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Conserved domains on  [gi|872679093|ref|WP_048542893|]
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fumarylacetoacetate hydrolase family protein [Bacillus wiedmannii]

Protein Classification

fumarylacetoacetate hydrolase family protein( domain architecture ID 10480489)

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
FAA_hydrolase pfam01557
Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) ...
80-298 2.08e-80

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: 242.96  E-value: 2.08e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093   80 IRDFYAFEQHVKTARGRrglEVVPEWYDIPVFYFTNHRAVIGPDDFVIGPKKSKKLDYELEIACVIGKEGRNISREQAEE 159
Cdd:pfam01557   1 VCVGLNYAEHAREAGKA---EPVPDFPIPLVLFVKPPSSLIGPGDPIVRPAGVTKLDYEAELAVVIGRPARDVSPEEALD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093  160 YIFGYCIMNDWSARDLQATEMKVGLGPAKGKDFATSLGAHLVTKEELdvyrnGDRYELEMTAHVNGKLLSKGNFQDIYYT 239
Cdd:pfam01557  78 YIFGYTLANDVSARDLQRREMPLQWFRGKSFDGFTPLGPWIVTRDEL-----PDPGDLRLRLRVNGEVRQDGNTSDMIFS 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 872679093  240 FAEMIERASEDVTLYPGDVIGSGTVGtGCVLELGTEEWLQDGDVVELTITGLGTLRNTV 298
Cdd:pfam01557 153 PAELIAHLSQFMTLRPGDIILTGTPS-GVGAGRAPPVFLKPGDTVEVEIEGLGTLRNTV 210
 
Name Accession Description Interval E-value
FAA_hydrolase pfam01557
Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) ...
80-298 2.08e-80

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: 242.96  E-value: 2.08e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093   80 IRDFYAFEQHVKTARGRrglEVVPEWYDIPVFYFTNHRAVIGPDDFVIGPKKSKKLDYELEIACVIGKEGRNISREQAEE 159
Cdd:pfam01557   1 VCVGLNYAEHAREAGKA---EPVPDFPIPLVLFVKPPSSLIGPGDPIVRPAGVTKLDYEAELAVVIGRPARDVSPEEALD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093  160 YIFGYCIMNDWSARDLQATEMKVGLGPAKGKDFATSLGAHLVTKEELdvyrnGDRYELEMTAHVNGKLLSKGNFQDIYYT 239
Cdd:pfam01557  78 YIFGYTLANDVSARDLQRREMPLQWFRGKSFDGFTPLGPWIVTRDEL-----PDPGDLRLRLRVNGEVRQDGNTSDMIFS 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 872679093  240 FAEMIERASEDVTLYPGDVIGSGTVGtGCVLELGTEEWLQDGDVVELTITGLGTLRNTV 298
Cdd:pfam01557 153 PAELIAHLSQFMTLRPGDIILTGTPS-GVGAGRAPPVFLKPGDTVEVEIEGLGTLRNTV 210
YcgM COG0179
2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) ...
102-299 3.16e-56

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: 181.03  E-value: 3.16e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093 102 VPEWydiPVFYFTNHRAVIGPDDFVIGPKKSKKLDYELEIACVIGKEGRNISREQAEEYIFGYCIMNDWSARDLQateMK 181
Cdd:COG0179   26 VPEE---PVLFLKPPSALVGPGDPIPLPAGSGKLDYEGELAVVIGKRARNVSEEDALDHVAGYTVANDVTARDLQ---RE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093 182 VGLGPAKGKDFATS--LGAHLVTKEELdvyrnGDRYELEMTAHVNGKLLSKGNFQDIYYTFAEMIERASEDVTLYPGDVI 259
Cdd:COG0179  100 RGGQWTRGKSFDTFcpLGPWIVTADEI-----PDPQDLRIRLRVNGEVRQDGNTSDMIFSVAELIAYLSQFMTLEPGDVI 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 872679093 260 GSGT---VGTgcvlelgteewLQDGDVVELTITGLGTLRNTVK 299
Cdd:COG0179  175 LTGTpagVGP-----------LKPGDVVEVEIEGIGTLRNTVV 206
PLN02856 PLN02856
fumarylacetoacetase
51-287 1.41e-35

