTASL 259
Cdd:cd01339  160 VKDVQAMVLGGHGDTMVPLPRYSTVGGIPLTEL-------ITKEEIDEIVERTRNGGAEIVNLLKTGSayYAPAAAIAEM 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442630559 260 ASAILRNTSSVAAVSTSVLGEHGIdKDVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSANIMSD 325
Cdd:cd01339  233 VEAILKDKKRVLPCSAYLEGEYGI-KDIFVGVPVVLGKNGVEKIIELDLTDEEKEAFDKSVESVKE 297
LDH_3 cd05290
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
22-320 3.14e-81

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: 249.17  E-value: 3.14e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  22 KVTIVGIGQVGMASAFSILAQNVSKEVCLIDVCADKLQGELMDLQH--GSNFLKNPQITAStDFAASANSRLCIVTAG-- 97
Cdd:cd05290    1 KLVVIGAGHVGSAVLNYALALGLFSEIVLIDVNEGVAEGEALDFHHatALTYSTNTKIRAG-DYDDCADADIIVITAGps 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  98 VRQKEGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMSQR 177
Cdd:cd05290   80 IDPGNTDDRLDLAQTNAKIIREIMGNITKVTKEAVIILITNPLDIAVYIAATEFDYPANKVIGTGTMLDTARLRRIVADK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 178 LGVAPTSCHGWIIGEHGDSSVPVWSGVNIAGVRLRELNPILGTgeDPEKWNELHKQVVDSAYEVIKLKGYTSWAIGLSTA 257
Cdd:cd05290  160 YGVDPKNVTGYVLGEHGSHAFPVWSLVNIAGLPLDELEALFGK--EPIDKDELLEEVVQAAYDVFNRKGWTNAGIAKSAS 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442630559 258 SLASAILRNTSSVAAVSTSVLGEHGIdKDVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSA 320
Cdd:cd05290  238 RLIKAILLDERSILPVCTLLSGEYGL-SDVALSLPTVIGAKGIERVLEIPLDEWELEKLHKSA 299
LDH_MDH_like cd00650
NAD-dependent, lactate dehydrogenase-like, 2-hydroxycarboxylate dehydrogenase family; Members ...
23-323 3.17e-68

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: 214.11  E-value: 3.17e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  23 VTIVG-IGQVGMASAFSILAQNVS--KEVCLIDVCADKLQGELMDLQHGSNFLKNPQITASTDF-AASANSRLCIVTAGV 98
Cdd:cd00650    1 IAVIGaGGNVGPALAFGLADGSVLlaIELVLYDIDEEKLKGVAMDLQDAVEPLADIKVSITDDPyEAFKDADVVIITAGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  99 RQKEGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTnLDSSRFRFLMSQRL 178
Cdd:cd00650   81 GRKPGMGRLDLLKRNVPIVKEIGDNIEKYSPDAWIIVVSNPVDIITYLVWRYSGLPKEKVIGLGT-LDPIRFRRILAEKL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 179 GVAPTSCHGWIIGEHGDSSVPVWSGVNIAgvrlrelnpilgtgedpekwnelhkqvvdsayeviklkgytswaigLSTAS 258
Cdd:cd00650  160 GVDPDDVKVYILGEHGGSQVPDWSTVRIA----------------------------------------------TSIAD 193
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442630559 259 LASAILRNTSSVAAVSTSVLGEHGIDKDVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSANIM 323
Cdd:cd00650  194 LIRSLLNDEGEILPVGVRNNGQIGIPDDVVVSVPCIVGKNGVEEPIEVGLTDFELEKLQKSADTL 258
MalateDH_bact TIGR01763
malate dehydrogenase, NAD-dependent; This enzyme converts malate into oxaloacetate in the ...
22-326 3.05e-60

