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Conserved domains on  [gi|568918221|ref|XP_006500154|]
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fumarylacetoacetate hydrolase domain-containing protein 2A isoform X2 [Mus musculus]

Protein Classification

fumarylacetoacetate hydrolase family protein( domain architecture ID 11415096)

fumarylacetoacetate (FAA) hydrolase family protein belongs to the FAA hydrolase family which includes a large variety of metabolic enzymes, including those with hydrolase functions involved in the breakdown of aromatic compounds, oxaloacetate decarboxylase, and enzymes associated with other catabolic pathways including decarboxylation of substrates other than oxaloacetate, hydration, isomerization and hydroxylation reactions

CATH:  2.30.30.370
Gene Ontology:  GO:0003824|GO:0016787
PubMed:  29487229
SCOP:  4002580

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YcgM COG0179
2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) ...
 1-152 1.82e-83

2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 439949  Cd Length: 206  Bit Score: 243.82  E-value: 1.82e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918221   1 MAVVIGKKGKHIKATDVMAHVAGFTVAHDVSARDWQMRNGKQWLLGKTFDTFCPLGPALVTKDTIADPHNLKICCRVNGE 80
Cdd:COG0179   62 LAVVIGKRARNVSEEDALDHVAGYTVANDVTARDLQRERGGQWTRGKSFDTFCPLGPWIVTADEIPDPQDLRIRLRVNGE 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568918221  81 VVQSSNTNQMVFKTEYLIAWVSQFVTLYPGDLLLTGTPPGVGMfrkppvfLKKGDEVQCEIEELGVIINKVV 152
Cdd:COG0179  142 VRQDGNTSDMIFSVAELIAYLSQFMTLEPGDVILTGTPAGVGP-------LKPGDVVEVEIEGIGTLRNTVV 206
 
Name Accession Description Interval E-value
YcgM COG0179
2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) ...
 1-152 1.82e-83

2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 439949  Cd Length: 206  Bit Score: 243.82  E-value: 1.82e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918221   1 MAVVIGKKGKHIKATDVMAHVAGFTVAHDVSARDWQMRNGKQWLLGKTFDTFCPLGPALVTKDTIADPHNLKICCRVNGE 80
Cdd:COG0179   62 LAVVIGKRARNVSEEDALDHVAGYTVANDVTARDLQRERGGQWTRGKSFDTFCPLGPWIVTADEIPDPQDLRIRLRVNGE 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568918221  81 VVQSSNTNQMVFKTEYLIAWVSQFVTLYPGDLLLTGTPPGVGMfrkppvfLKKGDEVQCEIEELGVIINKVV 152
Cdd:COG0179  142 VRQDGNTSDMIFSVAELIAYLSQFMTLEPGDVILTGTPAGVGP-------LKPGDVVEVEIEGIGTLRNTVV 206
FAA_hydrolase pfam01557
Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) ...
 1-151 2.65e-71

Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) hydrolase, or fumarylacetoacetate hydrolase (FAH) and it also includes HHDD isomerase/OPET decarboxylase from E. coli strain W. FAA is the last enzyme in the tyrosine catabolic pathway, it hydrolyses fumarylacetoacetate into fumarate and acetoacetate which then join the citric acid cycle. Mutations in FAA cause type I tyrosinemia in humans this is an inherited disorder mainly affecting the liver leading to liver cirrhosis, hepatocellular carcinoma, renal tubular damages and neurologic crises amongst other symptoms. The enzymatic defect causes the toxic accumulation of phenylalanine/tyrosine catabolites. The E. coli W enzyme HHDD isomerase/OPET decarboxylase contains two copies of this domain and functions in fourth and fifth steps of the homoprotocatechuate pathway; here it decarboxylates OPET to HHDD and isomerizes this to OHED. The final products of this pathway are pyruvic acid and succinic semialdehyde. This family also includes various hydratases and 4-oxalocrotonate decarboxylases which are involved in the bacterial meta-cleavage pathways for degradation of aromatic compounds. 2-hydroxypentadienoic acid hydratase encoded by mhpD in E. coli is involved in the phenylpropionic acid pathway of E. coli and catalyzes the conversion of 2-hydroxy pentadienoate to 4-hydroxy-2-keto-pentanoate and uses a Mn2+ co-factor. OHED hydratase encoded by hpcG in E. coli is involved in the homoprotocatechuic acid (HPC) catabolism. XylI in P. putida is a 4-Oxalocrotonate decarboxylase.


