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Conserved domains on  [gi|386869251|ref|NP_001248312|]
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ubiquitin-conjugating enzyme E2 variant 3 isoform d [Homo sapiens]

Protein Classification

ubiquitin-conjugating enzyme E2 variant 3( domain architecture ID 10530350)

ubiquitin-conjugating enzyme E2 variant 3 (UEV-3) may be a negative regulator of polyubiquitination

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 ...
 158-339 1.96e-93

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 cd05293:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 312  Bit Score: 281.42  E-value: 1.96e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 158 KTVNKITVVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLEIF----NLPNVEISKDLSASAHSKVVIFTVN 232
Cdd:cd05293    1 KPRNKVTVVGVGQVGMACAISILAKGLADELVLVDVVEDkLKGEAMDLQHGsaflKNPKIEADKDYSVTANSKVVIVTAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 233 SLGSSQSY-LDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNV 311
Cdd:cd05293   81 ARQNEGESrLDLVQRNVDIFKGIIPKLVKYSPNAILLVVSNPVDIMTYVAWKLSGLPKHRVIGSGCNLDSARFRYLIAER 160

                        170       180
                 ....*....|....*....|....*...
gi 386869251 312 LKAQTSGKEVWVIGEQGEDKVLTWSGQE 339
Cdd:cd05293  161 LGVAPSSVHGWIIGEHGDSSVPVWSGVN 188
UEV pfam05743
UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101) ...
 21-116 6.06e-47

UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101). Altered transcripts of this gene have been detected in sporadic breast cancers and many other human malignancies. However, the involvement of this gene in neoplastic transformation and tumorigenesis is still elusive. TSG101 is required for normal cell function of embryonic and adult tissues but that this gene is not a tumour suppressor for sporadic forms of breast cancer. This family is related to the ubiquitin conjugating enzymes.


:

Pssm-ID: 399041  Cd Length: 119  Bit Score: 155.50  E-value: 6.06e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251   21 TVEELRNVNVFFPHFKYSMDTY----------------------GNTYNIPIRFWILDSHPFAPPICFLKPTANMGILVG 78
Cdd:pfam05743   1 TFKDLVNVLRKFPNLKPRTDVYtfndgssklllnlygtipvtykGNTYNIPILIWLPDTYPFSPPICYVKPTASMVIKVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 386869251   79 KHVDAQGRIYLPYLQNWSHPKSVIVGLIKEMIAKFQEE 116
Cdd:pfam05743  81 HHVDAQGRVYLPYLHNWNHPSSNLVDLVQELAQVFQED 118
 
Name Accession Description Interval E-value
LDH_1 cd05293
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
 158-339 1.96e-93

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: 281.42  E-value: 1.96e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 158 KTVNKITVVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLEIF----NLPNVEISKDLSASAHSKVVIFTVN 232
Cdd:cd05293    1 KPRNKVTVVGVGQVGMACAISILAKGLADELVLVDVVEDkLKGEAMDLQHGsaflKNPKIEADKDYSVTANSKVVIVTAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 233 SLGSSQSY-LDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNV 311
Cdd:cd05293   81 ARQNEGESrLDLVQRNVDIFKGIIPKLVKYSPNAILLVVSNPVDIMTYVAWKLSGLPKHRVIGSGCNLDSARFRYLIAER 160

                        170       180
                 ....*....|....*....|....*...
gi 386869251 312 LKAQTSGKEVWVIGEQGEDKVLTWSGQE 339
Cdd:cd05293  161 LGVAPSSVHGWIIGEHGDSSVPVWSGVN 188
UEV pfam05743
UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101) ...
 21-116 6.06e-47

UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101). Altered transcripts of this gene have been detected in sporadic breast cancers and many other human malignancies. However, the involvement of this gene in neoplastic transformation and tumorigenesis is still elusive. TSG101 is required for normal cell function of embryonic and adult tissues but that this gene is not a tumour suppressor for sporadic forms of breast cancer. This family is related to the ubiquitin conjugating enzymes.


