NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|103472015|ref|NP_060784|]
View 

ubiquitin-conjugating enzyme E2 variant 3 isoform b [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 180-361 2.47e-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: 281.80  E-value: 2.47e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 180 KTVNKITVVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLEIF----NLPNVEISKDLSASAHSKVVIFTVN 254
Cdd:cd05293    1 KPRNKVTVVGVGQVGMACAISILAKGLADELVLVDVVEDkLKGEAMDLQHGsaflKNPKIEADKDYSVTANSKVVIVTAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 255 SLGSSQSY-LDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNV 333
Cdd:cd05293   81 ARQNEGESrLDLVQRNVDIFKGIIPKLVKYSPNAILLVVSNPVDIMTYVAWKLSGLPKHRVIGSGCNLDSARFRYLIAER 160

                        170       180
                 ....*....|....*....|....*...
gi 103472015 334 LKAQTSGKEVWVIGEQGEDKVLTWSGQE 361
Cdd:cd05293  161 LGVAPSSVHGWIIGEHGDSSVPVWSGVN 188
UEV pfam05743
UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101) ...
 21-138 1.52e-65

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: 203.65  E-value: 1.52e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015   21 TVEELRNVNVFFPHFKYSMDTYVFKDSSQKDLLNFTGTIPVMYQGNTYNIPIRFWILDSHPFAPPICFLKPTANMGILVG 100
Cdd:pfam05743   1 TFKDLVNVLRKFPNLKPRTDVYTFNDGSSKLLLNLYGTIPVTYKGNTYNIPILIWLPDTYPFSPPICYVKPTASMVIKVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 103472015  101 KHVDAQGRIYLPYLQNWSHPKSVIVGLIKEMIAKFQEE 138
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 ...
 180-361 2.47e-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: 281.80  E-value: 2.47e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 180 KTVNKITVVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLEIF----NLPNVEISKDLSASAHSKVVIFTVN 254
Cdd:cd05293    1 KPRNKVTVVGVGQVGMACAISILAKGLADELVLVDVVEDkLKGEAMDLQHGsaflKNPKIEADKDYSVTANSKVVIVTAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 255 SLGSSQSY-LDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNV 333
Cdd:cd05293   81 ARQNEGESrLDLVQRNVDIFKGIIPKLVKYSPNAILLVVSNPVDIMTYVAWKLSGLPKHRVIGSGCNLDSARFRYLIAER 160

                        170       180
                 ....*....|....*....|....*...
gi 103472015 334 LKAQTSGKEVWVIGEQGEDKVLTWSGQE 361
Cdd:cd05293  161 LGVAPSSVHGWIIGEHGDSSVPVWSGVN 188
UEV pfam05743
UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101) ...
 21-138 1.52e-65

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: 203.65  E-value: 1.52e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015   21 TVEELRNVNVFFPHFKYSMDTYVFKDSSQKDLLNFTGTIPVMYQGNTYNIPIRFWILDSHPFAPPICFLKPTANMGILVG 100
Cdd:pfam05743   1 TFKDLVNVLRKFPNLKPRTDVYTFNDGSSKLLLNLYGTIPVTYKGNTYNIPILIWLPDTYPFSPPICYVKPTASMVIKVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 103472015  101 KHVDAQGRIYLPYLQNWSHPKSVIVGLIKEMIAKFQEE 138
Cdd:pfam05743  81 HHVDAQGRVYLPYLHNWNHPSSNLVDLVQELAQVFQED 118
UEV_TSG101-like cd11685
ubiquitin E2 variant (UEV) domain of TSG101 and related proteins; This subfamily includes the ...
 19-143 8.64e-55

