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Conserved domains on  [gi|1850101489|ref|WP_172901056|]
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fumarylacetoacetate hydrolase family protein [Sinorhizobium fredii]

Protein Classification

fumarylacetoacetate hydrolase family protein( domain architecture ID 11467721)

fumarylacetoacetate (FAA) hydrolase family protein similar to FAA hydrolase that catalyzes the hydrolysis of 4-fumarylacetoacetate to form acetoacetate and fumarate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3970 COG3970
Fumarylacetoacetate (FAA) hydrolase family protein [General function prediction only];
4-376 0e+00

Fumarylacetoacetate (FAA) hydrolase family protein [General function prediction only];


:

Pssm-ID: 443170 [Multi-domain]  Cd Length: 335  Bit Score: 583.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850101489   4 ETGTFVGRAWRPDVE-GPSLVTVREGDLIDITSkAVPTMRDLLDLSDPVAHVRSASGEAIAPVDAVMAK--PERGSGEVH 80
Cdd:COG3970     1 DQATLVGRVWRPGVGgGPRVVVVRGGRVYDLTA-AAPTVSDLLEAPDPAAAVRAAAGERLGSLDDLLNSlgAPRDPADPR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850101489  81 LLAPCDLQAVKACGVTFARSMIERVIEERAagdatraeairtrmaaiigdslrnlkagspeaagvkaaliEEGVWSQYLE 160
Cdd:COG3970    80 LLAPVDLQEVKAAGVTFARSMLERVIEEQA----------------------------------------AEGLWSQYLE 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850101489 161 VGIGPDAEVFTKAQPLSSVGWGAAVGLHPISRWNNPEPEIVLAVSADGRAKGATLGNDVNLRDVEGRSALLLGKAKDNNA 240
Cdd:COG3970   120 VYIGPDPEIFTKATPLRSVGPGAPVGIRPDSEWNNPEPELVLVVNSRGEIVGATLGNDVNLRDIEGRSALLLPQAKDNNA 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850101489 241 SCAVGPFVRLFDETYSIDDVRNADLDLLIEGPDGFRLKGASTMREISRDPLDLVAQTVGPHHQYPDGLMLFMGTLFAPVE 320
Cdd:COG3970   200 SCAIGPFIRLFDETFTLDDVRDLEIRLTIEGEDGFVLEGSSSMAEISRDPEELVAQTLGRHHQYPDGFVLFTGTLFAPTQ 279
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1850101489 321 DRGEPGQGFTHKIGDVVTISSPALGSLVNTVRLSTDCPPWTFGIAALMRNLAKREL 376
Cdd:COG3970   280 DRDGPGQGFTHKPGDVVEISIPGLGTLVNTVVLSDEAPPWTFGIRALMRNLAARGL 335
 
Name Accession Description Interval E-value
COG3970 COG3970
Fumarylacetoacetate (FAA) hydrolase family protein [General function prediction only];
4-376 0e+00

Fumarylacetoacetate (FAA) hydrolase family protein [General function prediction only];


Pssm-ID: 443170 [Multi-domain]  Cd Length: 335  Bit Score: 583.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850101489   4 ETGTFVGRAWRPDVE-GPSLVTVREGDLIDITSkAVPTMRDLLDLSDPVAHVRSASGEAIAPVDAVMAK--PERGSGEVH 80
Cdd:COG3970     1 DQATLVGRVWRPGVGgGPRVVVVRGGRVYDLTA-AAPTVSDLLEAPDPAAAVRAAAGERLGSLDDLLNSlgAPRDPADPR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850101489  81 LLAPCDLQAVKACGVTFARSMIERVIEERAagdatraeairtrmaaiigdslrnlkagspeaagvkaaliEEGVWSQYLE 160
Cdd:COG3970    80 LLAPVDLQEVKAAGVTFARSMLERVIEEQA----------------------------------------AEGLWSQYLE 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850101489 161 VGIGPDAEVFTKAQPLSSVGWGAAVGLHPISRWNNPEPEIVLAVSADGRAKGATLGNDVNLRDVEGRSALLLGKAKDNNA 240
Cdd:COG3970   120 VYIGPDPEIFTKATPLRSVGPGAPVGIRPDSEWNNPEPELVLVVNSRGEIVGATLGNDVNLRDIEGRSALLLPQAKDNNA 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850101489 241 SCAVGPFVRLFDETYSIDDVRNADLDLLIEGPDGFRLKGASTMREISRDPLDLVAQTVGPHHQYPDGLMLFMGTLFAPVE 320
Cdd:COG3970   200 SCAIGPFIRLFDETFTLDDVRDLEIRLTIEGEDGFVLEGSSSMAEISRDPEELVAQTLGRHHQYPDGFVLFTGTLFAPTQ 279
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1850101489 321 DRGEPGQGFTHKIGDVVTISSPALGSLVNTVRLSTDCPPWTFGIAALMRNLAKREL 376
Cdd:COG3970   280 DRDGPGQGFTHKPGDVVEISIPGLGTLVNTVVLSDEAPPWTFGIRALMRNLAARGL 335
FAA_hydrolase pfam01557
Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) ...
168-351 1.13e-04