Pssm-ID: 399041  Cd Length: 119  Bit Score: 155.50  E-value: 6.06e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251   21 TVEELRNVNVFFPHFKYSMDTY----------------------GNTYNIPIRFWILDSHPFAPPICFLKPTANMGILVG 78
Cdd:pfam05743   1 TFKDLVNVLRKFPNLKPRTDVYtfndgssklllnlygtipvtykGNTYNIPILIWLPDTYPFSPPICYVKPTASMVIKVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 386869251   79 KHVDAQGRIYLPYLQNWSHPKSVIVGLIKEMIAKFQEE 116
Cdd:pfam05743  81 HHVDAQGRVYLPYLHNWNHPSSNLVDLVQELAQVFQED 118
PLN02602 PLN02602
lactate dehydrogenase
 139-336 4.12e-44

lactate dehydrogenase


Pssm-ID: 178212 [Multi-domain]  Cd Length: 350  Bit Score: 155.31  E-value: 4.12e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 139 KITEGVSDTNSKSWANHENKTVNKITVVGGGELGIACTLAISAKGIADRLVLLD-LSEGTKGATMDLE---IFnLPNVEI 214
Cdd:PLN02602  16 DLSQAFFKPIHNSSPPSPTRRHTKVSVVGVGNVGMAIAQTILTQDLADELALVDvNPDKLRGEMLDLQhaaAF-LPRTKI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 215 --SKDLSASAHSKVVIFTVNS-LGSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANR 291
Cdd:PLN02602  95 laSTDYAVTAGSDLCIVTAGArQIPGESRLNLLQRNVALFRKIIPELAKYSPDTILLIVSNPVDVLTYVAWKLSGFPANR 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 386869251 292 VIGIGCNLDSQRLQYIITNVLKAQTSGKEVWVIGEQGEDKVLTWS 336
Cdd:PLN02602 175 VIGSGTNLDSSRFRFLIADHLDVNAQDVQAYIVGEHGDSSVALWS 219
UEV_TSG101-like cd11685
ubiquitin E2 variant (UEV) domain of TSG101 and related proteins; This subfamily includes the ...
 19-121 2.61e-38

ubiquitin E2 variant (UEV) domain of TSG101 and related proteins; This subfamily includes the UEV domain of eukaryotic tumor susceptibility gene 101 protein (TSG101, also known as ESCRT-I complex subunit TSG101, vacuolar protein-sorting protein 23, or Vps23) which functions in endocytic trafficking. TSG101 is a component of the ESCRT (endosomal sorting complex required for transport)-I complex, one of four complexes (ESCRT 0, -I, -II, -III) in the vacuolar protein sorting pathway. TSG101 also facilitates HIV-1 virus budding from infected cells, perhaps by linking the p6 domain of the viral structural Gag protein to the vacuolar protein sorting machinery. The UEV domain of TSG101 binds to an essential tetrapeptide motif within the p6 domain of the structural Gag protein and also to ubiquitin. UEVs are homologous to E2 ubiquitin ligases but lack the conserved cysteine residue required for catalytic activity.


Pssm-ID: 467408  Cd Length: 126  Bit Score: 133.20  E-value: 2.61e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251  19 DLTVEELRNVNVFFPHFKYSMDTY----------------------GNTYNIPIRFWILDSHPFAPPICFLKPTANMGIL 76
Cdd:cd11685    1 DRVREDLLNLLQKYPSLKPKTDTFtfndgssklllcltgtipityrGSTYNIPITIWLPETYPYSPPIVYVVPTPSMMII 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 386869251  77 -VGKHVDAQGRIYLPYLQNWSHPKSVIVGLIKEMIAKFQEELPMYS 121
Cdd:cd11685   81 kPHPHVDPNGRVYLPYLSEWNPPSSNLVDLVQELSAVFSEEPPVYS 126
L-LDH-NAD TIGR01771
L-lactate dehydrogenase; This model represents the NAD-dependent L-lactate dehydrogenases from ...
 165-337 1.89e-36

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: 133.48  E-value: 1.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251  165 VVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLE---IFNLPNVEI-SKDLSASAHSKVVIFTVnslGSSQ- 238
Cdd:TIGR01771   1 IIGAGNVGSSTAFALLNQGIADEIVLIDINKDkAEGEAMDLQhaaSFLPTPKKIrSGDYSDCKDADLVVITA---GAPQk 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251  239 ---SYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNVLKAQ 315
Cdd:TIGR01771  78 pgeTRLELVGRNVRIMKSIVPEVVKSGFDGIFLVATNPVDILTYVAWKLSGFPKNRVIGSGTVLDTARLRYLLAEKLGVD 157