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: 176.34  E-value: 8.64e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015  19 DLTVEELRNVNVFFPHFKYSMDTYVFKDSSQKDLLNFTGTIPVMYQGNTYNIPIRFWILDSHPFAPPICFLKPTANMGIL 98
Cdd:cd11685    1 DRVREDLLNLLQKYPSLKPKTDTFTFNDGSSKLLLCLTGTIPITYRGSTYNIPITIWLPETYPYSPPIVYVVPTPSMMII 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 103472015  99 -VGKHVDAQGRIYLPYLQNWSHPKSVIVGLIKEMIAKFQEELPMYS 143
Cdd:cd11685   81 kPHPHVDPNGRVYLPYLSEWNPPSSNLVDLVQELSAVFSEEPPVYS 126
PLN02602 PLN02602
lactate dehydrogenase
 161-358 6.13e-44

lactate dehydrogenase


Pssm-ID: 178212 [Multi-domain]  Cd Length: 350  Bit Score: 155.31  E-value: 6.13e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 161 KITEGVSDTNSKSWANHENKTVNKITVVGGGELGIACTLAISAKGIADRLVLLD-LSEGTKGATMDLE---IFnLPNVEI 236
Cdd:PLN02602  16 DLSQAFFKPIHNSSPPSPTRRHTKVSVVGVGNVGMAIAQTILTQDLADELALVDvNPDKLRGEMLDLQhaaAF-LPRTKI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 237 --SKDLSASAHSKVVIFTVNS-LGSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANR 313
Cdd:PLN02602  95 laSTDYAVTAGSDLCIVTAGArQIPGESRLNLLQRNVALFRKIIPELAKYSPDTILLIVSNPVDVLTYVAWKLSGFPANR 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 103472015 314 VIGIGCNLDSQRLQYIITNVLKAQTSGKEVWVIGEQGEDKVLTWS 358
Cdd:PLN02602 175 VIGSGTNLDSSRFRFLIADHLDVNAQDVQAYIVGEHGDSSVALWS 219
L-LDH-NAD TIGR01771
L-lactate dehydrogenase; This model represents the NAD-dependent L-lactate dehydrogenases from ...
 187-359 2.77e-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: 133.86  E-value: 2.77e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015  187 VVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLE---IFNLPNVEI-SKDLSASAHSKVVIFTVnslGSSQ- 260
Cdd:TIGR01771   1 IIGAGNVGSSTAFALLNQGIADEIVLIDINKDkAEGEAMDLQhaaSFLPTPKKIrSGDYSDCKDADLVVITA---GAPQk 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015  261 ---SYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNVLKAQ 337
Cdd:TIGR01771  78 pgeTRLELVGRNVRIMKSIVPEVVKSGFDGIFLVATNPVDILTYVAWKLSGFPKNRVIGSGTVLDTARLRYLLAEKLGVD 157

                         170       180
                  ....*....|....*....|..
gi 103472015  338 TSGKEVWVIGEQGEDKVLTWSG 359
Cdd:TIGR01771 158 PQSVHAYIIGEHGDSEVPVWSS 179
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ...
 183-358 4.85e-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: 130.52  E-value: 4.85e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 183 NKITVVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLE---IFNLPNVEI-SKDLSASAHSKVVIFTV-NSL 256
Cdd:COG0039    1 MKVAIIGAGNVGSTLAFRLASGGLADELVLIDINEGkAEGEALDLAdafPLLGFDVKItAGDYEDLADADVVVITAgAPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 257 GSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNVLKA 336
Cdd:COG0039   81 KPGMSRLDLLEANAKIFKSVGEAIKKYAPDAIVLVVTNPVDVMTYIAQKASGLPKERVIGMGTVLDSARFRSFLAEKLGV 160