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: 195.09  E-value: 3.05e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559   22 KVTIVGIGQVGMASAFsILAQNVSKEVCLIDVCADKLQGELMDLQHGSNF-LKNPQITASTDFAASANSRLCIVTAGVRQ 100
Cdd:TIGR01763   3 KISVIGAGFVGATTAF-RLAEKELADLVLLDVVEGIPQGKALDMYEASPVgGFDTKVTGTNNYADTANSDIVVITAGLPR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  101 KEGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMSQRLGV 180
Cdd:TIGR01763  82 KPGMSREDLLSMNAGIVREVTGRIMEHSPNPIIVVVSNPLDAMTYVAWQKSGFPKERVIGQAGVLDSARFRTFIAMELGV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  181 APTSCHGWIIGEHGDSSVPVWSGVNIAGVRLRELNPilgtgedPEKWNELHKQVVDSAYEVIKL--KGYTSWAIGLSTAS 258
Cdd:TIGR01763 162 SVQDVTACVLGGHGDAMVPLVRYSTVAGIPVADLIS-------AERIAEIVERTRKGGGEIVNLlkQGSAYYAPAASVVE 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442630559  259 LASAILRNTSSVAAVSTSVLGEHGIDkDVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSANIMSDV 326
Cdd:TIGR01763 235 MVEAILKDRKRVLPCAAYLDGQYGID-GIYVGVPVILGKNGVEHIYELKLDQSELALLNKSAKIVDEN 301
LDH-like_MDH_nadp cd05294
A lactate dehydrogenases-like structure with malate dehydrogenase enzymatic activity; The ...
22-325 1.48e-56

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: 185.69  E-value: 1.48e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  22 KVTIVGI-GQVGMASAFSILAQNVSKEVCLIDVCA--DKLQGELMDLQHG-SNFLKNPQITASTDFAASANSRLCIVTAG 97
Cdd:cd05294    2 KVSIIGAsGRVGSATALLLAKEDVVKEINLISRPKslEKLKGLRLDIYDAlAAAGIDAEIKISSDLSDVAGSDIVIITAG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  98 VRQKEGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMSQR 177
Cdd:cd05294   82 VPRKEGMSRLDLAKKNAKIVKKYAKQIAEFAPDTKILVVTNPVDVMTYKALKESGFDKNRVFGLGTHLDSLRFKVAIAKH 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 178 LGVAPTSCHGWIIGEHGDSSVPVWSGVNIAGVRLRELnpilgtgedpEKW-----NELHKQVVDSAYEVIKLKGYTSWAI 252
Cdd:cd05294  162 FNVHISEVHTRIIGEHGDSMVPLISSTSIGGIPIKRF----------PEYkdfdvEKIVETVKNAGQNIISLKGGSEYGP 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442630559 253 GLSTASLASAILRNTSSVAAVSTSVLGE-HGIdKDVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSANIMSD 325
Cdd:cd05294  232 ASAISNLVRTIANDERRILTVSTYLEGEiDGI-RDVCIGVPVKLGKNGIEEIVPIEMDDDEREAFRKSAEIVKK 304
PTZ00082 PTZ00082
L-lactate dehydrogenase; Provisional
22-331 3.59e-52

L-lactate dehydrogenase; Provisional


Pssm-ID: 173376 [Multi-domain]  Cd Length: 321  Bit Score: 174.88  E-value: 3.59e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  22 KVTIVGIGQVGMASAFSILAQNVSkEVCLIDVCADKLQGELMDLQHG-SNFLKNPQITASTDFAASANSRLCIVTAGVRQ 100
Cdd:PTZ00082   8 KISLIGSGNIGGVMAYLIVLKNLG-DVVLFDIVKNIPQGKALDISHSnVIAGSNSKVIGTNNYEDIAGSDVVIVTAGLTK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 101 KEGES-----RLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMS 175
Cdd:PTZ00082  87 RPGKSdkewnRDDLLPLNAKIMDEVAEGIKKYCPNAFVIVITNPLDVMVKLLQEHSGLPKNKVCGMAGVLDSSRLRTYIA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 176 QRLGVAPTSCHGWIIGEHGDSSVPVWSGVNIAGVRLRELNPILGTGEdpEKWNELHKQVVDSAYEVIKLKGYTS--WAIG 253
Cdd:PTZ00082 167 EKLGVNPRDVHASVIGAHGDKMVPLPRYVTVGGIPLSEFIKKGLITQ--EEIDEIVERTRNTGKEIVDLLGTGSayFAPA 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442630559 254 LSTASLASAILRNTSSVAAVSTSVLGEHGIdKDVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKSANIMSDVQAGLK 331
Cdd:PTZ00082 245 AAAIEMAEAYLKDKKRVLPCSAYLEGQYGH-KDIYMGTPAVIGANGVEKIIELDLTPEEQKKFDESIKEVKRLEALLK 321
Ldh_1_N pfam00056
lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic ...
22-160 5.21e-51