                         170       180
                  ....*....|....*....|..
gi 386869251  316 TSGKEVWVIGEQGEDKVLTWSG 337
Cdd:TIGR01771 158 PQSVHAYIIGEHGDSEVPVWSS 179
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ...
 161-336 4.43e-35

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: 130.14  E-value: 4.43e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 161 NKITVVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLE---IFNLPNVEI-SKDLSASAHSKVVIFTV-NSL 234
Cdd:COG0039    1 MKVAIIGAGNVGSTLAFRLASGGLADELVLIDINEGkAEGEALDLAdafPLLGFDVKItAGDYEDLADADVVVITAgAPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 235 GSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNVLKA 314
Cdd:COG0039   81 KPGMSRLDLLEANAKIFKSVGEAIKKYAPDAIVLVVTNPVDVMTYIAQKASGLPKERVIGMGTVLDSARFRSFLAEKLGV 160

                        170       180
                 ....*....|....*....|..
gi 386869251 315 QTSGKEVWVIGEQGEDKVLTWS 336
Cdd:COG0039  161 SPRDVHAYVLGEHGDSMVPLWS 182
Ldh_1_N pfam00056
lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic ...
 161-294 1.60e-25

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: 99.99  E-value: 1.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251  161 NKITVVG-GGELGIACTLAISAKGIADRLVLLDL-SEGTKGATMDLE--IFNLPNVEI--SKDLSASAHSKVVIFT--VN 232
Cdd:pfam00056   1 VKVAVVGaAGGVGQSLAFLLANKGLADELVLYDIvKEKLEGVAMDLShgSTFLLVPGIvgGGDYEDLKDADVVVITagVP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869251  233 SlGSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIG 294
Cdd:pfam00056  81 R-KPGMTRLDLLNVNAKIFKSIGPALAKYAPNAIVLVVSNPVDILTYVAWKASGFPPNRVFG 141
 
Name Accession Description Interval E-value
LDH_1 cd05293
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
 158-339 1.96e-93

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: 281.42  E-value: 1.96e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 158 KTVNKITVVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLEIF----NLPNVEISKDLSASAHSKVVIFTVN 232
Cdd:cd05293    1 KPRNKVTVVGVGQVGMACAISILAKGLADELVLVDVVEDkLKGEAMDLQHGsaflKNPKIEADKDYSVTANSKVVIVTAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 233 SLGSSQSY-LDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNV 311
Cdd:cd05293   81 ARQNEGESrLDLVQRNVDIFKGIIPKLVKYSPNAILLVVSNPVDIMTYVAWKLSGLPKHRVIGSGCNLDSARFRYLIAER 160

                        170       180
                 ....*....|....*....|....*...
gi 386869251 312 LKAQTSGKEVWVIGEQGEDKVLTWSGQE 339
Cdd:cd05293  161 LGVAPSSVHGWIIGEHGDSSVPVWSGVN 188
UEV pfam05743
UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101) ...
 21-116 6.06e-47

UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101). Altered transcripts of this gene have been detected in sporadic breast cancers and many other human malignancies. However, the involvement of this gene in neoplastic transformation and tumorigenesis is still elusive. TSG101 is required for normal cell function of embryonic and adult tissues but that this gene is not a tumour suppressor for sporadic forms of breast cancer. This family is related to the ubiquitin conjugating enzymes.


Pssm-ID: 399041  Cd Length: 119  Bit Score: 155.50  E-value: 6.06e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251   21 TVEELRNVNVFFPHFKYSMDTY----------------------GNTYNIPIRFWILDSHPFAPPICFLKPTANMGILVG 78
Cdd:pfam05743   1 TFKDLVNVLRKFPNLKPRTDVYtfndgssklllnlygtipvtykGNTYNIPILIWLPDTYPFSPPICYVKPTASMVIKVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 386869251   79 KHVDAQGRIYLPYLQNWSHPKSVIVGLIKEMIAKFQEE 116
Cdd:pfam05743  81 HHVDAQGRVYLPYLHNWNHPSSNLVDLVQELAQVFQED 118
PLN02602 PLN02602
lactate dehydrogenase
 139-336 4.12e-44