                        170       180
                 ....*....|....*....|..
gi 103472015 337 QTSGKEVWVIGEQGEDKVLTWS 358
Cdd:COG0039  161 SPRDVHAYVLGEHGDSMVPLWS 182
Ldh_1_N pfam00056
lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic ...
 183-316 2.12e-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: 2.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015  183 NKITVVG-GGELGIACTLAISAKGIADRLVLLDL-SEGTKGATMDLE--IFNLPNVEI--SKDLSASAHSKVVIFT--VN 254
Cdd:pfam00056   1 VKVAVVGaAGGVGQSLAFLLANKGLADELVLYDIvKEKLEGVAMDLShgSTFLLVPGIvgGGDYEDLKDADVVVITagVP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 103472015  255 SlGSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIG 316
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 ...
 180-361 2.47e-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: 281.80  E-value: 2.47e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 180 KTVNKITVVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLEIF----NLPNVEISKDLSASAHSKVVIFTVN 254
Cdd:cd05293    1 KPRNKVTVVGVGQVGMACAISILAKGLADELVLVDVVEDkLKGEAMDLQHGsaflKNPKIEADKDYSVTANSKVVIVTAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 255 SLGSSQSY-LDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNV 333
Cdd:cd05293   81 ARQNEGESrLDLVQRNVDIFKGIIPKLVKYSPNAILLVVSNPVDIMTYVAWKLSGLPKHRVIGSGCNLDSARFRYLIAER 160

                        170       180
                 ....*....|....*....|....*...
gi 103472015 334 LKAQTSGKEVWVIGEQGEDKVLTWSGQE 361
Cdd:cd05293  161 LGVAPSSVHGWIIGEHGDSSVPVWSGVN 188
UEV pfam05743
UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101) ...
 21-138 1.52e-65

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: 203.65  E-value: 1.52e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015   21 TVEELRNVNVFFPHFKYSMDTYVFKDSSQKDLLNFTGTIPVMYQGNTYNIPIRFWILDSHPFAPPICFLKPTANMGILVG 100
Cdd:pfam05743   1 TFKDLVNVLRKFPNLKPRTDVYTFNDGSSKLLLNLYGTIPVTYKGNTYNIPILIWLPDTYPFSPPICYVKPTASMVIKVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 103472015  101 KHVDAQGRIYLPYLQNWSHPKSVIVGLIKEMIAKFQEE 138
Cdd:pfam05743  81 HHVDAQGRVYLPYLHNWNHPSSNLVDLVQELAQVFQED 118
UEV_TSG101-like cd11685
ubiquitin E2 variant (UEV) domain of TSG101 and related proteins; This subfamily includes the ...
 19-143 8.64e-55

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: 176.34  E-value: 8.64e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015  19 DLTVEELRNVNVFFPHFKYSMDTYVFKDSSQKDLLNFTGTIPVMYQGNTYNIPIRFWILDSHPFAPPICFLKPTANMGIL 98
Cdd:cd11685    1 DRVREDLLNLLQKYPSLKPKTDTFTFNDGSSKLLLCLTGTIPITYRGSTYNIPITIWLPETYPYSPPIVYVVPTPSMMII 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 103472015  99 -VGKHVDAQGRIYLPYLQNWSHPKSVIVGLIKEMIAKFQEELPMYS 143
Cdd:cd11685   81 kPHPHVDPNGRVYLPYLSEWNPPSSNLVDLVQELSAVFSEEPPVYS 126
PLN02602 PLN02602
lactate dehydrogenase
 161-358 6.13e-44

lactate dehydrogenase


Pssm-ID: 178212 [Multi-domain]  Cd Length: 350  Bit Score: 155.31  E-value: 6.13e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 161 KITEGVSDTNSKSWANHENKTVNKITVVGGGELGIACTLAISAKGIADRLVLLD-LSEGTKGATMDLE---IFnLPNVEI 236
Cdd:PLN02602  16 DLSQAFFKPIHNSSPPSPTRRHTKVSVVGVGNVGMAIAQTILTQDLADELALVDvNPDKLRGEMLDLQhaaAF-LPRTKI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 237 --SKDLSASAHSKVVIFTVNS-LGSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANR 313
Cdd:PLN02602  95 laSTDYAVTAGSDLCIVTAGArQIPGESRLNLLQRNVALFRKIIPELAKYSPDTILLIVSNPVDVLTYVAWKLSGFPANR 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 103472015 314 VIGIGCNLDSQRLQYIITNVLKAQTSGKEVWVIGEQGEDKVLTWS 358
Cdd:PLN02602 175 VIGSGTNLDSSRFRFLIADHLDVNAQDVQAYIVGEHGDSSVALWS 219
LDH_like cd00300
L-lactate dehydrogenase-like enzymes; Members of this subfamily are tetrameric NAD-dependent ...
 185-358 2.06e-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: 147.42  E-value: 2.06e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 185 ITVVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLE----IFNLPNVEISKDLSASAHSKVVIFTVnslGSS 259
Cdd:cd00300    1 ITIIGAGNVGAAVAFALIAKGLASELVLVDVNEEkAKGDALDLShasaFLATGTIVRGGDYADAADADIVVITA---GAP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 260 Q----SYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNVLK 335
Cdd:cd00300   78 RkpgeTRLDLINRNAPILRSVITNLKKYGPDAIILVVSNPVDILTYVAQKLSGLPKNRVIGSGTLLDSARFRSLLAEKLD 157