Pssm-ID: 460252  Cd Length: 210  Bit Score: 213.30  E-value: 2.65e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918221    1 MAVVIGKKGKHIKATDVMAHVAGFTVAHDVSARDWQMRNGK-QWLLGKTFDTFCPLGPALVTKDTIADPHNLKICCRVNG 79
Cdd:pfam01557  59 LAVVIGRPARDVSPEEALDYIFGYTLANDVSARDLQRREMPlQWFRGKSFDGFTPLGPWIVTRDELPDPGDLRLRLRVNG 138

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568918221   80 EVVQSSNTNQMVFKTEYLIAWVSQFVTLYPGDLLLTGTPPGVGMFRKPPVFLKKGDEVQCEIEELGVIINKV 151
Cdd:pfam01557 139 EVRQDGNTSDMIFSPAELIAHLSQFMTLRPGDIILTGTPSGVGAGRAPPVFLKPGDTVEVEIEGLGTLRNTV 210
HpaG-C-term TIGR02303
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit; ...
 1-152 1.09e-43

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit; This model represents one of two subunits/domains of the bifunctional isomerase/decarboxylase involved in 4-hydroxyphenylacetate degradation. In E. coli and some other species this enzyme is encoded by a single polypeptide containing both this domain and the closely related N-terminal domain (TIGR02305). In other species such as Pasteurella multocida these domains are found as two separate proteins (usually as tandem genes). Together, these domains carry out the decarboxylation of 5-oxopent-3-ene-1,2,5-tricarboxylic acid (OPET) to 2-hydroxy-2,4-diene-1,7-dioate (HHDD) and the subsequent isomerization to 2-oxohept-3-ene-1,7-dioate (OHED).


Pssm-ID: 131356 [Multi-domain]  Cd Length: 245  Bit Score: 144.18  E-value: 1.09e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918221    1 MAVVIGKKGKHIKATDVMAHVAGFTVAHDVSARDWQMRNGKQWLLGKTFDTFCPLGPALVTKDTIADPHNLKICCRVNGE 80
Cdd:TIGR02303  99 LAVVVGKTAKNVKREDAMDYVLGYTIANDYAIRDYLENYYRPNLRVKNRDTFTPIGPWIVDKEDVEDPMNLWLRTYVNGE 178

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568918221   81 VVQSSNTNQMVFKTEYLIAWVSQFVTLYPGDLLLTGTPPGVgmfrkppVFLKKGDEVQCEIEELGVIINKVV 152
Cdd:TIGR02303 179 LTQEGNTSDMIFSVAELIEYLSEFMTLEPGDVILTGTPKGL-------SDVKPGDVVRLEIEGVGALENPIV 243
PRK15203 PRK15203
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional
 1-152 2.34e-35

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional


Pssm-ID: 185125 [Multi-domain]  Cd Length: 429  Bit Score: 126.70  E-value: 2.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918221   1 MAVVIGKKGKHIKATDVMAHVAGFTVAHDVSARDWQMRNGKQWLLGKTFDTFCPLGPALVTKDTIADPHNLKICCRVNGE 80
Cdd:PRK15203 279 LVVVIGKQARKVSEADAMDYVAGYTVCNDYAIRDYLENYYRPNLRVKSRDGLTPILSTIVPKEAIPDPHNLTLRTFVNGE 358

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568918221  81 VVQSSNTNQMVFKTEYLIAWVSQFVTLYPGDLLLTGTPPGVGMfrkppvfLKKGDEVQCEIEELGVIINKVV 152
Cdd:PRK15203 359 LRQQGTTADLIFSVPFLIAYLSEFMTLNPGDMIATGTPKGLSD-------VVPGDEVVVEVEGVGRLVNRIV 423
 