lactate dehydrogenase


Pssm-ID: 178212 [Multi-domain]  Cd Length: 350  Bit Score: 155.31  E-value: 4.12e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 139 KITEGVSDTNSKSWANHENKTVNKITVVGGGELGIACTLAISAKGIADRLVLLD-LSEGTKGATMDLE---IFnLPNVEI 214
Cdd:PLN02602  16 DLSQAFFKPIHNSSPPSPTRRHTKVSVVGVGNVGMAIAQTILTQDLADELALVDvNPDKLRGEMLDLQhaaAF-LPRTKI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 215 --SKDLSASAHSKVVIFTVNS-LGSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANR 291
Cdd:PLN02602  95 laSTDYAVTAGSDLCIVTAGArQIPGESRLNLLQRNVALFRKIIPELAKYSPDTILLIVSNPVDVLTYVAWKLSGFPANR 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 386869251 292 VIGIGCNLDSQRLQYIITNVLKAQTSGKEVWVIGEQGEDKVLTWS 336
Cdd:PLN02602 175 VIGSGTNLDSSRFRFLIADHLDVNAQDVQAYIVGEHGDSSVALWS 219
LDH_like cd00300
L-lactate dehydrogenase-like enzymes; Members of this subfamily are tetrameric NAD-dependent ...
 163-336 1.77e-41

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: 147.03  E-value: 1.77e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 163 ITVVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLE----IFNLPNVEISKDLSASAHSKVVIFTVnslGSS 237
Cdd:cd00300    1 ITIIGAGNVGAAVAFALIAKGLASELVLVDVNEEkAKGDALDLShasaFLATGTIVRGGDYADAADADIVVITA---GAP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 238 Q----SYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNVLK 313
Cdd:cd00300   78 RkpgeTRLDLINRNAPILRSVITNLKKYGPDAIILVVSNPVDILTYVAQKLSGLPKNRVIGSGTLLDSARFRSLLAEKLD 157

                        170       180
                 ....*....|....*....|...
gi 386869251 314 AQTSGKEVWVIGEQGEDKVLTWS 336
Cdd:cd00300  158 VDPQSVHAYVLGEHGDSQVVAWS 180
UEV_TSG101-like cd11685
ubiquitin E2 variant (UEV) domain of TSG101 and related proteins; This subfamily includes the ...
 19-121 2.61e-38

ubiquitin E2 variant (UEV) domain of TSG101 and related proteins; This subfamily includes the UEV domain of eukaryotic tumor susceptibility gene 101 protein (TSG101, also known as ESCRT-I complex subunit TSG101, vacuolar protein-sorting protein 23, or Vps23) which functions in endocytic trafficking. TSG101 is a component of the ESCRT (endosomal sorting complex required for transport)-I complex, one of four complexes (ESCRT 0, -I, -II, -III) in the vacuolar protein sorting pathway. TSG101 also facilitates HIV-1 virus budding from infected cells, perhaps by linking the p6 domain of the viral structural Gag protein to the vacuolar protein sorting machinery. The UEV domain of TSG101 binds to an essential tetrapeptide motif within the p6 domain of the structural Gag protein and also to ubiquitin. UEVs are homologous to E2 ubiquitin ligases but lack the conserved cysteine residue required for catalytic activity.


Pssm-ID: 467408  Cd Length: 126  Bit Score: 133.20  E-value: 2.61e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251  19 DLTVEELRNVNVFFPHFKYSMDTY----------------------GNTYNIPIRFWILDSHPFAPPICFLKPTANMGIL 76
Cdd:cd11685    1 DRVREDLLNLLQKYPSLKPKTDTFtfndgssklllcltgtipityrGSTYNIPITIWLPETYPYSPPIVYVVPTPSMMII 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 386869251  77 -VGKHVDAQGRIYLPYLQNWSHPKSVIVGLIKEMIAKFQEELPMYS 121
Cdd:cd11685   81 kPHPHVDPNGRVYLPYLSEWNPPSSNLVDLVQELSAVFSEEPPVYS 126
L-LDH-NAD TIGR01771
L-lactate dehydrogenase; This model represents the NAD-dependent L-lactate dehydrogenases from ...
 165-337 1.89e-36

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: 133.48  E-value: 1.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251  165 VVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLE---IFNLPNVEI-SKDLSASAHSKVVIFTVnslGSSQ- 238
Cdd:TIGR01771   1 IIGAGNVGSSTAFALLNQGIADEIVLIDINKDkAEGEAMDLQhaaSFLPTPKKIrSGDYSDCKDADLVVITA---GAPQk 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251  239 ---SYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNVLKAQ 315
Cdd:TIGR01771  78 pgeTRLELVGRNVRIMKSIVPEVVKSGFDGIFLVATNPVDILTYVAWKLSGFPKNRVIGSGTVLDTARLRYLLAEKLGVD 157