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: 165.86  E-value: 5.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559   22 KVTIVG-IGQVGMASAFSILAQNVSKEVCLIDVCADKLQGELMDLQHGSNFLKNPQITASTDFAASANSRLCIVTAGVRQ 100
Cdd:pfam00056   2 KVAVVGaAGGVGQSLAFLLANKGLADELVLYDIVKEKLEGVAMDLSHGSTFLLVPGIVGGGDYEDLKDADVVVITAGVPR 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  101 KEGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIG 160
Cdd:pfam00056  82 KPGMTRLDLLNVNAKIFKSIGPALAKYAPNAIVLVVSNPVDILTYVAWKASGFPPNRVFG 141
PTZ00117 PTZ00117
malate dehydrogenase; Provisional
22-328 1.81e-48

malate dehydrogenase; Provisional


Pssm-ID: 173409 [Multi-domain]  Cd Length: 319  Bit Score: 164.89  E-value: 1.81e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  22 KVTIVGIGQVGMASAFSILAQNVSkEVCLIDVCADKLQGELMDLQHGSNFLKNP-QITASTDFAASANSRLCIVTAGVRQ 100
Cdd:PTZ00117   7 KISMIGAGQIGSTVALLILQKNLG-DVVLYDVIKGVPQGKALDLKHFSTLVGSNiNILGTNNYEDIKDSDVVVITAGVQR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 101 KEGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFRFLMSQRLGV 180
Cdd:PTZ00117  86 KEEMTREDLLTINGKIMKSVAESVKKYCPNAFVICVTNPLDCMVKVFQEKSGIPSNKICGMAGVLDSSRFRCNLAEKLGV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 181 APTSCHGWIIGEHGDSSVPVWSGVNIAGVRLRELnpILGTGEDPEKWNELHKQVVDSAYEVIKL--KGYTSWAIGLSTAS 258
Cdd:PTZ00117 166 SPGDVSAVVIGGHGDLMVPLPRYCTVNGIPLSDF--VKKGAITEKEINEIIKKTRNMGGEIVKLlkKGSAFFAPAAAIVA 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442630559 259 LASAILRNTSSVAAVSTSVLGEHGIdKDVFLSLPCVLNANGVTSVVKQILTPTEVEQLQKS-ANIMSDVQA 328
Cdd:PTZ00117 244 MIEAYLKDEKRVLVCSVYLNGQYNC-KNLFVGVPVVIGGKGIEKVIELELNAEEKELFDKSiESIQELTQK 313
Ldh_1_C pfam02866
lactate/malate dehydrogenase, alpha/beta C-terminal domain; L-lactate dehydrogenases are ...
163-320 6.71e-29

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: 109.37  E-value: 6.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  163 TNLDSSRFRFLMSQRLGVAPTSCHGWIIGEHGDSSVPVWSGVNIAGVRLREL-NPILGTGEDPEKwnELHKQVVDSAYEV 241
Cdd:pfam02866   1 TTLDINRARTFLAEKAGVDPRVVNVPVIGGHSGTEFPDWSHANVTIIPLQSQvKENLKDSEWELE--ELTHRVQNAGYEV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  242 IKLK-GYTSWAIGLSTASLASAILRNTSSVAAVSTSVLGEHGIDKDVFLSLPCVLNANGVTSVVKQI-LTPTEVEQLQKS 319
Cdd:pfam02866  79 IKAKaGSATLSMAVAGARFIRAILRGEGGVLSVGVYEDGYYGVPDDIYFSFPVVLGKDGVEKVLEIGpLNDFEREKMEKS 158

                  .
gi 442630559  320 A 320
Cdd:pfam02866 159 A 159
MDH cd00704
Malate dehydrogenase; Malate dehydrogenase (MDH) is one of the key enzymes in the citric acid ...
22-317 1.55e-15

