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Conserved domains on  [gi|446596677|ref|WP_000674023|]
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MULTISPECIES: fumarylacetoacetate hydrolase family protein [Bacillus]

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 1.89e-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: 1.89e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677   80 IRDFYAFEQHVKTARGRRgldVVPEWYDIPVFYFTNHRAVIGPNDVVIGPKKSEKLDYELEIACVIGKEGRNISREQAEE 159
Cdd:pfam01557   1 VCVGLNYAEHAREAGKAE---PVPDFPIPLVLFVKPPSSLIGPGDPIVRPAGVTKLDYEAELAVVIGRPARDVSPEEALD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677  160 YIFGYCIMNDWSARDLQATEMKVGLGPAKGKDFATSLGAHLVTKEELdvyrnGDRYELEMTAHVNGKLLSKGNFQDIYYT 239
Cdd:pfam01557  78 YIFGYTLANDVSARDLQRREMPLQWFRGKSFDGFTPLGPWIVTRDEL-----PDPGDLRLRLRVNGEVRQDGNTSDMIFS 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446596677  240 FAEMIERASEDVTLYPGDVIGSGTVGtGCILELGTEEWLQDGDVVELTITGLGTLRNTV 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 1.89e-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: 1.89e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677   80 IRDFYAFEQHVKTARGRRgldVVPEWYDIPVFYFTNHRAVIGPNDVVIGPKKSEKLDYELEIACVIGKEGRNISREQAEE 159
Cdd:pfam01557   1 VCVGLNYAEHAREAGKAE---PVPDFPIPLVLFVKPPSSLIGPGDPIVRPAGVTKLDYEAELAVVIGRPARDVSPEEALD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677  160 YIFGYCIMNDWSARDLQATEMKVGLGPAKGKDFATSLGAHLVTKEELdvyrnGDRYELEMTAHVNGKLLSKGNFQDIYYT 239
Cdd:pfam01557  78 YIFGYTLANDVSARDLQRREMPLQWFRGKSFDGFTPLGPWIVTRDEL-----PDPGDLRLRLRVNGEVRQDGNTSDMIFS 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446596677  240 FAEMIERASEDVTLYPGDVIGSGTVGtGCILELGTEEWLQDGDVVELTITGLGTLRNTV 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 2.97e-57

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: 183.73  E-value: 2.97e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677 102 VPEWydiPVFYFTNHRAVIGPNDVVIGPKKSEKLDYELEIACVIGKEGRNISREQAEEYIFGYCIMNDWSARDLQateMK 181
Cdd:COG0179   26 VPEE---PVLFLKPPSALVGPGDPIPLPAGSGKLDYEGELAVVIGKRARNVSEEDALDHVAGYTVANDVTARDLQ---RE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677 182 VGLGPAKGKDFATS--LGAHLVTKEELdvyrnGDRYELEMTAHVNGKLLSKGNFQDIYYTFAEMIERASEDVTLYPGDVI 259
Cdd:COG0179  100 RGGQWTRGKSFDTFcpLGPWIVTADEI-----PDPQDLRIRLRVNGEVRQDGNTSDMIFSVAELIAYLSQFMTLEPGDVI 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446596677 260 GSGT---VGTgcilelgteewLQDGDVVELTITGLGTLRNTVK 299
Cdd:COG0179  175 LTGTpagVGP-----------LKPGDVVEVEIEGIGTLRNTVV 206
PLN02856 PLN02856
fumarylacetoacetase
59-287 3.45e-36

fumarylacetoacetase


Pssm-ID: 215461 [Multi-domain]  Cd Length: 424  Bit Score: 134.82  E-value: 3.45e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677  59 EKGIYSLEEVQ--LAAAIPNPSsirDFYAFEQHVKTArGR--RGLD--VVPEWYDIPVFYftnH-RA---VIGPNDV--- 125
Cdd:PLN02856 110 KKAFHPMSDVEmlLPAVIGDYT---DFFSSREHATNV-GTmfRGPEnaLNPNWLHLPIGY---HgRAssvVPSGTDIrrp 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677 126 -------------VIGPkkSEKLDYELEIACVIG---KEGRNISREQAEEYIFGYCIMNDWSARDLQATEMkVGLGPAKG 189
Cdd:PLN02856 183 rgqlhpndgssrpYFGP--SAKLDFELEMAAFVGpgnELGKPIPVNEAKDHIFGLVLMNDWSARDIQKWEY-VPLGPFLG 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677 190 KDFATSLGAHLVTKEELDVYR-----------------NGDRYELEMTAHV------NGKLLSKGNFQDIYYTFAEMIer 246
Cdd:PLN02856 260 KSFATTISPWIVTLDALEPFRcdapaqdppplpylaekNRKSYDISLEVAIkpagqsKASVVCRSNFKHLYWTLAQQL-- 337
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446596677 247 ASEDVT---LYPGDVIGSGTVG------TGCILEL-------------GTEEWLQDGDVVELT 287
Cdd:PLN02856 338 AHHTVNgcnLRPGDLLGSGTISgpepgsLGCLLELtwagsrevsleggTRRKFLEDGDEVVLS 400
HpaG-C-term TIGR02303
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit; ...
109-301 7.84e-34