                         170       180
                  ....*....|....*....|..
gi 386869251  316 TSGKEVWVIGEQGEDKVLTWSG 337
Cdd:TIGR01771 158 PQSVHAYIIGEHGDSEVPVWSS 179
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ...
 161-336 4.43e-35

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: 130.14  E-value: 4.43e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 161 NKITVVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLE---IFNLPNVEI-SKDLSASAHSKVVIFTV-NSL 234
Cdd:COG0039    1 MKVAIIGAGNVGSTLAFRLASGGLADELVLIDINEGkAEGEALDLAdafPLLGFDVKItAGDYEDLADADVVVITAgAPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 235 GSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNVLKA 314
Cdd:COG0039   81 KPGMSRLDLLEANAKIFKSVGEAIKKYAPDAIVLVVTNPVDVMTYIAQKASGLPKERVIGMGTVLDSARFRSFLAEKLGV 160

                        170       180
                 ....*....|....*....|..
gi 386869251 315 QTSGKEVWVIGEQGEDKVLTWS 336
Cdd:COG0039  161 SPRDVHAYVLGEHGDSMVPLWS 182
LDH_2 cd05292
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
 161-336 8.68e-34

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: 126.84  E-value: 8.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 161 NKITVVGGGELGIACTLAISAKGIADRLVLLDLS-EGTKGATMDLE---IFNLPNVEISKDLSASAHSKVVIFTVnslGS 236
Cdd:cd05292    1 MKVAIVGAGFVGSTTAYALLLRGLASEIVLVDINkAKAEGEAMDLAhgtPFVKPVRIYAGDYADCKGADVVVITA---GA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 237 SQ----SYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNVL 312
Cdd:cd05292   78 NQkpgeTRLDLLKRNVAIFKEIIPQILKYAPDAILLVVTNPVDVLTYVAYKLSGLPPNRVIGSGTVLDTARFRYLLGEHL 157

                        170       180
                 ....*....|....*....|....
gi 386869251 313 KAQTSGKEVWVIGEQGEDKVLTWS 336
Cdd:cd05292  158 GVDPRSVHAYIIGEHGDSEVAVWS 181
ldh PRK00066
L-lactate dehydrogenase; Reviewed
 157-336 2.02e-31

L-lactate dehydrogenase; Reviewed


Pssm-ID: 178836 [Multi-domain]  Cd Length: 315  Bit Score: 120.38  E-value: 2.02e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 157 NKTVNKITVVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLE---IFNLPNVEISKDLSASAHSKVVIFTVn 232
Cdd:PRK00066   3 KKQHNKVVLVGDGAVGSSYAYALVNQGIADELVIIDINKEkAEGDAMDLShavPFTSPTKIYAGDYSDCKDADLVVITA- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 233 slGSSQ----SYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYII 308
Cdd:PRK00066  82 --GAPQkpgeTRLDLVEKNLKIFKSIVGEVMASGFDGIFLVASNPVDILTYATWKLSGFPKERVIGSGTSLDSARFRYML 159

                        170       180
                 ....*....|....*....|....*...
gi 386869251 309 TNVLKAQTSGKEVWVIGEQGEDKVLTWS 336
Cdd:PRK00066 160 SEKLDVDPRSVHAYIIGEHGDTEFPVWS 187
HicDH_like cd05291
L-2-hydroxyisocapronate dehydrogenases and some bacterial L-lactate dehydrogenases; ...
 161-336 4.73e-28

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


Pssm-ID: 133427 [Multi-domain]  Cd Length: 306  Bit Score: 111.41  E-value: 4.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 161 NKITVVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLE--IFNLPN-VEISK-DLSASAHSKVVIFTV-NSL 234
Cdd:cd05291    1 RKVVIIGAGHVGSSFAYSLVNQGIADELVLIDINEEkAEGEALDLEdaLAFLPSpVKIKAgDYSDCKDADIVVITAgAPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 235 GSSQSYLDVVQSNVDMFRALVPAL------GhysqhsVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYII 308
Cdd:cd05291   81 KPGETRLDLLEKNAKIMKSIVPKIkasgfdG------IFLVASNPVDVITYVVQKLSGLPKNRVIGTGTSLDTARLRRAL 154