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: 76.16  E-value: 1.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  22 KVTIVGI-GQVGMASAFSILAQNV---SKEVCL----IDVCADKLQGELMDLQHgSNFLKNPQITASTDFA-ASANSRLC 92
Cdd:cd00704    2 HVLITGAaGQIGYNLLFLIASGELfgdDQPVILhlldIPPAMKALEGVVMELQD-CAFPLLKGVVITTDPEeAFKDVDVA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  93 IVTAGVRQKEGESRLSLVQRNTDILKNIIPKLVEY-SPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFR 171
Cdd:cd00704   81 ILVGAFPRKPGMERADLLRKNAKIFKEQGEALNKVaKPTVKVLVVGNPANTNALIALKNAPNLPPKNFTALTRLDHNRAK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 172 FLMSQRLGVAPTSCHGWII-GEHGDSSVPvwsGVNIAGVRLRELnPILGTGEDPEKW--NELHKQVVDSAYEVIKLKGYT 248
Cdd:cd00704  161 AQVARKLGVRVSDVKNVIIwGNHSNTQVP---DLSNAVVYGPGG-TEWVLDLLDEEWlnDEFVKTVQKRGAAIIKKRGAS 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 249 SwaiGLSTASLA----SAILRNTSSVAAVSTSVL---GEHGIDKDVFLSLPCVLNANG---VTSV-----VKQILTPTEV 313
Cdd:cd00704  237 S---AASAAKAIadhvKDWLFGTPPGEIVSMGVYspgNPYGIPPGIVFSFPCTCKGGGwhvVEDLklndwLREKLKATEE 313

                 ....
gi 442630559 314 EQLQ 317
Cdd:cd00704  314 ELIE 317
PTZ00325 PTZ00325
malate dehydrogenase; Provisional
22-332 2.30e-13

malate dehydrogenase; Provisional


Pssm-ID: 240360 [Multi-domain]  Cd Length: 321  Bit Score: 69.69  E-value: 2.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  22 KVTIVG----IGQvgmasAFSILAQNVS--KEVCLIDVCADKlqGELMDLQHgsnFLKNPQITASTD----FAASANSRL 91
Cdd:PTZ00325  10 KVAVLGaaggIGQ-----PLSLLLKQNPhvSELSLYDIVGAP--GVAADLSH---IDTPAKVTGYADgelwEKALRGADL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  92 CIVTAGVRQKEGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVAW----KLSGLPKNRVIGSgTNLDS 167
Cdd:PTZ00325  80 VLICAGVPRKPGMTRDDLFNTNAPIVRDLVAAVASSAPKAIVGIVSNPVNSTVPIAAetlkKAGVYDPRKLFGV-TTLDV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 168 SRFRFLMSQRLGVAPTSCHGWIIGEHGDSS-VPVWSGvniAGVRLRElnpilgtgedpEKWNELHKQVVDSAYEVIKLKG 246
Cdd:PTZ00325 159 VRARKFVAEALGMNPYDVNVPVVGGHSGVTiVPLLSQ---TGLSLPE-----------EQVEQITHRVQVGGDEVVKAKE 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 247 ytswAIGLSTASLASAilrntssVAAVSTSVL----GEHGI------DKDV-----FLSLPCVLNANGVTSVVKQ-ILTP 310
Cdd:PTZ00325 225 ----GAGSATLSMAYA-------AAEWSTSVLkalrGDKGIvecafvESDMrpecpFFSSPVELGKEGVERVLPIgPLNA 293
                        330       340
                 ....*....|....*....|...
gi 442630559 311 TEVEQLQKS-ANIMSDVQAGLKF 332
Cdd:PTZ00325 294 YEEELLEAAvPDLKKNIEKGLEF 316
LDH_protist TIGR01756
lactate dehydrogenase; This model represents a family of protist lactate dehydrogenases which ...
96-305 4.02e-07