                        170       180
                 ....*....|....*....|...
gi 103472015 336 AQTSGKEVWVIGEQGEDKVLTWS 358
Cdd:cd00300  158 VDPQSVHAYVLGEHGDSQVVAWS 180
L-LDH-NAD TIGR01771
L-lactate dehydrogenase; This model represents the NAD-dependent L-lactate dehydrogenases from ...
 187-359 2.77e-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: 133.86  E-value: 2.77e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015  187 VVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLE---IFNLPNVEI-SKDLSASAHSKVVIFTVnslGSSQ- 260
Cdd:TIGR01771   1 IIGAGNVGSSTAFALLNQGIADEIVLIDINKDkAEGEAMDLQhaaSFLPTPKKIrSGDYSDCKDADLVVITA---GAPQk 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015  261 ---SYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNVLKAQ 337
Cdd:TIGR01771  78 pgeTRLELVGRNVRIMKSIVPEVVKSGFDGIFLVATNPVDILTYVAWKLSGFPKNRVIGSGTVLDTARLRYLLAEKLGVD 157

                         170       180
                  ....*....|....*....|..
gi 103472015  338 TSGKEVWVIGEQGEDKVLTWSG 359
Cdd:TIGR01771 158 PQSVHAYIIGEHGDSEVPVWSS 179
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ...
 183-358 4.85e-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: 130.52  E-value: 4.85e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 183 NKITVVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLE---IFNLPNVEI-SKDLSASAHSKVVIFTV-NSL 256
Cdd:COG0039    1 MKVAIIGAGNVGSTLAFRLASGGLADELVLIDINEGkAEGEALDLAdafPLLGFDVKItAGDYEDLADADVVVITAgAPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 257 GSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNVLKA 336
Cdd:COG0039   81 KPGMSRLDLLEANAKIFKSVGEAIKKYAPDAIVLVVTNPVDVMTYIAQKASGLPKERVIGMGTVLDSARFRSFLAEKLGV 160

                        170       180
                 ....*....|....*....|..
gi 103472015 337 QTSGKEVWVIGEQGEDKVLTWS 358
Cdd:COG0039  161 SPRDVHAYVLGEHGDSMVPLWS 182
LDH_2 cd05292
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
 183-358 8.56e-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: 127.22  E-value: 8.56e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 183 NKITVVGGGELGIACTLAISAKGIADRLVLLDLS-EGTKGATMDLE---IFNLPNVEISKDLSASAHSKVVIFTVnslGS 258
Cdd:cd05292    1 MKVAIVGAGFVGSTTAYALLLRGLASEIVLVDINkAKAEGEAMDLAhgtPFVKPVRIYAGDYADCKGADVVVITA---GA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 259 SQ----SYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNVL 334
Cdd:cd05292   78 NQkpgeTRLDLLKRNVAIFKEIIPQILKYAPDAILLVVTNPVDVLTYVAYKLSGLPPNRVIGSGTVLDTARFRYLLGEHL 157

                        170       180
                 ....*....|....*....|....
gi 103472015 335 KAQTSGKEVWVIGEQGEDKVLTWS 358
Cdd:cd05292  158 GVDPRSVHAYIIGEHGDSEVAVWS 181
ldh PRK00066
L-lactate dehydrogenase; Reviewed
 179-358 2.84e-31

