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Conserved domains on  [gi|498450293|ref|WP_010755815|]
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hypothetical protein [Enterococcus pallens]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
2-295 5.98e-126

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


The actual alignment was detected with superfamily member cd05291:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 306  Bit Score: 361.40  E-value: 5.98e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   2 KKAAIIGVGHVGSTLAYTLITRNIVDELVLFDKKEGQLLSEYNDLFDGQVDRYNHVKLIDSNLSELADTDVLIFSAGDIT 81
Cdd:cd05291    1 RKVVIIGAGHVGSSFAYSLVNQGIADELVLIDINEEKAEGEALDLEDALAFLPSPVKIKAGDYSDCKDADIVVITAGAPQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  82 IfeGNSDRFAELYLTKEIVEEWAPKIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGTTLDSARMKHAVSKKF 161
Cdd:cd05291   81 K--PGETRLDLLEKNAKIMKSIVPKIKASGFDGIFLVASNPVDVITYVVQKLSGLPKNRVIGTGTSLDTARLRRALAEKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 162 NVHPSSVEGYVLGEHGESQFVAWSSVRIGGIPIAEML-----SASELEELEGIARAGGWITMRGKGYTSFGIANQAALVV 236
Cdd:cd05291  159 NVDPRSVHAYVLGEHGDSQFVAWSTVTVGGKPLLDLLkegklSELDLDEIEEDVRKAGYEIINGKGATYYGIATALARIV 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498450293 237 EAVLNNNFKVLPVSSYSE----KDQCYAGHPAKVGSTGIIEDYHFSLTELEKQKWEKSIETIK 295
Cdd:cd05291  239 KAILNDENAILPVSAYLDgeygEKDVYIGVPAIIGRNGVEEVIELDLTEEEQEKFEKSADIIK 301
 
Name Accession Description Interval E-value
HicDH_like cd05291
L-2-hydroxyisocapronate dehydrogenases and some bacterial L-lactate dehydrogenases; ...
2-295 5.98e-126

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: 361.40  E-value: 5.98e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   2 KKAAIIGVGHVGSTLAYTLITRNIVDELVLFDKKEGQLLSEYNDLFDGQVDRYNHVKLIDSNLSELADTDVLIFSAGDIT 81
Cdd:cd05291    1 RKVVIIGAGHVGSSFAYSLVNQGIADELVLIDINEEKAEGEALDLEDALAFLPSPVKIKAGDYSDCKDADIVVITAGAPQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  82 IfeGNSDRFAELYLTKEIVEEWAPKIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGTTLDSARMKHAVSKKF 161
Cdd:cd05291   81 K--PGETRLDLLEKNAKIMKSIVPKIKASGFDGIFLVASNPVDVITYVVQKLSGLPKNRVIGTGTSLDTARLRRALAEKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 162 NVHPSSVEGYVLGEHGESQFVAWSSVRIGGIPIAEML-----SASELEELEGIARAGGWITMRGKGYTSFGIANQAALVV 236
Cdd:cd05291  159 NVDPRSVHAYVLGEHGDSQFVAWSTVTVGGKPLLDLLkegklSELDLDEIEEDVRKAGYEIINGKGATYYGIATALARIV 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498450293 237 EAVLNNNFKVLPVSSYSE----KDQCYAGHPAKVGSTGIIEDYHFSLTELEKQKWEKSIETIK 295
Cdd:cd05291  239 KAILNDENAILPVSAYLDgeygEKDVYIGVPAIIGRNGVEEVIELDLTEEEQEKFEKSADIIK 301
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ...
2-295 1.11e-102

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: 302.32  E-value: 1.11e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   2 KKAAIIGVGHVGSTLAYTLITRNIVDELVLFDKKEGQLLSEYNDLFDGQVDRYNHVKLIDSNLSELADTDVLIFSAGdIT 81
Cdd:COG0039    1 MKVAIIGAGNVGSTLAFRLASGGLADELVLIDINEGKAEGEALDLADAFPLLGFDVKITAGDYEDLADADVVVITAG-AP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  82 IFEGNSdRFAELYLTKEIVEEWAPKIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGTTLDSARMKHAVSKKF 161
Cdd:COG0039   80 RKPGMS-RLDLLEANAKIFKSVGEAIKKYAPDAIVLVVTNPVDVMTYIAQKASGLPKERVIGMGTVLDSARFRSFLAEKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 162 NVHPSSVEGYVLGEHGESQFVAWSSVRIGGIPIAEMLSASE--LEELEGIARAGGWITMRGKGYTSFGIANQAALVVEAV 239
Cdd:COG0039  159 GVSPRDVHAYVLGEHGDSMVPLWSHATVGGIPLTELIKETDedLDEIIERVRKGGAEIIEGKGSTYYAIAAAAARIVEAI 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498450293 240 LNNNFKVLPVSSYSE-----KDqCYAGHPAKVGSTGIIEDYHFSLTELEKQKWEKSIETIK 295
Cdd:COG0039  239 LRDEKRVLPVSVYLDgeygiED-VYLGVPVVIGRNGVEKIVELELTDEERAKLDASAEELK 298
L-LDH-NAD TIGR01771
L-lactate dehydrogenase; This model represents the NAD-dependent L-lactate dehydrogenases from ...
6-295 1.87e-89