fumarylacetoacetase


Pssm-ID: 215461 [Multi-domain]  Cd Length: 424  Bit Score: 132.89  E-value: 1.41e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093  51 VLR-NMENPEKGIYSLEEVQ--LAAAIPNPSsirDFYAFEQHVKTArGR--RGLE--VVPEWYDIPVFYFTNHRAVI--- 120
Cdd:PLN02856 101 ALRdNSELRKKAFHPMSDVEmlLPAVIGDYT---DFFSSREHATNV-GTmfRGPEnaLNPNWLHLPIGYHGRASSVVpsg 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093 121 --------------GPDDFVIGPkkSKKLDYELEIACVIG---KEGRNISREQAEEYIFGYCIMNDWSARDLQATEMkVG 183
Cdd:PLN02856 177 tdirrprgqlhpndGSSRPYFGP--SAKLDFELEMAAFVGpgnELGKPIPVNEAKDHIFGLVLMNDWSARDIQKWEY-VP 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093 184 LGPAKGKDFATSLGAHLVTKEELDVYR-----------------NGDRYELEMTAHV------NGKLLSKGNFQDIYYTF 240
Cdd:PLN02856 254 LGPFLGKSFATTISPWIVTLDALEPFRcdapaqdppplpylaekNRKSYDISLEVAIkpagqsKASVVCRSNFKHLYWTL 333
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872679093 241 AEMIerASEDVT---LYPGDVIGSGTVG------TGCVLEL-------------GTEEWLQDGDVVELT 287
Cdd:PLN02856 334 AQQL--AHHTVNgcnLRPGDLLGSGTISgpepgsLGCLLELtwagsrevsleggTRRKFLEDGDEVVLS 400
HpaG-C-term TIGR02303
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit; ...
109-301 3.95e-32

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: 119.92  E-value: 3.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093  109 PVFYFTNHRAVIGPDDFVIGPKKSKKLDYELEIACVIGKEGRNISREQAEEYIFGYCIMNDWSARDLQATEMKVGLgPAK 188
Cdd:TIGR02303  67 PLVFLKGNNTLTGHKGVTYRPKDVRFMHYECELAVVVGKTAKNVKREDAMDYVLGYTIANDYAIRDYLENYYRPNL-RVK 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093  189 GKDFATSLGAHLVTKEELDvyrngDRYELEMTAHVNGKLLSKGNFQDIYYTFAEMIERASEDVTLYPGDVIGSGTvgtgc 268
Cdd:TIGR02303 146 NRDTFTPIGPWIVDKEDVE-----DPMNLWLRTYVNGELTQEGNTSDMIFSVAELIEYLSEFMTLEPGDVILTGT----- 215
                         170       180       190
                  ....*....|....*....|....*....|...
gi 872679093  269 vlELGTEEwLQDGDVVELTITGLGTLRNTVKKE 301
Cdd:TIGR02303 216 --PKGLSD-VKPGDVVRLEIEGVGALENPIVSE 245
 
Name Accession Description Interval E-value
FAA_hydrolase pfam01557
Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) ...
80-298 2.08e-80

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: 242.96  E-value: 2.08e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093   80 IRDFYAFEQHVKTARGRrglEVVPEWYDIPVFYFTNHRAVIGPDDFVIGPKKSKKLDYELEIACVIGKEGRNISREQAEE 159
Cdd:pfam01557   1 VCVGLNYAEHAREAGKA---EPVPDFPIPLVLFVKPPSSLIGPGDPIVRPAGVTKLDYEAELAVVIGRPARDVSPEEALD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093  160 YIFGYCIMNDWSARDLQATEMKVGLGPAKGKDFATSLGAHLVTKEELdvyrnGDRYELEMTAHVNGKLLSKGNFQDIYYT 239
Cdd:pfam01557  78 YIFGYTLANDVSARDLQRREMPLQWFRGKSFDGFTPLGPWIVTRDEL-----PDPGDLRLRLRVNGEVRQDGNTSDMIFS 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 872679093  240 FAEMIERASEDVTLYPGDVIGSGTVGtGCVLELGTEEWLQDGDVVELTITGLGTLRNTV 298
Cdd:pfam01557 153 PAELIAHLSQFMTLRPGDIILTGTPS-GVGAGRAPPVFLKPGDTVEVEIEGLGTLRNTV 210
YcgM COG0179
2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) ...
102-299 3.16e-56