Name Accession Description Interval E-value
YcgM COG0179
2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) ...
 1-152 1.82e-83

2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 439949  Cd Length: 206  Bit Score: 243.82  E-value: 1.82e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918221   1 MAVVIGKKGKHIKATDVMAHVAGFTVAHDVSARDWQMRNGKQWLLGKTFDTFCPLGPALVTKDTIADPHNLKICCRVNGE 80
Cdd:COG0179   62 LAVVIGKRARNVSEEDALDHVAGYTVANDVTARDLQRERGGQWTRGKSFDTFCPLGPWIVTADEIPDPQDLRIRLRVNGE 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568918221  81 VVQSSNTNQMVFKTEYLIAWVSQFVTLYPGDLLLTGTPPGVGMfrkppvfLKKGDEVQCEIEELGVIINKVV 152
Cdd:COG0179  142 VRQDGNTSDMIFSVAELIAYLSQFMTLEPGDVILTGTPAGVGP-------LKPGDVVEVEIEGIGTLRNTVV 206
FAA_hydrolase pfam01557
Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) ...
 1-151 2.65e-71

Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) hydrolase, or fumarylacetoacetate hydrolase (FAH) and it also includes HHDD isomerase/OPET decarboxylase from E. coli strain W. FAA is the last enzyme in the tyrosine catabolic pathway, it hydrolyses fumarylacetoacetate into fumarate and acetoacetate which then join the citric acid cycle. Mutations in FAA cause type I tyrosinemia in humans this is an inherited disorder mainly affecting the liver leading to liver cirrhosis, hepatocellular carcinoma, renal tubular damages and neurologic crises amongst other symptoms. The enzymatic defect causes the toxic accumulation of phenylalanine/tyrosine catabolites. The E. coli W enzyme HHDD isomerase/OPET decarboxylase contains two copies of this domain and functions in fourth and fifth steps of the homoprotocatechuate pathway; here it decarboxylates OPET to HHDD and isomerizes this to OHED. The final products of this pathway are pyruvic acid and succinic semialdehyde. This family also includes various hydratases and 4-oxalocrotonate decarboxylases which are involved in the bacterial meta-cleavage pathways for degradation of aromatic compounds. 2-hydroxypentadienoic acid hydratase encoded by mhpD in E. coli is involved in the phenylpropionic acid pathway of E. coli and catalyzes the conversion of 2-hydroxy pentadienoate to 4-hydroxy-2-keto-pentanoate and uses a Mn2+ co-factor. OHED hydratase encoded by hpcG in E. coli is involved in the homoprotocatechuic acid (HPC) catabolism. XylI in P. putida is a 4-Oxalocrotonate decarboxylase.


Pssm-ID: 460252  Cd Length: 210  Bit Score: 213.30  E-value: 2.65e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918221    1 MAVVIGKKGKHIKATDVMAHVAGFTVAHDVSARDWQMRNGK-QWLLGKTFDTFCPLGPALVTKDTIADPHNLKICCRVNG 79
Cdd:pfam01557  59 LAVVIGRPARDVSPEEALDYIFGYTLANDVSARDLQRREMPlQWFRGKSFDGFTPLGPWIVTRDELPDPGDLRLRLRVNG 138

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568918221   80 EVVQSSNTNQMVFKTEYLIAWVSQFVTLYPGDLLLTGTPPGVGMFRKPPVFLKKGDEVQCEIEELGVIINKV 151
Cdd:pfam01557 139 EVRQDGNTSDMIFSPAELIAHLSQFMTLRPGDIILTGTPSGVGAGRAPPVFLKPGDTVEVEIEGLGTLRNTV 210
HpaG-C-term TIGR02303
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit; ...
 1-152 1.09e-43

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit; This model represents one of two subunits/domains of the bifunctional isomerase/decarboxylase involved in 4-hydroxyphenylacetate degradation. In E. coli and some other species this enzyme is encoded by a single polypeptide containing both this domain and the closely related N-terminal domain (TIGR02305). In other species such as Pasteurella multocida these domains are found as two separate proteins (usually as tandem genes). Together, these domains carry out the decarboxylation of 5-oxopent-3-ene-1,2,5-tricarboxylic acid (OPET) to 2-hydroxy-2,4-diene-1,7-dioate (HHDD) and the subsequent isomerization to 2-oxohept-3-ene-1,7-dioate (OHED).