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: 124.15  E-value: 7.84e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677  109 PVFYFTNHRAVIGPNDVVIGPKKSEKLDYELEIACVIGKEGRNISREQAEEYIFGYCIMNDWSARDLQATEMKVGLgPAK 188
Cdd:TIGR02303  67 PLVFLKGNNTLTGHKGVTYRPKDVRFMHYECELAVVVGKTAKNVKREDAMDYVLGYTIANDYAIRDYLENYYRPNL-RVK 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677  189 GKDFATSLGAHLVTKEELDvyrngDRYELEMTAHVNGKLLSKGNFQDIYYTFAEMIERASEDVTLYPGDVIGSGTvgtgc 268
Cdd:TIGR02303 146 NRDTFTPIGPWIVDKEDVE-----DPMNLWLRTYVNGELTQEGNTSDMIFSVAELIEYLSEFMTLEPGDVILTGT----- 215
                         170       180       190
                  ....*....|....*....|....*....|...
gi 446596677  269 ilELGTEEwLQDGDVVELTITGLGTLRNTVKKE 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 1.89e-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: 1.89e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677   80 IRDFYAFEQHVKTARGRRgldVVPEWYDIPVFYFTNHRAVIGPNDVVIGPKKSEKLDYELEIACVIGKEGRNISREQAEE 159
Cdd:pfam01557   1 VCVGLNYAEHAREAGKAE---PVPDFPIPLVLFVKPPSSLIGPGDPIVRPAGVTKLDYEAELAVVIGRPARDVSPEEALD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677  160 YIFGYCIMNDWSARDLQATEMKVGLGPAKGKDFATSLGAHLVTKEELdvyrnGDRYELEMTAHVNGKLLSKGNFQDIYYT 239
Cdd:pfam01557  78 YIFGYTLANDVSARDLQRREMPLQWFRGKSFDGFTPLGPWIVTRDEL-----PDPGDLRLRLRVNGEVRQDGNTSDMIFS 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446596677  240 FAEMIERASEDVTLYPGDVIGSGTVGtGCILELGTEEWLQDGDVVELTITGLGTLRNTV 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 2.97e-57

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: 183.73  E-value: 2.97e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677 102 VPEWydiPVFYFTNHRAVIGPNDVVIGPKKSEKLDYELEIACVIGKEGRNISREQAEEYIFGYCIMNDWSARDLQateMK 181
Cdd:COG0179   26 VPEE---PVLFLKPPSALVGPGDPIPLPAGSGKLDYEGELAVVIGKRARNVSEEDALDHVAGYTVANDVTARDLQ---RE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677 182 VGLGPAKGKDFATS--LGAHLVTKEELdvyrnGDRYELEMTAHVNGKLLSKGNFQDIYYTFAEMIERASEDVTLYPGDVI 259
Cdd:COG0179  100 RGGQWTRGKSFDTFcpLGPWIVTADEI-----PDPQDLRIRLRVNGEVRQDGNTSDMIFSVAELIAYLSQFMTLEPGDVI 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446596677 260 GSGT---VGTgcilelgteewLQDGDVVELTITGLGTLRNTVK 299
Cdd:COG0179  175 LTGTpagVGP-----------LKPGDVVEVEIEGIGTLRNTVV 206
PLN02856 PLN02856
fumarylacetoacetase
59-287 3.45e-36

fumarylacetoacetase


Pssm-ID: 215461 [Multi-domain]  Cd Length: 424  Bit Score: 134.82  E-value: 3.45e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677  59 EKGIYSLEEVQ--LAAAIPNPSsirDFYAFEQHVKTArGR--RGLD--VVPEWYDIPVFYftnH-RA---VIGPNDV--- 125
Cdd:PLN02856 110 KKAFHPMSDVEmlLPAVIGDYT---DFFSSREHATNV-GTmfRGPEnaLNPNWLHLPIGY---HgRAssvVPSGTDIrrp 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677 126 -------------VIGPkkSEKLDYELEIACVIG---KEGRNISREQAEEYIFGYCIMNDWSARDLQATEMkVGLGPAKG 189
Cdd:PLN02856 183 rgqlhpndgssrpYFGP--SAKLDFELEMAAFVGpgnELGKPIPVNEAKDHIFGLVLMNDWSARDIQKWEY-VPLGPFLG 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677 190 KDFATSLGAHLVTKEELDVYR-----------------NGDRYELEMTAHV------NGKLLSKGNFQDIYYTFAEMIer 246
Cdd:PLN02856 260 KSFATTISPWIVTLDALEPFRcdapaqdppplpylaekNRKSYDISLEVAIkpagqsKASVVCRSNFKHLYWTLAQQL-- 337
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446596677 247 ASEDVT---LYPGDVIGSGTVG------TGCILEL-------------GTEEWLQDGDVVELT 287
Cdd:PLN02856 338 AHHTVNgcnLRPGDLLGSGTISgpepgsLGCLLELtwagsrevsleggTRRKFLEDGDEVVLS 400
HpaG-C-term TIGR02303
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit; ...
109-301 7.84e-34