L-lactate dehydrogenase; Reviewed


Pssm-ID: 178836 [Multi-domain]  Cd Length: 315  Bit Score: 120.77  E-value: 2.84e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 179 NKTVNKITVVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLE---IFNLPNVEISKDLSASAHSKVVIFTVn 254
Cdd:PRK00066   3 KKQHNKVVLVGDGAVGSSYAYALVNQGIADELVIIDINKEkAEGDAMDLShavPFTSPTKIYAGDYSDCKDADLVVITA- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 255 slGSSQ----SYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYII 330
Cdd:PRK00066  82 --GAPQkpgeTRLDLVEKNLKIFKSIVGEVMASGFDGIFLVASNPVDILTYATWKLSGFPKERVIGSGTSLDSARFRYML 159

                        170       180
                 ....*....|....*....|....*...
gi 103472015 331 TNVLKAQTSGKEVWVIGEQGEDKVLTWS 358
Cdd:PRK00066 160 SEKLDVDPRSVHAYIIGEHGDTEFPVWS 187
HicDH_like cd05291
L-2-hydroxyisocapronate dehydrogenases and some bacterial L-lactate dehydrogenases; ...
 183-358 6.01e-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: 6.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 183 NKITVVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLE--IFNLPN-VEISK-DLSASAHSKVVIFTV-NSL 256
Cdd:cd05291    1 RKVVIIGAGHVGSSFAYSLVNQGIADELVLIDINEEkAEGEALDLEdaLAFLPSpVKIKAgDYSDCKDADIVVITAgAPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 257 GSSQSYLDVVQSNVDMFRALVPAL------GhysqhsVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYII 330
Cdd:cd05291   81 KPGETRLDLLEKNAKIMKSIVPKIkasgfdG------IFLVASNPVDVITYVVQKLSGLPKNRVIGTGTSLDTARLRRAL 154

                        170       180
                 ....*....|....*....|....*...
gi 103472015 331 TNVLKAQTSGKEVWVIGEQGEDKVLTWS 358
Cdd:cd05291  155 AEKLNVDPRSVHAYVLGEHGDSQFVAWS 182
PRK06223 PRK06223
malate dehydrogenase; Reviewed
 183-354 5.51e-27

malate dehydrogenase; Reviewed


Pssm-ID: 180477 [Multi-domain]  Cd Length: 307  Bit Score: 108.68  E-value: 5.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 183 NKITVVGGGELGIACTLAISAKGIADrLVLLDLSEG-TKGATMDL------EIFNLpNVEISKDLSASAHSKVVIFTVns 255
Cdd:PRK06223   3 KKISIIGAGNVGATLAHLLALKELGD-VVLFDIVEGvPQGKALDIaeaapvEGFDT-KITGTNDYEDIAGSDVVVITA-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 256 lGSS----QSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYII- 330
Cdd:PRK06223  79 -GVPrkpgMSRDDLLGINAKIMKDVAEGIKKYAPDAIVIVVTNPVDAMTYVALKESGFPKNRVIGMAGVLDSARFRTFIa 157