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: 43.04  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850101489 168 EVFTKAqPLSSVGWGAAVGLHPISRWNNPEPEIVLAVSADGRA----------KGATLGNDVNLRDV---EGRSALLLGK 234
Cdd:pfam01557  28 VLFVKP-PSSLIGPGDPIVRPAGVTKLDYEAELAVVIGRPARDvspeealdyiFGYTLANDVSARDLqrrEMPLQWFRGK 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850101489 235 AKDnnASCAVGPFVRLFDEtysIDDVRNADLDLLIEGpdgfRLKGASTMREISRDPLDLVA-----QTVGPhhqypdGLM 309
Cdd:pfam01557 107 SFD--GFTPLGPWIVTRDE---LPDPGDLRLRLRVNG----EVRQDGNTSDMIFSPAELIAhlsqfMTLRP------GDI 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1850101489 310 LFMGTLfaPVEDRGEPGQGFTHKiGDVVTISSPALGSLVNTV 351
Cdd:pfam01557 172 ILTGTP--SGVGAGRAPPVFLKP-GDTVEVEIEGLGTLRNTV 210
 
Name Accession Description Interval E-value
COG3970 COG3970
Fumarylacetoacetate (FAA) hydrolase family protein [General function prediction only];
4-376 0e+00

Fumarylacetoacetate (FAA) hydrolase family protein [General function prediction only];


Pssm-ID: 443170 [Multi-domain]  Cd Length: 335  Bit Score: 583.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850101489   4 ETGTFVGRAWRPDVE-GPSLVTVREGDLIDITSkAVPTMRDLLDLSDPVAHVRSASGEAIAPVDAVMAK--PERGSGEVH 80
Cdd:COG3970     1 DQATLVGRVWRPGVGgGPRVVVVRGGRVYDLTA-AAPTVSDLLEAPDPAAAVRAAAGERLGSLDDLLNSlgAPRDPADPR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850101489  81 LLAPCDLQAVKACGVTFARSMIERVIEERAagdatraeairtrmaaiigdslrnlkagspeaagvkaaliEEGVWSQYLE 160
Cdd:COG3970    80 LLAPVDLQEVKAAGVTFARSMLERVIEEQA----------------------------------------AEGLWSQYLE 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850101489 161 VGIGPDAEVFTKAQPLSSVGWGAAVGLHPISRWNNPEPEIVLAVSADGRAKGATLGNDVNLRDVEGRSALLLGKAKDNNA 240
Cdd:COG3970   120 VYIGPDPEIFTKATPLRSVGPGAPVGIRPDSEWNNPEPELVLVVNSRGEIVGATLGNDVNLRDIEGRSALLLPQAKDNNA 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850101489 241 SCAVGPFVRLFDETYSIDDVRNADLDLLIEGPDGFRLKGASTMREISRDPLDLVAQTVGPHHQYPDGLMLFMGTLFAPVE 320
Cdd:COG3970   200 SCAIGPFIRLFDETFTLDDVRDLEIRLTIEGEDGFVLEGSSSMAEISRDPEELVAQTLGRHHQYPDGFVLFTGTLFAPTQ 279
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1850101489 321 DRGEPGQGFTHKIGDVVTISSPALGSLVNTVRLSTDCPPWTFGIAALMRNLAKREL 376
Cdd:COG3970   280 DRDGPGQGFTHKPGDVVEISIPGLGTLVNTVVLSDEAPPWTFGIRALMRNLAARGL 335
YcgM COG0179
2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) ...
169-352 2.07e-05

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: 45.06  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850101489 169 VFTKAqPLSSVGWGAAVGLHPISRWNNPEPEIVLAVSADGR------AK----GATLGNDVNLRDVEGRSALLLGKAKDN 238
Cdd:COG0179    32 LFLKP-PSALVGPGDPIPLPAGSGKLDYEGELAVVIGKRARnvseedALdhvaGYTVANDVTARDLQRERGGQWTRGKSF 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850101489 239 NASCAVGPFVRLFDEtysIDDVRNADLDLLIEGpdgfRLKGASTMREISRDPLDLVAQ-----TVGPhhqypdGLMLFMG 313
Cdd:COG0179   111 DTFCPLGPWIVTADE---IPDPQDLRIRLRVNG----EVRQDGNTSDMIFSVAELIAYlsqfmTLEP------GDVILTG 177
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1850101489 314 TlfaPvedrgePGQGFThKIGDVVTISSPALGSLVNTVR 352
Cdd:COG0179   178 T---P------AGVGPL-KPGDVVEVEIEGIGTLRNTVV 206
FAA_hydrolase pfam01557
Fumarylacetoacetate (FAA) hydrolase family; This family consists of fumarylacetoacetate (FAA) ...
168-351 1.13e-04

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: 43.04  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850101489 168 EVFTKAqPLSSVGWGAAVGLHPISRWNNPEPEIVLAVSADGRA----------KGATLGNDVNLRDV---EGRSALLLGK 234
Cdd:pfam01557  28 VLFVKP-PSSLIGPGDPIVRPAGVTKLDYEAELAVVIGRPARDvspeealdyiFGYTLANDVSARDLqrrEMPLQWFRGK 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850101489 235 AKDnnASCAVGPFVRLFDEtysIDDVRNADLDLLIEGpdgfRLKGASTMREISRDPLDLVA-----QTVGPhhqypdGLM 309
Cdd:pfam01557 107 SFD--GFTPLGPWIVTRDE---LPDPGDLRLRLRVNG----EVRQDGNTSDMIFSPAELIAhlsqfMTLRP------GDI 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1850101489 310 LFMGTLfaPVEDRGEPGQGFTHKiGDVVTISSPALGSLVNTV 351
Cdd:pfam01557 172 ILTGTP--SGVGAGRAPPVFLKP-GDTVEVEIEGLGTLRNTV 210
 
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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