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: 268.68  E-value: 1.87e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293    6 IIGVGHVGSTLAYTLITRNIVDELVLFDKKEGQLLSEYNDLFDGQVDRYNHVKLIDSNLSELADTDVLIFSAGDITifEG 85
Cdd:TIGR01771   1 IIGAGNVGSSTAFALLNQGIADEIVLIDINKDKAEGEAMDLQHAASFLPTPKKIRSGDYSDCKDADLVVITAGAPQ--KP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   86 NSDRFAELYLTKEIVEEWAPKIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGTTLDSARMKHAVSKKFNVHP 165
Cdd:TIGR01771  79 GETRLELVGRNVRIMKSIVPEVVKSGFDGIFLVATNPVDILTYVAWKLSGFPKNRVIGSGTVLDTARLRYLLAEKLGVDP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  166 SSVEGYVLGEHGESQFVAWSSVRIGGIPIAEMLSAS------ELEELEGIARAGGWITMRGKGYTSFGIANQAALVVEAV 239
Cdd:TIGR01771 159 QSVHAYIIGEHGDSEVPVWSSATIGGVPLLDYLKAKgtetdlDLEEIEKEVRDAAYEIINRKGATYYGIGMAVARIVEAI 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  240 LNNNFKVLPVSSYSE----KDQCYAGHPAKVGSTGIIEDYHFSLTELEKQKWEKSIETIK 295
Cdd:TIGR01771 239 LHDENRVLPVSAYLDgeygIKDVYIGVPAVLGRNGVEEIIELPLSDEEKEAFQKSAETLK 298
ldh PRK00066
L-lactate dehydrogenase; Reviewed
2-295 1.04e-69

L-lactate dehydrogenase; Reviewed


Pssm-ID: 178836 [Multi-domain]  Cd Length: 315  Bit Score: 218.61  E-value: 1.04e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   2 KKAAIIGVGHVGSTLAYTLITRNIVDELVLFDKKEGQLLSEYNDLFDGqVDRYNHVKLIDSNLSELADTDVLIFSAG--- 78
Cdd:PRK00066   7 NKVVLVGDGAVGSSYAYALVNQGIADELVIIDINKEKAEGDAMDLSHA-VPFTSPTKIYAGDYSDCKDADLVVITAGapq 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  79 ------------DITIFegnsdrfaelyltKEIVEEwapkIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGT 146
Cdd:PRK00066  86 kpgetrldlvekNLKIF-------------KSIVGE----VMASGFDGIFLVASNPVDILTYATWKLSGFPKERVIGSGT 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 147 TLDSARMKHAVSKKFNVHPSSVEGYVLGEHGESQFVAWSSVRIGGIPIAEMLS------ASELEELEGIARAGGWITMRG 220
Cdd:PRK00066 149 SLDSARFRYMLSEKLDVDPRSVHAYIIGEHGDTEFPVWSHANVAGVPLEEYLEeneqydEEDLDEIFENVRDAAYEIIEK 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498450293 221 KGYTSFGIANQAALVVEAVLNNNFKVLPVSSYSE----KDQCYAGHPAKVGSTGIIEDYHFSLTELEKQKWEKSIETIK 295
Cdd:PRK00066 229 KGATYYGIAMALARITKAILNNENAVLPVSAYLEgqygEEDVYIGVPAVVNRNGIREIVELPLNDDEKQKFAHSADVLK 307
Ldh_1_C pfam02866
lactate/malate dehydrogenase, alpha/beta C-terminal domain; L-lactate dehydrogenases are ...
146-295 4.63e-24

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: 95.89  E-value: 4.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  146 TTLDSARMKHAVSKKFNVHPSSVEGYVLGEHGESQFVAWSSVRIGGIPIAEM------LSASELEEL-EGIARAGGWITM 218
Cdd:pfam02866   1 TTLDINRARTFLAEKAGVDPRVVNVPVIGGHSGTEFPDWSHANVTIIPLQSQvkenlkDSEWELEELtHRVQNAGYEVIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  219 RGKGYTSFGIANQAALVVEAVLNNNFKVLPVSSYSE-----KDQCYAGHPAKVGSTGIIEDYH-FSLTELEKQKWEKSIE 292
Cdd:pfam02866  81 AKAGSATLSMAVAGARFIRAILRGEGGVLSVGVYEDgyygvPDDIYFSFPVVLGKDGVEKVLEiGPLNDFEREKMEKSAA 160