                        170       180
                 ....*....|....*....|....*...
gi 103472015 331 --TNVlkaqtSGKEV--WVIGEQGEDKV 354
Cdd:PRK06223 158 eeLNV-----SVKDVtaFVLGGHGDSMV 180
Ldh_1_N pfam00056
lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic ...
 183-316 2.12e-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: 2.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015  183 NKITVVG-GGELGIACTLAISAKGIADRLVLLDL-SEGTKGATMDLE--IFNLPNVEI--SKDLSASAHSKVVIFT--VN 254
Cdd:pfam00056   1 VKVAVVGaAGGVGQSLAFLLANKGLADELVLYDIvKEKLEGVAMDLShgSTFLLVPGIvgGGDYEDLKDADVVVITagVP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 103472015  255 SlGSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIG 316
Cdd:pfam00056  81 R-KPGMTRLDLLNVNAKIFKSIGPALAKYAPNAIVLVVSNPVDILTYVAWKASGFPPNRVFG 141
LDH-like_MDH cd01339
L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an ...
 185-354 1.51e-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: 99.09  E-value: 1.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 185 ITVVGGGELGIACTLAISAKGIADrLVLLDLSEG-TKGATMDL------EIFNlPNVEISKDLSASAHSKVVIFTVnslG 257
Cdd:cd01339    1 ISIIGAGNVGATLAQLLALKELGD-VVLLDIVEGlPQGKALDIsqaapiLGSD-TKVTGTNDYEDIAGSDVVVITA---G 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 258 SS----QSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNV 333
Cdd:cd01339   76 IPrkpgMSRDDLLGTNAKIVKEVAENIKKYAPNAIVIVVTNPLDVMTYVAYKASGFPRNRVIGMAGVLDSARFRYFIAEE 155

                        170       180
                 ....*....|....*....|...
gi 103472015 334 LKAqtSGKEV--WVIGEQGEDKV 354
Cdd:cd01339  156 LGV--SVKDVqaMVLGGHGDTMV 176
LDH_MDH_like cd00650
NAD-dependent, lactate dehydrogenase-like, 2-hydroxycarboxylate dehydrogenase family; Members ...
 185-358 6.53e-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: 6.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 185 ITVVG-GGELGIACTLAISAKG--IADRLVLLDLSEG-TKGATMDLEIF----NLPNVEISKDL-SASAHSKVVIFTVNS 255
Cdd:cd00650    1 IAVIGaGGNVGPALAFGLADGSvlLAIELVLYDIDEEkLKGVAMDLQDAveplADIKVSITDDPyEAFKDADVVIITAGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 256 LG-SSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCnLDSQRLQYIITNVL 334
Cdd:cd00650   81 GRkPGMGRLDLLKRNVPIVKEIGDNIEKYSPDAWIIVVSNPVDIITYLVWRYSGLPKEKVIGLGT-LDPIRFRRILAEKL 159

                        170       180
                 ....*....|....*....|....
gi 103472015 335 KAQTSGKEVWVIGEQGEDKVLTWS 358
Cdd:cd00650  160 GVDPDDVKVYILGEHGGSQVPDWS 183
LDH_3 cd05290
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
 184-359 2.99e-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: 78.53  E-value: 2.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 184 KITVVGGGELGIACTLAISAKGIADRLVLLDLSEG-TKGATMDLE----IFNLPNVEI-SKDLSASAHSKVVIFTVN-SL 256
Cdd:cd05290    1 KLVVIGAGHVGSAVLNYALALGLFSEIVLIDVNEGvAEGEALDFHhataLTYSTNTKIrAGDYDDCADADIIVITAGpSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 257 --GSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYIITNvl 334
Cdd:cd05290   81 dpGNTDDRLDLAQTNAKIIREIMGNITKVTKEAVIILITNPLDIAVYIAATEFDYPANKVIGTGTMLDTARLRRIVAD-- 158

                        170       180
                 ....*....|....*....|....*..
gi 103472015 335 KAQTSGKEV--WVIGEQGEDKVLTWSG 359
Cdd:cd05290  159 KYGVDPKNVtgYVLGEHGSHAFPVWSL 185
LDH-like_MDH_nadp cd05294
A lactate dehydrogenases-like structure with malate dehydrogenase enzymatic activity; The ...
 184-354 1.60e-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: 73.59  E-value: 1.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 184 KITVVGG-GELGIACTLAISAKGIADRLVL--------------LDLSEGTKGATMDLEIfnlpnvEISKDLSASAHSKV 248
Cdd:cd05294    2 KVSIIGAsGRVGSATALLLAKEDVVKEINLisrpksleklkglrLDIYDALAAAGIDAEI------KISSDLSDVAGSDI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 249 VIFTVN-SLGSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQ 327
Cdd:cd05294   76 VIITAGvPRKEGMSRLDLAKKNAKIVKKYAKQIAEFAPDTKILVVTNPVDVMTYKALKESGFDKNRVFGLGTHLDSLRFK 155