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: 124.15  E-value: 7.84e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677  109 PVFYFTNHRAVIGPNDVVIGPKKSEKLDYELEIACVIGKEGRNISREQAEEYIFGYCIMNDWSARDLQATEMKVGLgPAK 188
Cdd:TIGR02303  67 PLVFLKGNNTLTGHKGVTYRPKDVRFMHYECELAVVVGKTAKNVKREDAMDYVLGYTIANDYAIRDYLENYYRPNL-RVK 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677  189 GKDFATSLGAHLVTKEELDvyrngDRYELEMTAHVNGKLLSKGNFQDIYYTFAEMIERASEDVTLYPGDVIGSGTvgtgc 268
Cdd:TIGR02303 146 NRDTFTPIGPWIVDKEDVE-----DPMNLWLRTYVNGELTQEGNTSDMIFSVAELIEYLSEFMTLEPGDVILTGT----- 215
                         170       180       190
                  ....*....|....*....|....*....|...
gi 446596677  269 ilELGTEEwLQDGDVVELTITGLGTLRNTVKKE 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 3.93e-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: 115.33  E-value: 3.93e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677   82 DFYAFEQHVkTARGR--RGLD--VVPEWYDIPVFYFTNHRAVI----------------GPNDVVIGPKKseKLDYELEI 141
Cdd:TIGR01266 125 DFYSSIQHA-TNVGImfRGKEnaLLPNWKHLPVGYHGRASSIVvsgtplrrpmgqtlpdNAKPPVFGPCK--LLDMELEM 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677  142 ACVIGKE---GRNISREQAEEYIFGYCIMNDWSARDLQATEMkVGLGPAKGKDFATSLGAHLVTKEELDVYR----NGD- 213
Cdd:TIGR01266 202 AFFVGPGnrlGEPIPISKAEEHIFGVVLMNDWSARDIQAWEY-VPLGPFLAKSFGTTISPWVVPIDALEPFRvpnpKQDp 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677  214 ------------RYELEMTAHVNGK------LLSKGNFQDIYYTFAEMIerASEDVT---LYPGDVIGSGTVGT------ 266
Cdd:TIGR01266 281 kplpylchdapyTFDINLEVSLKGEgmsepaTICRSNFKHMYWTMLQQL--AHHSVNgcnLRPGDLLGSGTISGsepgsf 358
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446596677  267 GCILEL---GTEE----------WLQDGDVVELT--------ITGLGTLRNTV 298
Cdd:TIGR01266 359 GSMLELswkGKKPidvaqgetrtFLEDGDEVILRghcqgegyRVGFGECAGKV 411
PRK15203 PRK15203
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional
109-304 3.64e-22

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional


Pssm-ID: 185125 [Multi-domain]  Cd Length: 429  Bit Score: 95.89  E-value: 3.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677 109 PVFYFTNHRAVIGPNDVVIGPKKSEKLDYELEIACVIGKEGRNISREQAEEYIFGYCIMNDWSARDLQATEMKVGLgPAK 188
Cdd:PRK15203 247 PLVFLKAPNTLTGDNQTSVRPNNIEYMHYEAELVVVIGKQARKVSEADAMDYVAGYTVCNDYAIRDYLENYYRPNL-RVK 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677 189 GKDFATSLGAHLVTKEELDvyrngDRYELEMTAHVNGKLLSKGNFQDIYYTFAEMIERASEDVTLYPGDVIGSgtvgtgc 268
Cdd:PRK15203 326 SRDGLTPILSTIVPKEAIP-----DPHNLTLRTFVNGELRQQGTTADLIFSVPFLIAYLSEFMTLNPGDMIAT------- 393
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446596677 269 ilelGTEEWLQD---GDVVELTITGLGTLRNTVKKEKEA 304
Cdd:PRK15203 394 ----GTPKGLSDvvpGDEVVVEVEGVGRLVNRIVSEETA 428
PRK12764 PRK12764
fumarylacetoacetate hydrolase family protein;
124-299 6.70e-18