                  ...
gi 498450293  293 TIK 295
Cdd:pfam02866 161 ELK 163
 
Name Accession Description Interval E-value
HicDH_like cd05291
L-2-hydroxyisocapronate dehydrogenases and some bacterial L-lactate dehydrogenases; ...
2-295 5.98e-126

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: 361.40  E-value: 5.98e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   2 KKAAIIGVGHVGSTLAYTLITRNIVDELVLFDKKEGQLLSEYNDLFDGQVDRYNHVKLIDSNLSELADTDVLIFSAGDIT 81
Cdd:cd05291    1 RKVVIIGAGHVGSSFAYSLVNQGIADELVLIDINEEKAEGEALDLEDALAFLPSPVKIKAGDYSDCKDADIVVITAGAPQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  82 IfeGNSDRFAELYLTKEIVEEWAPKIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGTTLDSARMKHAVSKKF 161
Cdd:cd05291   81 K--PGETRLDLLEKNAKIMKSIVPKIKASGFDGIFLVASNPVDVITYVVQKLSGLPKNRVIGTGTSLDTARLRRALAEKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 162 NVHPSSVEGYVLGEHGESQFVAWSSVRIGGIPIAEML-----SASELEELEGIARAGGWITMRGKGYTSFGIANQAALVV 236
Cdd:cd05291  159 NVDPRSVHAYVLGEHGDSQFVAWSTVTVGGKPLLDLLkegklSELDLDEIEEDVRKAGYEIINGKGATYYGIATALARIV 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498450293 237 EAVLNNNFKVLPVSSYSE----KDQCYAGHPAKVGSTGIIEDYHFSLTELEKQKWEKSIETIK 295
Cdd:cd05291  239 KAILNDENAILPVSAYLDgeygEKDVYIGVPAIIGRNGVEEVIELDLTEEEQEKFEKSADIIK 301
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ...
2-295 1.11e-102

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: 302.32  E-value: 1.11e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   2 KKAAIIGVGHVGSTLAYTLITRNIVDELVLFDKKEGQLLSEYNDLFDGQVDRYNHVKLIDSNLSELADTDVLIFSAGdIT 81
Cdd:COG0039    1 MKVAIIGAGNVGSTLAFRLASGGLADELVLIDINEGKAEGEALDLADAFPLLGFDVKITAGDYEDLADADVVVITAG-AP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  82 IFEGNSdRFAELYLTKEIVEEWAPKIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGTTLDSARMKHAVSKKF 161
Cdd:COG0039   80 RKPGMS-RLDLLEANAKIFKSVGEAIKKYAPDAIVLVVTNPVDVMTYIAQKASGLPKERVIGMGTVLDSARFRSFLAEKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 162 NVHPSSVEGYVLGEHGESQFVAWSSVRIGGIPIAEMLSASE--LEELEGIARAGGWITMRGKGYTSFGIANQAALVVEAV 239
Cdd:COG0039  159 GVSPRDVHAYVLGEHGDSMVPLWSHATVGGIPLTELIKETDedLDEIIERVRKGGAEIIEGKGSTYYAIAAAAARIVEAI 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498450293 240 LNNNFKVLPVSSYSE-----KDqCYAGHPAKVGSTGIIEDYHFSLTELEKQKWEKSIETIK 295
Cdd:COG0039  239 LRDEKRVLPVSVYLDgeygiED-VYLGVPVVIGRNGVEKIVELELTDEERAKLDASAEELK 298
L-LDH-NAD TIGR01771
L-lactate dehydrogenase; This model represents the NAD-dependent L-lactate dehydrogenases from ...
6-295 1.87e-89

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: 268.68  E-value: 1.87e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293    6 IIGVGHVGSTLAYTLITRNIVDELVLFDKKEGQLLSEYNDLFDGQVDRYNHVKLIDSNLSELADTDVLIFSAGDITifEG 85
Cdd:TIGR01771   1 IIGAGNVGSSTAFALLNQGIADEIVLIDINKDKAEGEAMDLQHAASFLPTPKKIRSGDYSDCKDADLVVITAGAPQ--KP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   86 NSDRFAELYLTKEIVEEWAPKIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGTTLDSARMKHAVSKKFNVHP 165
Cdd:TIGR01771  79 GETRLELVGRNVRIMKSIVPEVVKSGFDGIFLVATNPVDILTYVAWKLSGFPKNRVIGSGTVLDTARLRYLLAEKLGVDP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  166 SSVEGYVLGEHGESQFVAWSSVRIGGIPIAEMLSAS------ELEELEGIARAGGWITMRGKGYTSFGIANQAALVVEAV 239
Cdd:TIGR01771 159 QSVHAYIIGEHGDSEVPVWSSATIGGVPLLDYLKAKgtetdlDLEEIEKEVRDAAYEIINRKGATYYGIGMAVARIVEAI 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  240 LNNNFKVLPVSSYSE----KDQCYAGHPAKVGSTGIIEDYHFSLTELEKQKWEKSIETIK 295
Cdd:TIGR01771 239 LHDENRVLPVSAYLDgeygIKDVYIGVPAVLGRNGVEEIIELPLSDEEKEAFQKSAETLK 298
LDH_like cd00300
L-lactate dehydrogenase-like enzymes; Members of this subfamily are tetrameric NAD-dependent ...
5-295 1.17e-83