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: 51.04  E-value: 4.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559   96 AGVRQKEGESRLSLVQRNTDILKNIIPKLVEYSPDTI-LLMVSNPVDIMTYVAW----KLSglPKNrvIGSGTNLDSSRF 170
Cdd:TIGR01756  68 ASVPLKPGEVRADLLTKNTPIFKATGEALSEYAKPTVkVLVIGNPVNTNCLVAMlhapKLS--AEN--FSSLCMLDHNRA 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  171 RFLMSQRLGVAPTSCHGWII-GEHGDSSVPVWSGVNIA-GVRLRELNPILgtgEDPEKWNELHKQVVDSAYEVIKLKGYT 248
Cdd:TIGR01756 144 VSRIASKLKVPVDHIYHVVVwGNHAESMVADLTHAEFTkNGKHQKVFDEL---CRDYPEPDFFEVIAQRAWKILEMRGFT 220
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442630559  249 SwAIGLSTASLA--SAILRNTSSVAAVSTSVL----GEHGIDKDVFLSLPCVLNANGVTSVVK 305
Cdd:TIGR01756 221 S-AASPVKASLQhmKAWLFGTRPGEVLSMGIPvpegNPYGIKPGVIFSFPCTVDEDGKVHVVE 282
MDH_euk_cyt TIGR01758
malate dehydrogenase, NAD-dependent; This model represents the NAD-dependent cytosolic malate ...
22-292 4.14e-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 [Multi-domain]  Cd Length: 324  Bit Score: 51.00  E-value: 4.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559   22 KVTIVGI-GQVG-----MASAFSILAQNVSKEVCLIDV--CADKLQGELMDLQHGSnFLKNPQITASTDFA-ASANSRLC 92
Cdd:TIGR01758   1 RVVVTGAaGQIGyallpMIARGRMLGKDQPIILHLLDIppAMKVLEGVVMELMDCA-FPLLDGVVPTHDPAvAFTDVDVA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559   93 IVTAGVRQKEGESRLSLVQRNTDILKNIIPKLVEY-SPDTILLMVSNPVDIMTYVAWKLSGLPKNRVIGSGTNLDSSRFR 171
Cdd:TIGR01758  80 ILVGAFPRKEGMERRDLLSKNVKIFKEQGRALDKLaKKDCKVLVVGNPANTNALVLSNYAPSIPPKNFSALTRLDHNRAL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  172 FLMSQRLGVAPTSCHGWII-GEHGDSSVPvwsGVNIAGVRlrelnpiLGTGEDP-------EKW--NELHKQVVDSAYEV 241
Cdd:TIGR01758 160 AQVAERAGVPVSDVKNVIIwGNHSSTQYP---DVNHATVT-------KGGKQKPvreaikdDAYldGEFITTVQQRGAAI 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 442630559  242 IKLKGYTSwaiGLSTASLASAILRN----TSSVAAVSTSVLGE---HGIDKDVFLSLP 292
Cdd:TIGR01758 230 IRARKLSS---ALSAAKAAVDQMHDwvlgTPEGTFVSMGVYSDgspYGVPKGLIFSFP 284
MDH_chloroplast-like cd01338
Chloroplast-like malate dehydrogenases; MDH is one of the key enzymes in the citric acid cycle, ...
58-305 3.54e-05

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: 44.89  E-value: 3.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  58 LQGELMDLQHGSnF--LKNPQITASTDFA-ASANSRLCiVTAGVRQKeGESRLSLVQRNTDILKNIIPKLVEY-SPDTIL 133
Cdd:cd01338   48 LEGVAMELEDCA-FplLAEIVITDDPNVAfKDADWALL-VGAKPRGP-GMERADLLKANGKIFTAQGKALNDVaSRDVKV 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 134 LMVSNPVDIMTYVAWKLS-GLPKNRvIGSGTNLDSSRFRFLMSQRLGVAPTSCHGWII-GEHGDSSVPVWSGVNIAGvrl 211
Cdd:cd01338  125 LVVGNPCNTNALIAMKNApDIPPDN-FTAMTRLDHNRAKSQLAKKAGVPVTDVKNMVIwGNHSPTQYPDFTNATIGG--- 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559 212 relNPILGTGEDpEKW--NELHKQVVDSAYEVIKLKGYTSwaiglsTASLASAIL---RN----TSSVAAVSTSVL--GE 280
Cdd:cd01338  201 ---KPAAEVIND-RAWleDEFIPTVQKRGAAIIKARGASS------AASAANAAIdhmRDwvlgTPEGDWFSMAVPsdGS 270
                        250       260
                 ....*....|....*....|....*
gi 442630559 281 HGIDKDVFLSLPCVLNaNGVTSVVK 305
Cdd:cd01338  271 YGIPEGLIFSFPVRSK-GGGYEIVE 294
PLN00106 PLN00106
malate dehydrogenase
91-193 1.02e-04

malate dehydrogenase


Pssm-ID: 215058 [Multi-domain]  Cd Length: 323  Bit Score: 43.40  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442630559  91 LCIVTAGVRQKEGESRLSLVQRNTDILKNIIPKLVEYSPDTILLMVSNPVDIMTYVA---WKLSGL--PKnRVIGSgTNL 165
Cdd:PLN00106  89 LVIIPAGVPRKPGMTRDDLFNINAGIVKTLCEAVAKHCPNALVNIISNPVNSTVPIAaevLKKAGVydPK-KLFGV-TTL 166
                         90       100
                 ....*....|....*....|....*...
gi 442630559 166 DSSRFRFLMSQRLGVAPTSCHGWIIGEH 193
Cdd:PLN00106 167 DVVRANTFVAEKKGLDPADVDVPVVGGH 194
 
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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