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: 181.03  E-value: 3.16e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093 102 VPEWydiPVFYFTNHRAVIGPDDFVIGPKKSKKLDYELEIACVIGKEGRNISREQAEEYIFGYCIMNDWSARDLQateMK 181
Cdd:COG0179   26 VPEE---PVLFLKPPSALVGPGDPIPLPAGSGKLDYEGELAVVIGKRARNVSEEDALDHVAGYTVANDVTARDLQ---RE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093 182 VGLGPAKGKDFATS--LGAHLVTKEELdvyrnGDRYELEMTAHVNGKLLSKGNFQDIYYTFAEMIERASEDVTLYPGDVI 259
Cdd:COG0179  100 RGGQWTRGKSFDTFcpLGPWIVTADEI-----PDPQDLRIRLRVNGEVRQDGNTSDMIFSVAELIAYLSQFMTLEPGDVI 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 872679093 260 GSGT---VGTgcvlelgteewLQDGDVVELTITGLGTLRNTVK 299
Cdd:COG0179  175 LTGTpagVGP-----------LKPGDVVEVEIEGIGTLRNTVV 206
PLN02856 PLN02856
fumarylacetoacetase
51-287 1.41e-35

fumarylacetoacetase


Pssm-ID: 215461 [Multi-domain]  Cd Length: 424  Bit Score: 132.89  E-value: 1.41e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093  51 VLR-NMENPEKGIYSLEEVQ--LAAAIPNPSsirDFYAFEQHVKTArGR--RGLE--VVPEWYDIPVFYFTNHRAVI--- 120
Cdd:PLN02856 101 ALRdNSELRKKAFHPMSDVEmlLPAVIGDYT---DFFSSREHATNV-GTmfRGPEnaLNPNWLHLPIGYHGRASSVVpsg 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093 121 --------------GPDDFVIGPkkSKKLDYELEIACVIG---KEGRNISREQAEEYIFGYCIMNDWSARDLQATEMkVG 183
Cdd:PLN02856 177 tdirrprgqlhpndGSSRPYFGP--SAKLDFELEMAAFVGpgnELGKPIPVNEAKDHIFGLVLMNDWSARDIQKWEY-VP 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093 184 LGPAKGKDFATSLGAHLVTKEELDVYR-----------------NGDRYELEMTAHV------NGKLLSKGNFQDIYYTF 240
Cdd:PLN02856 254 LGPFLGKSFATTISPWIVTLDALEPFRcdapaqdppplpylaekNRKSYDISLEVAIkpagqsKASVVCRSNFKHLYWTL 333
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872679093 241 AEMIerASEDVT---LYPGDVIGSGTVG------TGCVLEL-------------GTEEWLQDGDVVELT 287
Cdd:PLN02856 334 AQQL--AHHTVNgcnLRPGDLLGSGTISgpepgsLGCLLELtwagsrevsleggTRRKFLEDGDEVVLS 400
HpaG-C-term TIGR02303
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit; ...
109-301 3.95e-32

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: 119.92  E-value: 3.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093  109 PVFYFTNHRAVIGPDDFVIGPKKSKKLDYELEIACVIGKEGRNISREQAEEYIFGYCIMNDWSARDLQATEMKVGLgPAK 188
Cdd:TIGR02303  67 PLVFLKGNNTLTGHKGVTYRPKDVRFMHYECELAVVVGKTAKNVKREDAMDYVLGYTIANDYAIRDYLENYYRPNL-RVK 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093  189 GKDFATSLGAHLVTKEELDvyrngDRYELEMTAHVNGKLLSKGNFQDIYYTFAEMIERASEDVTLYPGDVIGSGTvgtgc 268
Cdd:TIGR02303 146 NRDTFTPIGPWIVDKEDVE-----DPMNLWLRTYVNGELTQEGNTSDMIFSVAELIEYLSEFMTLEPGDVILTGT----- 215
                         170       180       190
                  ....*....|....*....|....*....|...
gi 872679093  269 vlELGTEEwLQDGDVVELTITGLGTLRNTVKKE 301
Cdd:TIGR02303 216 --PKGLSD-VKPGDVVRLEIEGVGALENPIVSE 245
fum_ac_acetase TIGR01266
fumarylacetoacetase; This enzyme catalyzes the final step in the breakdown of tyrosine or ...
82-298 2.12e-29