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: 253.73  E-value: 1.17e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   5 AIIGVGHVGSTLAYTLITRNIVDELVLFDKKEGQLLSEYNDLFDGQVDRYNHVKLIDSNLSELADTDVLIFSAGdiTIFE 84
Cdd:cd00300    2 TIIGAGNVGAAVAFALIAKGLASELVLVDVNEEKAKGDALDLSHASAFLATGTIVRGGDYADAADADIVVITAG--APRK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  85 GNSDRFAELYLTKEIVEEWAPKIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGTTLDSARMKHAVSKKFNVH 164
Cdd:cd00300   80 PGETRLDLINRNAPILRSVITNLKKYGPDAIILVVSNPVDILTYVAQKLSGLPKNRVIGSGTLLDSARFRSLLAEKLDVD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 165 PSSVEGYVLGEHGESQFVAWSSVRIGGIPIAEML--SASELEELEGIARAGGWITMRGKGYTSFGIANQAALVVEAVLNN 242
Cdd:cd00300  160 PQSVHAYVLGEHGDSQVVAWSTATVGGLPLEELApfTKLDLEAIEEEVRTSGYEIIRLKGATNYGIATAIADIVKSILLD 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 498450293 243 NFKVLPVSSYSEK----DQCYAGHPAKVGSTGIIEDYHFSLTELEKQKWEKSIETIK 295
Cdd:cd00300  240 ERRVLPVSAVQEGqygiEDVALSVPAVVGREGVVRILEIPLTEDEEAKLQKSAEALK 296
LDH_2 cd05292
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
3-295 4.60e-70

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: 219.28  E-value: 4.60e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   3 KAAIIGVGHVGSTLAYTLITRNIVDELVLFD----KKEGQLLseynDLFDGqVDRYNHVKLIDSNLSELADTDVLIFSAG 78
Cdd:cd05292    2 KVAIVGAGFVGSTTAYALLLRGLASEIVLVDinkaKAEGEAM----DLAHG-TPFVKPVRIYAGDYADCKGADVVVITAG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  79 ditifegNSDRFAE--LYLTK---EIVEEWAPKIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGTTLDSARM 153
Cdd:cd05292   77 -------ANQKPGEtrLDLLKrnvAIFKEIIPQILKYAPDAILLVVTNPVDVLTYVAYKLSGLPPNRVIGSGTVLDTARF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 154 KHAVSKKFNVHPSSVEGYVLGEHGESQFVAWSSVRIGGIPIAEM-------LSASELEEL-EGIARAGGWItMRGKGYTS 225
Cdd:cd05292  150 RYLLGEHLGVDPRSVHAYIIGEHGDSEVAVWSSANIGGVPLDEFcklcgrpFDEEVREEIfEEVRNAAYEI-IERKGATY 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498450293 226 FGIANQAALVVEAVLNNNFKVLPVSS-----YSEKDqCYAGHPAKVGSTGIIEDYHFSLTELEKQKWEKSIETIK 295
Cdd:cd05292  229 YAIGLALARIVEAILRDENSVLTVSSlldgqYGIKD-VALSLPCIVGRSGVERVLPPPLSEEEEEALRASAEVLK 302
ldh PRK00066
L-lactate dehydrogenase; Reviewed
2-295 1.04e-69

L-lactate dehydrogenase; Reviewed


Pssm-ID: 178836 [Multi-domain]  Cd Length: 315  Bit Score: 218.61  E-value: 1.04e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   2 KKAAIIGVGHVGSTLAYTLITRNIVDELVLFDKKEGQLLSEYNDLFDGqVDRYNHVKLIDSNLSELADTDVLIFSAG--- 78
Cdd:PRK00066   7 NKVVLVGDGAVGSSYAYALVNQGIADELVIIDINKEKAEGDAMDLSHA-VPFTSPTKIYAGDYSDCKDADLVVITAGapq 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  79 ------------DITIFegnsdrfaelyltKEIVEEwapkIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGT 146
Cdd:PRK00066  86 kpgetrldlvekNLKIF-------------KSIVGE----VMASGFDGIFLVASNPVDILTYATWKLSGFPKERVIGSGT 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 147 TLDSARMKHAVSKKFNVHPSSVEGYVLGEHGESQFVAWSSVRIGGIPIAEMLS------ASELEELEGIARAGGWITMRG 220
Cdd:PRK00066 149 SLDSARFRYMLSEKLDVDPRSVHAYIIGEHGDTEFPVWSHANVAGVPLEEYLEeneqydEEDLDEIFENVRDAAYEIIEK 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498450293 221 KGYTSFGIANQAALVVEAVLNNNFKVLPVSSYSE----KDQCYAGHPAKVGSTGIIEDYHFSLTELEKQKWEKSIETIK 295
Cdd:PRK00066 229 KGATYYGIAMALARITKAILNNENAVLPVSAYLEgqygEEDVYIGVPAVVNRNGIREIVELPLNDDEKQKFAHSADVLK 307
PRK06223 PRK06223
malate dehydrogenase; Reviewed
1-295 2.25e-69