                        170       180
                 ....*....|....*....|....*..
gi 103472015 328 YIITNVLKAQTSGKEVWVIGEQGEDKV 354
Cdd:cd05294  156 VAIAKHFNVHISEVHTRIIGEHGDSMV 182
PTZ00117 PTZ00117
malate dehydrogenase; Provisional
 184-354 3.46e-11

malate dehydrogenase; Provisional


Pssm-ID: 173409 [Multi-domain]  Cd Length: 319  Bit Score: 63.59  E-value: 3.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 184 KITVVGGGELGIACTLAISAKGIADrLVLLDLSEGT-KGATMDL-----------EIFNLPNVEISKDlsasahSKVVIF 251
Cdd:PTZ00117   7 KISMIGAGQIGSTVALLILQKNLGD-VVLYDVIKGVpQGKALDLkhfstlvgsniNILGTNNYEDIKD------SDVVVI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 252 TVN-SLGSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYII 330
Cdd:PTZ00117  80 TAGvQRKEEMTREDLLTINGKIMKSVAESVKKYCPNAFVICVTNPLDCMVKVFQEKSGIPSNKICGMAGVLDSSRFRCNL 159

                        170       180
                 ....*....|....*....|....
gi 103472015 331 TNVLKAQTSGKEVWVIGEQGEDKV 354
Cdd:PTZ00117 160 AEKLGVSPGDVSAVVIGGHGDLMV 183
PTZ00082 PTZ00082
L-lactate dehydrogenase; Provisional
 183-355 1.74e-10

L-lactate dehydrogenase; Provisional


Pssm-ID: 173376 [Multi-domain]  Cd Length: 321  Bit Score: 61.63  E-value: 1.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 183 NKITVVGGGELGIACTLAISAKGIADrLVLLDLSEGT-KGATMDLEIFNL-----PNVEISKDLSASAHSKVVIFTV--- 253
Cdd:PTZ00082   7 RKISLIGSGNIGGVMAYLIVLKNLGD-VVLFDIVKNIpQGKALDISHSNViagsnSKVIGTNNYEDIAGSDVVIVTAglt 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015 254 ---NSLGSSQSYLDVVQSNVDMFRALVPALGHYSQHSVLLVASQPVEIMTYVTWKLSTFPANRVIGIGCNLDSQRLQYII 330
Cdd:PTZ00082  86 krpGKSDKEWNRDDLLPLNAKIMDEVAEGIKKYCPNAFVIVITNPLDVMVKLLQEHSGLPKNKVCGMAGVLDSSRLRTYI 165

                        170       180
                 ....*....|....*....|....*
gi 103472015 331 TNVLKAQTSGKEVWVIGEQGEDKVL 355
Cdd:PTZ00082 166 AEKLGVNPRDVHASVIGAHGDKMVP 190
UQ_con pfam00179
Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ...
 51-128 3.44e-03

Ubiquitin-conjugating enzyme; Proteins destined for proteasome-mediated degradation may be ubiquitinated. Ubiquitination follows conjugation of ubiquitin to a conserved cysteine residue of UBC homologs. TSG101 is one of several UBC homologs that lacks this active site cysteine.


Pssm-ID: 459701 [Multi-domain]  Cd Length: 139  Bit Score: 37.56  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 103472015   51 DLLNFTGTIP----VMYQGNTYNIPIRFwiLDSHPFAPPIC-FLKPtanmgILvgkH--VDAQGRIYLPYL--QNWS--- 118
Cdd:pfam00179  25 NLFEWKVTIIgpdgTPYEGGVFKLSVEF--PEDYPFKPPKVkFTTK-----IY---HpnVDSSGEVCLDILkdERWSpal 94

                          90
                  ....*....|
gi 103472015  119 HPKSVIVGLI 128
Cdd:pfam00179  95 TLEQVLLSIQ 104
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH