ID   HPAG_SALDU              Reviewed;         429 AA.
AC   Q9RPU5;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase;
DE   Includes:
DE     RecName: Full=2-hydroxyhepta-2,4-diene-1,7-dioate isomerase;
DE              Short=HHDD isomerase;
DE              EC=5.3.3.10 {ECO:0000250|UniProtKB:P37352};
DE     AltName: Full=5-carboxymethyl-2-hydroxymuconate Delta-isomerase;
DE   Includes:
DE     RecName: Full=5-carboxymethyl-2-oxo-hex-3-ene-1,7-dioate decarboxylase;
DE              EC=4.1.1.68 {ECO:0000250|UniProtKB:P37352};
DE     AltName: Full=5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase;
DE              Short=OPET decarboxylase;
GN   Name=hpaG;
OS   Salmonella dublin.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=98360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2229;
RA   Galyov E.E., Wood M.W., Hedges S.;
RT   "Characterization of the hpa genetic locus from Salmonella dublin.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Decarboxylates OPET (5-oxo-pent-3-ene-1,2,5-tricarboxylic
CC       acid) into HHDD (2-hydroxy-hept-2,4-diene-1,7-dioate) and isomerizes it
CC       to OHED (2-oxo-hept-3-ene-1,7-dioate). {ECO:0000250|UniProtKB:P37352}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,4Z)-5-hydroxypenta-2,4-diene-1,2,5-tricarboxylate =
CC         (3E,5R)-5-carboxy-2-oxohept-3-enedioate; Xref=Rhea:RHEA:18813,
CC         ChEBI:CHEBI:47961, ChEBI:CHEBI:87491; EC=5.3.3.10;
CC         Evidence={ECO:0000250|UniProtKB:P37352};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3E,5R)-5-carboxy-2-oxohept-3-enedioate + H(+) = (4Z)-2-
CC         oxohept-4-enedioate + CO2; Xref=Rhea:RHEA:14397, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:87491, ChEBI:CHEBI:87507; EC=4.1.1.68;
CC         Evidence={ECO:0000250|UniProtKB:P37352};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P37352};
CC   -!- PATHWAY: Aromatic compound metabolism; 4-hydroxyphenylacetate
CC       degradation; pyruvate and succinate semialdehyde from 4-
CC       hydroxyphenylacetate: step 4/7.
CC   -!- PATHWAY: Aromatic compound metabolism; 4-hydroxyphenylacetate
CC       degradation; pyruvate and succinate semialdehyde from 4-
CC       hydroxyphenylacetate: step 5/7.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P37352}.
CC   -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF144422; AAD53501.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RPU5; -.
DR   SMR; Q9RPU5; -.
DR   UniPathway; UPA00208; UER00419.
DR   UniPathway; UPA00208; UER00420.
DR   GO; GO:0008704; F:5-carboxymethyl-2-hydroxymuconate delta-isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018800; F:5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1901023; P:4-hydroxyphenylacetate catabolic process; IEA:InterPro.
DR   Gene3D; 3.90.850.10; -; 2.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   InterPro; IPR012684; HPA_isomer/decarb_C.
DR   InterPro; IPR012686; HPA_isomer/decarb_N.
DR   Pfam; PF01557; FAA_hydrolase; 2.
DR   SUPFAM; SSF56529; SSF56529; 2.
DR   TIGRFAMs; TIGR02303; HpaG-C-term; 1.
DR   TIGRFAMs; TIGR02305; HpaG-N-term; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Isomerase; Lyase; Metal-binding;
KW   Multifunctional enzyme; Repeat.
FT   CHAIN           1..429
FT                   /note="4-hydroxyphenylacetate degradation bifunctional
FT                   isomerase/decarboxylase"
FT                   /id="PRO_0000156834"
FT   REPEAT          1..215
FT                   /note="Approximate"
FT   REPEAT          216..429
FT                   /note="Approximate"
FT   BINDING         276
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         278
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   429 AA;  47186 MW;  D32723999AC4084E CRC64;
     MKGTVFAVAL NHRSQLDAWQ EAFSQPPYNA PPKTAVWFIK PRNTVIRHGE PILYPQGEKV
     LSGATVALIV GKTASRKRSE AAAEYIAGYA LANEVSLPEE SFYRPAIKAK CRDGFCPLGE
     MAPLSDVDNL TIITEINGRE ADHWNTADLQ RSAAQLLSAL SEFATLNPGD AILLGTPQNR
     VALRPGDRVR ILAKGLPALE NPVVAEDEFA RNQTFTWPLS ATGTLFALGL NYADHASELA
     FTPPKEPLVF IKAPNTFTEH HQTSVRPNNV EYMHYEAELV VVIGKTARKV SEAEAMEYVA
     GYTVCNDYAI RDYLENYYRP NLRVKSRDGL TPIGPWIVDK EAVSDPHNLT LRTFVNGELR
     QEGTTADLIF SIPFLISYLS EFMTLQPGDM IATGTPKGLS DVVPGDEVVL EIKGVGRLVN
     QIVCEESAN