malate dehydrogenase; Reviewed


Pssm-ID: 180477 [Multi-domain]  Cd Length: 307  Bit Score: 217.69  E-value: 2.25e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   1 MKKAAIIGVGHVGSTLAYTLITRNIVDeLVLFDKKEGQLLSEYNDLFD-GQVDRYNHVKLIDSNLSELADTDVLIFSAG- 78
Cdd:PRK06223   2 RKKISIIGAGNVGATLAHLLALKELGD-VVLFDIVEGVPQGKALDIAEaAPVEGFDTKITGTNDYEDIAGSDVVVITAGv 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  79 ---------DItiFEGNSDrfaelyltkeIVEEWAPKIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGTTLD 149
Cdd:PRK06223  81 prkpgmsrdDL--LGINAK----------IMKDVAEGIKKYAPDAIVIVVTNPVDAMTYVALKESGFPKNRVIGMAGVLD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 150 SARMKHAVSKKFNVHPSSVEGYVLGEHGESQFVAWSSVRIGGIPIAEMLSASELEELegIAR---AGGWIT-MRGKGYTS 225
Cdd:PRK06223 149 SARFRTFIAEELNVSVKDVTAFVLGGHGDSMVPLVRYSTVGGIPLEDLLSKEKLDEI--VERtrkGGAEIVgLLKTGSAY 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498450293 226 FGIANQAALVVEAVLNNNFKVLPVSSYSE-----KDqCYAGHPAKVGSTGIIEDYHFSLTELEKQKWEKSIETIK 295
Cdd:PRK06223 227 YAPAASIAEMVEAILKDKKRVLPCSAYLEgeygvKD-VYVGVPVKLGKNGVEKIIELELDDEEKAAFDKSVEAVK 300
LDH_1 cd05293
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
3-294 3.81e-60

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: 193.98  E-value: 3.81e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   3 KAAIIGVGHVGSTLAYTLITRNIVDELVLFDKKEGQLLSEYNDLFDGQVDRYNHVKLIDSNLSELADTDVLIFSAGDITi 82
Cdd:cd05293    5 KVTVVGVGQVGMACAISILAKGLADELVLVDVVEDKLKGEAMDLQHGSAFLKNPKIEADKDYSVTANSKVVIVTAGARQ- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  83 fEGNSDRFAELYLTKEIVEEWAPKIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGTTLDSARMKHAVSKKFN 162
Cdd:cd05293   84 -NEGESRLDLVQRNVDIFKGIIPKLVKYSPNAILLVVSNPVDIMTYVAWKLSGLPKHRVIGSGCNLDSARFRYLIAERLG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 163 VHPSSVEGYVLGEHGESQFVAWSSVRIGGIPIAEML----SASELEELEGIARA---GGWITMRGKGYTSFGIANQAALV 235
Cdd:cd05293  163 VAPSSVHGWIIGEHGDSSVPVWSGVNVAGVRLQDLNpdigTDKDPEKWKEVHKQvvdSAYEVIKLKGYTSWAIGLSVADL 242
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498450293 236 VEAVLNNNFKVLPVSSYSE-----KDQCYAGHPAKVGSTGIIEDYHFSLTELEKQKWEKSIETI 294
Cdd:cd05293  243 VDAILRNTGRVHSVSTLVKglhgiEDEVFLSLPCILGENGITHVIKQPLTEEEQEKLQKSADTL 306
LDH-like_MDH cd01339
L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an ...
5-295 4.18e-60

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: 193.46  E-value: 4.18e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   5 AIIGVGHVGSTLAYTLITRNIVDeLVLFDKKEGQLLSEYNDLFD-GQVDRYNhVKLIDSN-LSELADTDVLIFSAGdITI 82
Cdd:cd01339    2 SIIGAGNVGATLAQLLALKELGD-VVLLDIVEGLPQGKALDISQaAPILGSD-TKVTGTNdYEDIAGSDVVVITAG-IPR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  83 FEGNSdRFAELYLTKEIVEEWAPKIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGTTLDSARMKHAVSKKFN 162
Cdd:cd01339   79 KPGMS-RDDLLGTNAKIVKEVAENIKKYAPNAIVIVVTNPLDVMTYVAYKASGFPRNRVIGMAGVLDSARFRYFIAEELG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 163 VHPSSVEGYVLGEHGESQFVAWSSVRIGGIPIAEMLSASELEELEGIARAGGW--ITMRGKGYTSFGIANQAALVVEAVL 240
Cdd:cd01339  158 VSVKDVQAMVLGGHGDTMVPLPRYSTVGGIPLTELITKEEIDEIVERTRNGGAeiVNLLKTGSAYYAPAAAIAEMVEAIL 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 241 NNNFKVLPVSSYSE-----KDqCYAGHPAKVGSTGIIEDYHFSLTELEKQKWEKSIETIK 295
Cdd:cd01339  238 KDKKRVLPCSAYLEgeygiKD-IFVGVPVVLGKNGVEKIIELDLTDEEKEAFDKSVESVK 296
LDH_3 cd05290
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
3-295 1.52e-54