fumarylacetoacetase; This enzyme catalyzes the final step in the breakdown of tyrosine or phenylalanine to fumarate and acetoacetate. [Energy metabolism, Amino acids and amines]


Pssm-ID: 162276 [Multi-domain]  Cd Length: 415  Bit Score: 116.10  E-value: 2.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093   82 DFYAFEQHVkTARGR--RGLE--VVPEWYDIPVFYFTNHRAVI----------------GPDDFVIGPkkSKKLDYELEI 141
Cdd:TIGR01266 125 DFYSSIQHA-TNVGImfRGKEnaLLPNWKHLPVGYHGRASSIVvsgtplrrpmgqtlpdNAKPPVFGP--CKLLDMELEM 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093  142 ACVIGKE---GRNISREQAEEYIFGYCIMNDWSARDLQATEMkVGLGPAKGKDFATSLGAHLVTKEELDVYR----NGD- 213
Cdd:TIGR01266 202 AFFVGPGnrlGEPIPISKAEEHIFGVVLMNDWSARDIQAWEY-VPLGPFLAKSFGTTISPWVVPIDALEPFRvpnpKQDp 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093  214 ------------RYELEMTAHVNGK------LLSKGNFQDIYYTFAEMIerASEDVT---LYPGDVIGSGTVGT------ 266
Cdd:TIGR01266 281 kplpylchdapyTFDINLEVSLKGEgmsepaTICRSNFKHMYWTMLQQL--AHHSVNgcnLRPGDLLGSGTISGsepgsf 358
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 872679093  267 GCVLEL---GTEE----------WLQDGDVVELT--------ITGLGTLRNTV 298
Cdd:TIGR01266 359 GSMLELswkGKKPidvaqgetrtFLEDGDEVILRghcqgegyRVGFGECAGKV 411
PRK15203 PRK15203
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional
109-304 3.97e-20

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional


Pssm-ID: 185125 [Multi-domain]  Cd Length: 429  Bit Score: 90.11  E-value: 3.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093 109 PVFYFTNHRAVIGPDDFVIGPKKSKKLDYELEIACVIGKEGRNISREQAEEYIFGYCIMNDWSARDLQATEMKVGLgPAK 188
Cdd:PRK15203 247 PLVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELVVVIGKQARKVSEADAMDYVAGYTVCNDYAIRDYLENYYRPNL-RVK 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093 189 GKDFATSLGAHLVTKEELDvyrngDRYELEMTAHVNGKLLSKGNFQDIYYTFAEMIERASEDVTLYPGDVIGSgtvgtgc 268
Cdd:PRK15203 326 SRDGLTPILSTIVPKEAIP-----DPHNLTLRTFVNGELRQQGTTADLIFSVPFLIAYLSEFMTLNPGDMIAT------- 393
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 872679093 269 vlelGTEEWLQD---GDVVELTITGLGTLRNTVKKEMEA 304
Cdd:PRK15203 394 ----GTPKGLSDvvpGDEVVVEVEGVGRLVNRIVSEETA 428
PRK12764 PRK12764
fumarylacetoacetate hydrolase family protein;
129-299 2.07e-17

