ID   NAGK_RALSP              Reviewed;         192 AA.
AC   O86042;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Fumarylpyruvate hydrolase {ECO:0000303|PubMed:11133965, ECO:0000312|EMBL:AAD12620.1};
DE            EC=3.7.1.20;
DE   AltName: Full=Naphthalene degradation protein K;
GN   Name=nagK {ECO:0000312|EMBL:AAD12620.1};
OS   Ralstonia sp.
OG   Plasmid pWWU2 {ECO:0000312|EMBL:AAD12620.1}.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=54061;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAD12620.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=U2 {ECO:0000312|EMBL:AAD12620.1};
RX   PubMed=11133965; DOI=10.1128/jb.183.2.700-708.2001;
RA   Zhou N.Y., Fuenmayor S.L., Williams P.A.;
RT   "nag genes of Ralstonia (formerly Pseudomonas) sp. strain U2 encoding
RT   enzymes for gentisate catabolism.";
RL   J. Bacteriol. 183:700-708(2001).
CC   -!- FUNCTION: Involved in the catabolism of gentisate (2,5-
CC       dihydroxybenzoate) a key intermediates in the aerobic pathways for the
CC       metabolism of a large number of aromatic compoun such as naphthalene.
CC       Catalyzes the hydrolytic cleavage of fumarylpyruvate to form fumarate
CC       and pyruvate. {ECO:0000269|PubMed:11133965}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-fumarylpyruvate + H2O = fumarate + H(+) + pyruvate;
CC         Xref=Rhea:RHEA:26168, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16854, ChEBI:CHEBI:29806; EC=3.7.1.20;
CC         Evidence={ECO:0000269|PubMed:11133965};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC       {ECO:0000269|PubMed:11133965}.
CC   -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
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DR   EMBL; AF036940; AAD12620.1; -; Genomic_DNA.
DR   AlphaFoldDB; O86042; -.
DR   SMR; O86042; -.
DR   KEGG; ag:AAD12620; -.
DR   BioCyc; MetaCyc:MON-14771; -.
DR   BRENDA; 3.7.1.20; 5275.
DR   UniPathway; UPA00082; -.
DR   GO; GO:0034545; F:fumarylpyruvate hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1901170; P:naphthalene catabolic process; IDA:UniProtKB.
DR   Gene3D; 3.90.850.10; -; 1.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   SUPFAM; SSF56529; SSF56529; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Hydrolase; Metal-binding; Plasmid;
KW   Pyruvate.
FT   CHAIN           1..192
FT                   /note="Fumarylpyruvate hydrolase"
FT                   /id="PRO_0000421468"
FT   BINDING         41
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         43
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   192 AA;  20886 MW;  661BD47519B61D45 CRC64;
     MGRPVDKSVE QAFYFTKSPQ TLVESGATVA YPPRTSNYHY EMELVLAIGK PGFRVSEDQA
     HELIYGYAAG LDMTRRDLQL VARDKGRPWD TGKDIEEGSV CSEIVPMQGV VVEQGAIALE
     VNGQTKQSSN VDKLIWNVRE IIADLSTYYH LQPGDLIYTG TPEGVGAVVA GDKIIGRVEG
     IAEISLTVGP AE