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: 179.45  E-value: 1.52e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   3 KAAIIGVGHVGSTLAYTLITRNIVDELVLFDKKEGQLLSEYNDLFDGQVDRYN-HVKLIDSNLSELADTDVLIFSAGDiT 81
Cdd:cd05290    1 KLVVIGAGHVGSAVLNYALALGLFSEIVLIDVNEGVAEGEALDFHHATALTYStNTKIRAGDYDDCADADIIVITAGP-S 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  82 IFEGNSDRFAELYLTK-EIVEEWAPKIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGTTLDSARMKHAVSKK 160
Cdd:cd05290   80 IDPGNTDDRLDLAQTNaKIIREIMGNITKVTKEAVIILITNPLDIAVYIAATEFDYPANKVIGTGTMLDTARLRRIVADK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 161 FNVHPSSVEGYVLGEHGESQFVAWSSVRIGGIPIAEMLSASELE-----ELEGIARAGGWITMRGKGYTSFGIANQAALV 235
Cdd:cd05290  160 YGVDPKNVTGYVLGEHGSHAFPVWSLVNIAGLPLDELEALFGKEpidkdELLEEVVQAAYDVFNRKGWTNAGIAKSASRL 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498450293 236 VEAVLNNNFKVLPVSSYSEKdqcYAGH-------PAKVGSTGIIEDYHFSLTELEKQKWEKSIETIK 295
Cdd:cd05290  240 IKAILLDERSILPVCTLLSG---EYGLsdvalslPTVIGAKGIERVLEIPLDEWELEKLHKSAKAIR 303
PLN02602 PLN02602
lactate dehydrogenase
3-294 1.39e-47

lactate dehydrogenase


Pssm-ID: 178212 [Multi-domain]  Cd Length: 350  Bit Score: 162.63  E-value: 1.39e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   3 KAAIIGVGHVGSTLAYTLITRNIVDELVLFDKKEGQLLSEYNDLfdgqvdryNHVKLIDSNLSELADTDVLIFSAGDITI 82
Cdd:PLN02602  39 KVSVVGVGNVGMAIAQTILTQDLADELALVDVNPDKLRGEMLDL--------QHAAAFLPRTKILASTDYAVTAGSDLCI 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  83 F-------EGNS-----DRFAELYltKEIVeewaPKIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGTTLDS 150
Cdd:PLN02602 111 VtagarqiPGESrlnllQRNVALF--RKII----PELAKYSPDTILLIVSNPVDVLTYVAWKLSGFPANRVIGSGTNLDS 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 151 ARMKHAVSKKFNVHPSSVEGYVLGEHGESQFVAWSSVRIGGIPIAEML----SASELEELEGIARA---GGWITMRGKGY 223
Cdd:PLN02602 185 SRFRFLIADHLDVNAQDVQAYIVGEHGDSSVALWSSVSVGGVPVLSFLekqqIAYEKETLEEIHRAvvdSAYEVIKLKGY 264
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498450293 224 TSFGIANQAALVVEAVLNNNFKVLPVSSYS------EKDQCYAGHPAKVGSTGIIEDYHFSLTELEKQKWEKSIETI 294
Cdd:PLN02602 265 TSWAIGYSVASLVRSLLRDQRRIHPVSVLAkgfhgiDEGDVFLSLPAQLGRNGVLGVVNVHLTDEEAERLRKSAKTL 341
PTZ00082 PTZ00082
L-lactate dehydrogenase; Provisional
2-297 5.06e-46