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 237193 [Multi-domain]  Cd Length: 500  Bit Score: 82.50  E-value: 2.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093 129 PKKSKKLDYELEIACVIGKEGRNISREQAEEYIFGYCIMNDWSARDLQATEMKVGLgPAKGKDFATSLGAHLVTKEELDV 208
Cdd:PRK12764  65 PAGTELLAFEGEIALVIGRPARRVSPEDAWSHVAAVTAANDLGVYDLRYADKGSNL-RSKGGDGFTPIGPALISARGVDP 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093 209 YRngdryeLEMTAHVNGKLLSKGNFQDIYYTFAEMIERASEDVTLYPGDVIGSGTVGTGCVlelgteewLQDGDVVELTI 288
Cdd:PRK12764 144 AQ------LRVRTWVNGELVQDDTTEDLLFPFAQLVADLSQLLTLEEGDVILTGTPAGSSV--------AAPGDVVEVEV 209
                        170
                 ....*....|....*...
gi 872679093 289 TGL-------GTLRNTVK 299
Cdd:PRK12764 210 DAPadgapstGRLVTRVV 227
HpaG-N-term TIGR02305
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, N-terminal subunit; ...
109-298 9.03e-17

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: 77.47  E-value: 9.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093  109 PVFYFTNHRAVIGPDDFVIGPKKSKKLDYELEIACVIGKEGRNISREQAEEYIFGYCIMNDWSardLQATEMKVGLGPAK 188
Cdd:TIGR02305  33 PVLYIKPRNTHNGCGQPIPLPAGVEKLRSGATLALVVGRTACRVREEEALDYVAGYALVNDVS---LPEDSYYRPAIKAK 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093  189 GKDFATSLGAHLVTKEEldvyrnGDRYELEMTAHVNGKLLSKGNFQDIYYTFAEMIERASEDVTLYPGDVIGSGTVGTGC 268
Cdd:TIGR02305 110 CRDGFCPIGPEVPLSAI------GNPDELTIYTYINGKPAQSNNTSNLVRSAAQLISELSEFMTLNPGDVLLLGTPEARV 183
                         170       180       190
                  ....*....|....*....|....*....|
gi 872679093  269 VlelgteewLQDGDVVELTITGLGTLRNTV 298
Cdd:TIGR02305 184 E--------VGPGDRVRVEAEGLGELENPV 205
PRK10691 PRK10691
fumarylacetoacetate hydrolase family protein;
129-290 1.64e-10

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 182650  Cd Length: 219  Bit Score: 59.72  E-value: 1.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093 129 PKKSKKLDYELEIACVIGKEGRNISREQAEEYIFGYCIMNDWSARDLQATEMKVG--LGPAKGKDFATSLGAHLVTKEel 206
Cdd:PRK10691  61 PKDFGSVHHEVELAVLIGATLRQATEEHVRKAIAGYGVALDLTLRDLQGKMKKAGqpWEKAKAFDNSCPISGFIPVAE-- 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093 207 dvyRNGDRYELEMTAHVNGKLLSKGNFQDIYYTFAEMIERASEDVTLYPGDVIGSGT---VGTgcvlelgteewLQDGDV 283
Cdd:PRK10691 139 ---FTGDPQNTTLGLSVNGEVRQQGNTADMIHPIVPLIAYMSRFFTLRAGDVVLTGTpegVGP-----------LQSGDE 204

                 ....*..
gi 872679093 284 VELTITG 290
Cdd:PRK10691 205 LTVTFNG 211
PRK15203 PRK15203
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional
106-303 2.34e-08

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional


Pssm-ID: 185125 [Multi-domain]  Cd Length: 429  Bit Score: 55.06  E-value: 2.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093 106 YDIP----VFYFTNHRAVIGPDDFVIGPKKSKKLDyELEIACVIGKEGRNISREQAEEYIFGYCIMNDWSARDLQATEMK 181
Cdd:PRK15203  28 YKAPpktaVWFIKPRNTVIRCGEPIPFPQGEKVLS-GATVALIVGKTATKVREEDAAEYIAGYALANDVSLPEESFYRPA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872679093 182 VglgPAKGKDFATSLGaHLVTKEELDvyrngdryELEMTAHVNGKLLSKGNFQDIYYTFAEMIERASEDVTLYPGDVIGS 261
Cdd:PRK15203 107 I---KAKCRDGFCPIG-ETVALSNVD--------NLTIYTEINGRPADHWNTADLQRNAAQLLSALSEFATLNPGDAILL 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 872679093 262 GTVGTGCVlelgteewLQDGDVVELTITGLGTLRNTVKKEME 303
Cdd:PRK15203 175 GTPQARVE--------IQPGDRVRVLAEGFPPLENPVVDERE 208
 
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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