                        170       180
                 ....*....|....*....|....*...
gi 386869251 309 TNVLKAQTSGKEVWVIGEQGEDKVLTWS 336
Cdd:cd05291  155 AEKLNVDPRSVHAYVLGEHGDSQFVAWS 182
PRK06223 PRK06223
malate dehydrogenase; Reviewed
 161-332 4.25e-27

malate dehydrogenase; Reviewed


Pssm-ID: 180477 [Multi-domain]  Cd Length: 307  Bit Score: 108.68  E-value: 4.25e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 161 NKITVVGGGELGIACTLAISAKGIADrLVLLDLSEG-TKGATMDL------EIFNLpNVEISKDLSASAHSKVVIFTVns 233
Cdd:PRK06223   3 KKISIIGAGNVGATLAHLLALKELGD-VVLFDIVEGvPQGKALDIaeaapvEGFDT-KITGTNDYEDIAGSDVVVITA-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 234 lGSS----QSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYII- 308
Cdd:PRK06223  79 -GVPrkpgMSRDDLLGINAKIMKDVAEGIKKYAPDAIVIVVTNPVDAMTYVALKESGFPKNRVIGMAGVLDSARFRTFIa 157

                        170       180
                 ....*....|....*....|....*...
gi 386869251 309 --TNVlkaqtSGKEV--WVIGEQGEDKV 332
Cdd:PRK06223 158 eeLNV-----SVKDVtaFVLGGHGDSMV 180
Ldh_1_N pfam00056
lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic ...
 161-294 1.60e-25

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: 99.99  E-value: 1.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251  161 NKITVVG-GGELGIACTLAISAKGIADRLVLLDL-SEGTKGATMDLE--IFNLPNVEI--SKDLSASAHSKVVIFT--VN 232
Cdd:pfam00056   1 VKVAVVGaAGGVGQSLAFLLANKGLADELVLYDIvKEKLEGVAMDLShgSTFLLVPGIvgGGDYEDLKDADVVVITagVP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869251  233 SlGSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIG 294
Cdd:pfam00056  81 R-KPGMTRLDLLNVNAKIFKSIGPALAKYAPNAIVLVVSNPVDILTYVAWKASGFPPNRVFG 141
LDH-like_MDH cd01339
L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an ...
 163-332 1.35e-23

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: 98.70  E-value: 1.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 163 ITVVGGGELGIACTLAISAKGIADrLVLLDLSEG-TKGATMDL------EIFNlPNVEISKDLSASAHSKVVIFTVnslG 235
Cdd:cd01339    1 ISIIGAGNVGATLAQLLALKELGD-VVLLDIVEGlPQGKALDIsqaapiLGSD-TKVTGTNDYEDIAGSDVVVITA---G 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 236 SS----QSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNV 311
Cdd:cd01339   76 IPrkpgMSRDDLLGTNAKIVKEVAENIKKYAPNAIVIVVTNPLDVMTYVAYKASGFPRNRVIGMAGVLDSARFRYFIAEE 155

                        170       180
                 ....*....|....*....|...
gi 386869251 312 LKAqtSGKEV--WVIGEQGEDKV 332
Cdd:cd01339  156 LGV--SVKDVqaMVLGGHGDTMV 176
LDH_MDH_like cd00650
NAD-dependent, lactate dehydrogenase-like, 2-hydroxycarboxylate dehydrogenase family; Members ...
 163-336 6.26e-21

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: 90.84  E-value: 6.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 163 ITVVG-GGELGIACTLAISAKG--IADRLVLLDLSEG-TKGATMDLEIF----NLPNVEISKDL-SASAHSKVVIFTVNS 233
Cdd:cd00650    1 IAVIGaGGNVGPALAFGLADGSvlLAIELVLYDIDEEkLKGVAMDLQDAveplADIKVSITDDPyEAFKDADVVIITAGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 234 LG-SSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCnLDSQRLQYIITNVL 312
Cdd:cd00650   81 GRkPGMGRLDLLKRNVPIVKEIGDNIEKYSPDAWIIVVSNPVDIITYLVWRYSGLPKEKVIGLGT-LDPIRFRRILAEKL 159

                        170       180
                 ....*....|....*....|....
gi 386869251 313 KAQTSGKEVWVIGEQGEDKVLTWS 336
Cdd:cd00650  160 GVDPDDVKVYILGEHGGSQVPDWS 183
LDH_3 cd05290
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
 162-337 2.93e-16