L-lactate dehydrogenase; Provisional


Pssm-ID: 173376 [Multi-domain]  Cd Length: 321  Bit Score: 157.93  E-value: 5.06e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   2 KKAAIIGVGHVGSTLAYTLITRNIVDeLVLFDKKEGQLLSEYNDLFDGQVDRYNHVKLIDSN-LSELADTDVLIFSAGdI 80
Cdd:PTZ00082   7 RKISLIGSGNIGGVMAYLIVLKNLGD-VVLFDIVKNIPQGKALDISHSNVIAGSNSKVIGTNnYEDIAGSDVVIVTAG-L 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  81 TIFEGNSD----RFAELYLTKEIVEEWAPKIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGTTLDSARMKHA 156
Cdd:PTZ00082  85 TKRPGKSDkewnRDDLLPLNAKIMDEVAEGIKKYCPNAFVIVITNPLDVMVKLLQEHSGLPKNKVCGMAGVLDSSRLRTY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 157 VSKKFNVHPSSVEGYVLGEHGESQFVAWSSVRIGGIPIAE-----MLSASELEELEGIARAGGW--ITMRGKGYTSFGIA 229
Cdd:PTZ00082 165 IAEKLGVNPRDVHASVIGAHGDKMVPLPRYVTVGGIPLSEfikkgLITQEEIDEIVERTRNTGKeiVDLLGTGSAYFAPA 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498450293 230 NQAALVVEAVLNNNFKVLPVSSYSE-----KDqCYAGHPAKVGSTGIIEDYHFSLTELEKQKWEKSIETIKFM 297
Cdd:PTZ00082 245 AAAIEMAEAYLKDKKRVLPCSAYLEgqyghKD-IYMGTPAVIGANGVEKIIELDLTPEEQKKFDESIKEVKRL 316
LDH-like_MDH_nadp cd05294
A lactate dehydrogenases-like structure with malate dehydrogenase enzymatic activity; The ...
3-295 2.91e-43

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: 150.25  E-value: 2.91e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   3 KAAIIGV-GHVGSTLAYTLITRNIVDELVLFDKKEG--QLLSEYNDLFDGQVDRYNHVKL-IDSNLSELADTDVLIFSAG 78
Cdd:cd05294    2 KVSIIGAsGRVGSATALLLAKEDVVKEINLISRPKSleKLKGLRLDIYDALAAAGIDAEIkISSDLSDVAGSDIVIITAG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  79 dITIFEGNSdrfaELYLTKE---IVEEWAPKIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGTTLDSARMKH 155
Cdd:cd05294   82 -VPRKEGMS----RLDLAKKnakIVKKYAKQIAEFAPDTKILVVTNPVDVMTYKALKESGFDKNRVFGLGTHLDSLRFKV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 156 AVSKKFNVHPSSVEGYVLGEHGESQFVAWSSVRIGGIPIAEMLSASEL---EELEGIARAGGWItMRGKGYTSFGIANQA 232
Cdd:cd05294  157 AIAKHFNVHISEVHTRIIGEHGDSMVPLISSTSIGGIPIKRFPEYKDFdveKIVETVKNAGQNI-ISLKGGSEYGPASAI 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498450293 233 ALVVEAVLNNNFKVLPVSSYSE------KDQCYaGHPAKVGSTGIIEDYHFSLTELEKQKWEKSIETIK 295
Cdd:cd05294  236 SNLVRTIANDERRILTVSTYLEgeidgiRDVCI-GVPVKLGKNGIEEIVPIEMDDDEREAFRKSAEIVK 303
LDH_MDH_like cd00650
NAD-dependent, lactate dehydrogenase-like, 2-hydroxycarboxylate dehydrogenase family; Members ...
5-295 5.13e-41

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: 143.23  E-value: 5.13e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   5 AIIGV-GHVGSTLAYTLITR--NIVDELVLFDKKEGQLLSEYNDLFDGQVDRYNHVKLIDSNLSE-LADTDVLIFSAGdI 80
Cdd:cd00650    2 AVIGAgGNVGPALAFGLADGsvLLAIELVLYDIDEEKLKGVAMDLQDAVEPLADIKVSITDDPYEaFKDADVVIITAG-V 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  81 TIFEGnSDRFAELYLTKEIVEEWAPKIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGTtLDSARMKHAVSKK 160
Cdd:cd00650   81 GRKPG-MGRLDLLKRNVPIVKEIGDNIEKYSPDAWIIVVSNPVDIITYLVWRYSGLPKEKVIGLGT-LDPIRFRRILAEK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 161 FNVHPSSVEGYVLGEHGESQFVAWSSVRiggipiaemlsaseleelegiaraggwitmrgkgytsfgIANQAALVVEAVL 240
Cdd:cd00650  159 LGVDPDDVKVYILGEHGGSQVPDWSTVR---------------------------------------IATSIADLIRSLL 199
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 241 NNNFKVLPVSSYSE-----KDQCYAGHPAKVGSTGIIEDYHFSLTELEKQKWEKSIETIK 295
Cdd:cd00650  200 NDEGEILPVGVRNNgqigiPDDVVVSVPCIVGKNGVEEPIEVGLTDFELEKLQKSADTLK 259
PTZ00117 PTZ00117
malate dehydrogenase; Provisional
1-301 3.29e-38