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 237193 [Multi-domain]  Cd Length: 500  Bit Score: 84.04  E-value: 6.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677 124 DVVIGPKKSEKLDYELEIACVIGKEGRNISREQAEEYIFGYCIMNDWSARDLQATEMKVGLgPAKGKDFATSLGAHLVTK 203
Cdd:PRK12764  60 GTVERPAGTELLAFEGEIALVIGRPARRVSPEDAWSHVAAVTAANDLGVYDLRYADKGSNL-RSKGGDGFTPIGPALISA 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677 204 EELDVYRngdryeLEMTAHVNGKLLSKGNFQDIYYTFAEMIERASEDVTLYPGDVIGSGT-VGTGCIlelgteewlQDGD 282
Cdd:PRK12764 139 RGVDPAQ------LRVRTWVNGELVQDDTTEDLLFPFAQLVADLSQLLTLEEGDVILTGTpAGSSVA---------APGD 203
                        170       180
                 ....*....|....*....|....
gi 446596677 283 VVELTITGL-------GTLRNTVK 299
Cdd:PRK12764 204 VVEVEVDAPadgapstGRLVTRVV 227
HpaG-N-term TIGR02305
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, N-terminal subunit; ...
109-298 2.69e-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: 78.62  E-value: 2.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677  109 PVFYFTNHRAVIGPNDVVIGPKKSEKLDYELEIACVIGKEGRNISREQAEEYIFGYCIMNDWSardLQATEMKVGLGPAK 188
Cdd:TIGR02305  33 PVLYIKPRNTHNGCGQPIPLPAGVEKLRSGATLALVVGRTACRVREEEALDYVAGYALVNDVS---LPEDSYYRPAIKAK 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677  189 GKDFATSLGAHLVTKEEldvyrnGDRYELEMTAHVNGKLLSKGNFQDIYYTFAEMIERASEDVTLYPGDVIGSGTVGTGC 268
Cdd:TIGR02305 110 CRDGFCPIGPEVPLSAI------GNPDELTIYTYINGKPAQSNNTSNLVRSAAQLISELSEFMTLNPGDVLLLGTPEARV 183
                         170       180       190
                  ....*....|....*....|....*....|
gi 446596677  269 IlelgteewLQDGDVVELTITGLGTLRNTV 298
Cdd:TIGR02305 184 E--------VGPGDRVRVEAEGLGELENPV 205
PRK10691 PRK10691
fumarylacetoacetate hydrolase family protein;
129-290 2.01e-10

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 182650  Cd Length: 219  Bit Score: 59.72  E-value: 2.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677 129 PKKSEKLDYELEIACVIGKEGRNISREQAEEYIFGYCIMNDWSARDLQATEMKVG--LGPAKGKDFATSLGAHLVTKEel 206
Cdd:PRK10691  61 PKDFGSVHHEVELAVLIGATLRQATEEHVRKAIAGYGVALDLTLRDLQGKMKKAGqpWEKAKAFDNSCPISGFIPVAE-- 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677 207 dvyRNGDRYELEMTAHVNGKLLSKGNFQDIYYTFAEMIERASEDVTLYPGDVIGSGT---VGTgcilelgteewLQDGDV 283
Cdd:PRK10691 139 ---FTGDPQNTTLGLSVNGEVRQQGNTADMIHPIVPLIAYMSRFFTLRAGDVVLTGTpegVGP-----------LQSGDE 204

                 ....*..
gi 446596677 284 VELTITG 290
Cdd:PRK10691 205 LTVTFNG 211
PRK15203 PRK15203
4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional
106-303 4.22e-09

4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase; Provisional


Pssm-ID: 185125 [Multi-domain]  Cd Length: 429  Bit Score: 57.37  E-value: 4.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677 106 YDIP----VFYFTNHRAVIGPNDVVIGPKkSEKLDYELEIACVIGKEGRNISREQAEEYIFGYCIMNDWSARDLQATEMK 181
Cdd:PRK15203  28 YKAPpktaVWFIKPRNTVIRCGEPIPFPQ-GEKVLSGATVALIVGKTATKVREEDAAEYIAGYALANDVSLPEESFYRPA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446596677 182 VglgPAKGKDFATSLGaHLVTKEELDvyrngdryELEMTAHVNGKLLSKGNFQDIYYTFAEMIERASEDVTLYPGDVIgs 261
Cdd:PRK15203 107 I---KAKCRDGFCPIG-ETVALSNVD--------NLTIYTEINGRPADHWNTADLQRNAAQLLSALSEFATLNPGDAI-- 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446596677 262 gtvgtgcilELGTEE---WLQDGDVVELTITGLGTLRNTVKKEKE 303
Cdd:PRK15203 173 ---------LLGTPQarvEIQPGDRVRVLAEGFPPLENPVVDERE 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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