Pssm-ID: 131356 [Multi-domain]  Cd Length: 245  Bit Score: 144.18  E-value: 1.09e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918221    1 MAVVIGKKGKHIKATDVMAHVAGFTVAHDVSARDWQMRNGKQWLLGKTFDTFCPLGPALVTKDTIADPHNLKICCRVNGE 80
Cdd:TIGR02303  99 LAVVVGKTAKNVKREDAMDYVLGYTIANDYAIRDYLENYYRPNLRVKNRDTFTPIGPWIVDKEDVEDPMNLWLRTYVNGE 178

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568918221   81 VVQSSNTNQMVFKTEYLIAWVSQFVTLYPGDLLLTGTPPGVgmfrkppVFLKKGDEVQCEIEELGVIINKVV 152
Cdd:TIGR02303 179 LTQEGNTSDMIFSVAELIEYLSEFMTLEPGDVILTGTPKGL-------SDVKPGDVVRLEIEGVGALENPIV 243
PRK15203 PRK15203
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional
 1-152 2.34e-35

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional


Pssm-ID: 185125 [Multi-domain]  Cd Length: 429  Bit Score: 126.70  E-value: 2.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918221   1 MAVVIGKKGKHIKATDVMAHVAGFTVAHDVSARDWQMRNGKQWLLGKTFDTFCPLGPALVTKDTIADPHNLKICCRVNGE 80
Cdd:PRK15203 279 LVVVIGKQARKVSEADAMDYVAGYTVCNDYAIRDYLENYYRPNLRVKSRDGLTPILSTIVPKEAIPDPHNLTLRTFVNGE 358

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568918221  81 VVQSSNTNQMVFKTEYLIAWVSQFVTLYPGDLLLTGTPPGVGMfrkppvfLKKGDEVQCEIEELGVIINKVV 152
Cdd:PRK15203 359 LRQQGTTADLIFSVPFLIAYLSEFMTLNPGDMIATGTPKGLSD-------VVPGDEVVVEVEGVGRLVNRIV 423
HpaG-N-term TIGR02305
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, N-terminal subunit; ...
 1-151 1.02e-34

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, N-terminal subunit; This model represents one of two subunits/domains of the bifunctional isomerase/decarboxylase involved in 4-hydroxyphenylacetate degradation. In E. coli and some other species this enzyme is encoded by a single polypeptide containing both this domain and the closely related C-terminal domain (TIGR02303). In other species such as Pasteurella multocida these domains are found as two separate proteins (usually as tandem genes). Together, these domains carry out the decarboxylation of 5-oxopent-3-ene-1,2,5-tricarboxylic acid (OPET) to 2-hydroxy-2,4-diene-1,7-dioate (HHDD) and the subsequent isomerization to 2-oxohept-3-ene-1,7-dioate (OHED).


Pssm-ID: 131358  Cd Length: 205  Bit Score: 119.84  E-value: 1.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918221    1 MAVVIGKKGKHIKATDVMAHVAGFTVAHDVS-ARDWQMRNGKQwllGKTFDTFCPLGPAlVTKDTIADPHNLKICCRVNG 79
Cdd:TIGR02305  65 LALVVGRTACRVREEEALDYVAGYALVNDVSlPEDSYYRPAIK---AKCRDGFCPIGPE-VPLSAIGNPDELTIYTYING 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568918221   80 EVVQSSNTNQMVFKTEYLIAWVSQFVTLYPGDLLLTGTPPGvgmfrkpPVFLKKGDEVQCEIEELGVIINKV 151
Cdd:TIGR02305 141 KPAQSNNTSNLVRSAAQLISELSEFMTLNPGDVLLLGTPEA-------RVEVGPGDRVRVEAEGLGELENPV 205
PRK10691 PRK10691
fumarylacetoacetate hydrolase family protein;
1-146 4.03e-27