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: 78.14  E-value: 2.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 162 KITVVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLE----IFNLPNVEI-SKDLSASAHSKVVIFTVN-SL 234
Cdd:cd05290    1 KLVVIGAGHVGSAVLNYALALGLFSEIVLIDVNEGvAEGEALDFHhataLTYSTNTKIrAGDYDDCADADIIVITAGpSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 235 --GSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNvl 312
Cdd:cd05290   81 dpGNTDDRLDLAQTNAKIIREIMGNITKVTKEAVIILITNPLDIAVYIAATEFDYPANKVIGTGTMLDTARLRRIVAD-- 158

                        170       180
                 ....*....|....*....|....*..
gi 386869251 313 KAQTSGKEV--WVIGEQGEDKVLTWSG 337
Cdd:cd05290  159 KYGVDPKNVtgYVLGEHGSHAFPVWSL 185
LDH-like_MDH_nadp cd05294
A lactate dehydrogenases-like structure with malate dehydrogenase enzymatic activity; The ...
 162-332 1.44e-14

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: 73.21  E-value: 1.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 162 KITVVGG-GELGIACTLAISAKGIADRLVL--------------LDLSEGTKGATMDLEIfnlpnvEISKDLSASAHSKV 226
Cdd:cd05294    2 KVSIIGAsGRVGSATALLLAKEDVVKEINLisrpksleklkglrLDIYDALAAAGIDAEI------KISSDLSDVAGSDI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 227 VIFTVN-SLGSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQ 305
Cdd:cd05294   76 VIITAGvPRKEGMSRLDLAKKNAKIVKKYAKQIAEFAPDTKILVVTNPVDVMTYKALKESGFDKNRVFGLGTHLDSLRFK 155

                        170       180
                 ....*....|....*....|....*..
gi 386869251 306 YIITNVLKAQTSGKEVWVIGEQGEDKV 332
Cdd:cd05294  156 VAIAKHFNVHISEVHTRIIGEHGDSMV 182
PTZ00117 PTZ00117
malate dehydrogenase; Provisional
 162-332 2.98e-11

malate dehydrogenase; Provisional


Pssm-ID: 173409 [Multi-domain]  Cd Length: 319  Bit Score: 63.59  E-value: 2.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 162 KITVVGGGELGIACTLAISAKGIADrLVLLDLSEGT-KGATMDL-----------EIFNLPNVEISKDlsasahSKVVIF 229
Cdd:PTZ00117   7 KISMIGAGQIGSTVALLILQKNLGD-VVLYDVIKGVpQGKALDLkhfstlvgsniNILGTNNYEDIKD------SDVVVI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 230 TVN-SLGSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYII 308
Cdd:PTZ00117  80 TAGvQRKEEMTREDLLTINGKIMKSVAESVKKYCPNAFVICVTNPLDCMVKVFQEKSGIPSNKICGMAGVLDSSRFRCNL 159

                        170       180
                 ....*....|....*....|....
gi 386869251 309 TNVLKAQTSGKEVWVIGEQGEDKV 332
Cdd:PTZ00117 160 AEKLGVSPGDVSAVVIGGHGDLMV 183
PTZ00082 PTZ00082
L-lactate dehydrogenase; Provisional
 161-333 1.54e-10

L-lactate dehydrogenase; Provisional


Pssm-ID: 173376 [Multi-domain]  Cd Length: 321  Bit Score: 61.63  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 161 NKITVVGGGELGIACTLAISAKGIADrLVLLDLSEGT-KGATMDLEIFNL-----PNVEISKDLSASAHSKVVIFTV--- 231
Cdd:PTZ00082   7 RKISLIGSGNIGGVMAYLIVLKNLGD-VVLFDIVKNIpQGKALDISHSNViagsnSKVIGTNNYEDIAGSDVVIVTAglt 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869251 232 ---NSLGSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYII 308
Cdd:PTZ00082  86 krpGKSDKEWNRDDLLPLNAKIMDEVAEGIKKYCPNAFVIVITNPLDVMVKLLQEHSGLPKNKVCGMAGVLDSSRLRTYI 165

                        170       180
                 ....*....|....*....|....*
gi 386869251 309 TNVLKAQTSGKEVWVIGEQGEDKVL 333
Cdd:PTZ00082 166 AEKLGVNPRDVHASVIGAHGDKMVP 190
 
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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