malate dehydrogenase; Provisional


Pssm-ID: 173409 [Multi-domain]  Cd Length: 319  Bit Score: 137.16  E-value: 3.29e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   1 MKKAAIIGVGHVGSTLAYTLITRNIVDeLVLFDKKEGQLLSEYNDLfdgqvdryNHVK-LIDSN--------LSELADTD 71
Cdd:PTZ00117   5 RKKISMIGAGQIGSTVALLILQKNLGD-VVLYDVIKGVPQGKALDL--------KHFStLVGSNinilgtnnYEDIKDSD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  72 VLIFSAGdITIFEGNSDRfaELY-LTKEIVEEWAPKIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFGTGTTLDS 150
Cdd:PTZ00117  76 VVVITAG-VQRKEEMTRE--DLLtINGKIMKSVAESVKKYCPNAFVICVTNPLDCMVKVFQEKSGIPSNKICGMAGVLDS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 151 ARMKHAVSKKFNVHPSSVEGYVLGEHGESQFVAWSSVRIGGIPIAE-----MLSASELEEL-EGIARAGGWIT-MRGKGY 223
Cdd:PTZ00117 153 SRFRCNLAEKLGVSPGDVSAVVIGGHGDLMVPLPRYCTVNGIPLSDfvkkgAITEKEINEIiKKTRNMGGEIVkLLKKGS 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293 224 TSFGIANQAALVVEAVLNNNFKVLPVSS-----YSEKDqCYAGHPAKVGSTGIIEDYHFSLTELEKQKWEKSIETIKFMH 298
Cdd:PTZ00117 233 AFFAPAAAIVAMIEAYLKDEKRVLVCSVylngqYNCKN-LFVGVPVVIGGKGIEKVIELELNAEEKELFDKSIESIQELT 311

                 ...
gi 498450293 299 STA 301
Cdd:PTZ00117 312 QKA 314
Ldh_1_C pfam02866
lactate/malate dehydrogenase, alpha/beta C-terminal domain; L-lactate dehydrogenases are ...
146-295 4.63e-24

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: 95.89  E-value: 4.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  146 TTLDSARMKHAVSKKFNVHPSSVEGYVLGEHGESQFVAWSSVRIGGIPIAEM------LSASELEEL-EGIARAGGWITM 218
Cdd:pfam02866   1 TTLDINRARTFLAEKAGVDPRVVNVPVIGGHSGTEFPDWSHANVTIIPLQSQvkenlkDSEWELEELtHRVQNAGYEVIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293  219 RGKGYTSFGIANQAALVVEAVLNNNFKVLPVSSYSE-----KDQCYAGHPAKVGSTGIIEDYH-FSLTELEKQKWEKSIE 292
Cdd:pfam02866  81 AKAGSATLSMAVAGARFIRAILRGEGGVLSVGVYEDgyygvPDDIYFSFPVVLGKDGVEKVLEiGPLNDFEREKMEKSAA 160

                  ...
gi 498450293  293 TIK 295
Cdd:pfam02866 161 ELK 163
Ldh_1_N pfam00056
lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic ...
2-143 5.29e-19

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: 81.50  E-value: 5.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293    2 KKAAIIGV-GHVGSTLAYTLITRNIVDELVLFDKKEGQLLSEYNDLFDGQVDRYNHVKLIDSNLSELADTDVLIFSAGdI 80
Cdd:pfam00056   1 VKVAVVGAaGGVGQSLAFLLANKGLADELVLYDIVKEKLEGVAMDLSHGSTFLLVPGIVGGGDYEDLKDADVVVITAG-V 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498450293   81 TIFEGNSdRFAELYLTKEIVEEWAPKIKESGFKGILVNITNPCDVVTQRLQELTGLPKERVFG 143
Cdd:pfam00056  80 PRKPGMT-RLDLLNVNAKIFKSIGPALAKYAPNAIVLVVSNPVDILTYVAWKASGFPPNRVFG 141
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
5-111 4.96e-03

Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; Aspartate-semialdehyde dehydrogenase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439906 [Multi-domain]  Cd Length: 333  Bit Score: 38.09  E-value: 4.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498450293   5 AIIGV-GHVGSTLAYTLITRNI-VDELVLF--DKKEGQLLSeyndlFDGQVdrynhVKLIDSNLSELADTDVLIFSAGDi 80
Cdd:COG0136    4 AVVGAtGAVGRVLLELLEERDFpVGELRLLasSRSAGKTVS-----FGGKE-----LTVEDATDFDFSGVDIALFSAGG- 72
                         90       100       110
                 ....*....|....*....|....*....|.
gi 498450293  81 tifegnsdrfaelyltkEIVEEWAPKIKESG 111
Cdd:COG0136   73 -----------------SVSKEYAPKAAAAG 86
MDH_chloroplast-like cd01338
Chloroplast-like malate dehydrogenases; MDH is one of the key enzymes in the citric acid cycle, ...
135-198 6.99e-03

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: 37.57  E-value: 6.99e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498450293 135 GLPKERvFGTGTTLDSARMKHAVSKKFNVHPSSVEGYVL-GEHGESQFVAWSSVRIGGIPIAEML 198
Cdd:cd01338  144 DIPPDN-FTAMTRLDHNRAKSQLAKKAGVPVTDVKNMVIwGNHSPTQYPDFTNATIGGKPAAEVI 207
 
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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