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 182650  Cd Length: 219  Bit Score: 100.55  E-value: 4.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918221   1 MAVVIGKKGKHIKATDVMAHVAGFTVAHDVSARDWQ---MRNGKQWLLGKTFDTFCPLGPALVTKDTIADPHNLKICCRV 77
Cdd:PRK10691  73 LAVLIGATLRQATEEHVRKAIAGYGVALDLTLRDLQgkmKKAGQPWEKAKAFDNSCPISGFIPVAEFTGDPQNTTLGLSV 152

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568918221  78 NGEVVQSSNTNQMVFKTEYLIAWVSQFVTLYPGDLLLTGTPPGVGmfrkPpvfLKKGDEVQCEIEELGV 146
Cdd:PRK10691 153 NGEVRQQGNTADMIHPIVPLIAYMSRFFTLRAGDVVLTGTPEGVG----P---LQSGDELTVTFNGHSL 214
PRK12764 PRK12764
fumarylacetoacetate hydrolase family protein;
1-142 3.07e-25

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 237193 [Multi-domain]  Cd Length: 500  Bit Score: 99.83  E-value: 3.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918221   1 MAVVIGKKGKHIKATDVMAHVAGFTVAHDVSARDWQMRNGKQWLLGKTFDTFCPLGPALVTKDTIaDPHNLKICCRVNGE 80
Cdd:PRK12764  77 IALVIGRPARRVSPEDAWSHVAAVTAANDLGVYDLRYADKGSNLRSKGGDGFTPIGPALISARGV-DPAQLRVRTWVNGE 155

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568918221  81 VVQSSNTNQMVFKTEYLIAWVSQFVTLYPGDLLLTGTPPGVGMfrkppvfLKKGDEVQCEIE 142
Cdd:PRK12764 156 LVQDDTTEDLLFPFAQLVADLSQLLTLEEGDVILTGTPAGSSV-------AAPGDVVEVEVD 210
PRK15203 PRK15203
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional
 1-152 2.35e-15

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional


Pssm-ID: 185125 [Multi-domain]  Cd Length: 429  Bit Score: 71.62  E-value: 2.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918221   1 MAVVIGKKGKHIKATDVMAHVAGFTVAHDVSARDWQMRngKQWLLGKTFDTFCPLGPALvtkdTIADPHNLKICCRVNGE 80
Cdd:PRK15203  66 VALIVGKTATKVREEDAAEYIAGYALANDVSLPEESFY--RPAIKAKCRDGFCPIGETV----ALSNVDNLTIYTEINGR 139

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568918221  81 VVQSSNTNQMVFKTEYLIAWVSQFVTLYPGDLLLTGTPpgvgmfrKPPVFLKKGDEVQCEIEELGVIINKVV 152
Cdd:PRK15203 140 PADHWNTADLQRNAAQLLSALSEFATLNPGDAILLGTP-------QARVEIQPGDRVRVLAEGFPPLENPVV 204
MhpD COG3971
2-keto-4-pentenoate hydratase [Secondary metabolites biosynthesis, transport and catabolism];
55-147 9.81e-04

2-keto-4-pentenoate hydratase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443171  Cd Length: 259  Bit Score: 37.80  E-value: 9.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918221  55 LGPALVTKDTIaDPHNLKICCRVNGEVVQSSNT--------NQMVFkteyLIAWVSQF-VTLYPGDLLLTGTppgVGmfr 125
Cdd:COG3971  165 LGPPPVDPDDL-DLRNVGVVLEKNGEVVATGAGaavlghplNAVAW----LANKLAARgIPLKAGDIVLTGS---LT--- 233

                         90       100
                 ....*....|....*....|..
gi 568918221 126 kPPVFLKKGDEVQCEIEELGVI 147
Cdd:COG3971  234 -PAVPVKPGDTVRADFGGLGSV 254
 
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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