ID   GALA_PSEPK              Reviewed;         340 AA.
AC   Q88JX5;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Gallate dioxygenase;
DE            EC=1.13.11.57;
DE   AltName: Full=Gallate degradation protein A;
GN   Name=galA; OrderedLocusNames=PP_2518;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP   INDUCTION.
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=16030014; DOI=10.1074/jbc.m502585200;
RA   Nogales J., Canales A., Jimenez-Barbero J., Garcia J.L., Diaz E.;
RT   "Molecular characterization of the gallate dioxygenase from Pseudomonas
RT   putida KT2440. The prototype of a new subgroup of extradiol dioxygenases.";
RL   J. Biol. Chem. 280:35382-35390(2005).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=21219457; DOI=10.1111/j.1365-2958.2010.07448.x;
RA   Nogales J., Canales A., Jimenez-Barbero J., Serra B., Pingarron J.M.,
RA   Garcia J.L., Diaz E.;
RT   "Unravelling the gallic acid degradation pathway in bacteria: the gal
RT   cluster from Pseudomonas putida.";
RL   Mol. Microbiol. 79:359-374(2011).
CC   -!- FUNCTION: Ring-cleavage dioxygenase that acts specifically on gallate
CC       to produce the keto-tautomer of 4-oxalomesaconate. Mediates the first
CC       step of gallate degradation pathway. {ECO:0000269|PubMed:16030014,
CC       ECO:0000269|PubMed:21219457}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3,4,5-trihydroxybenzoate + O2 = (1E)-4-oxobut-1-ene-1,2,4-
CC         tricarboxylate + 2 H(+); Xref=Rhea:RHEA:28927, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16918, ChEBI:CHEBI:57471;
CC         EC=1.13.11.57; Evidence={ECO:0000269|PubMed:16030014,
CC         ECO:0000269|PubMed:21219457};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:16030014};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=144 uM for gallate {ECO:0000269|PubMed:16030014};
CC         Vmax=53.2 umol/min/mg enzyme with gallate as substrate
CC         {ECO:0000269|PubMed:16030014};
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:16030014};
CC   -!- INDUCTION: By gallate. {ECO:0000269|PubMed:16030014}.
CC   -!- SIMILARITY: Belongs to the LigB/MhpB extradiol dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; AE015451; AAN68130.1; -; Genomic_DNA.
DR   RefSeq; NP_744666.2; NC_002947.4.
DR   AlphaFoldDB; Q88JX5; -.
DR   SMR; Q88JX5; -.
DR   STRING; 160488.PP_2518; -.
DR   EnsemblBacteria; AAN68130; AAN68130; PP_2518.
DR   KEGG; ag:AAN68130; -.
DR   KEGG; ppu:PP_2518; -.
DR   PATRIC; fig|160488.4.peg.2673; -.
DR   eggNOG; COG3384; Bacteria.
DR   HOGENOM; CLU_653589_0_0_6; -.
DR   PhylomeDB; Q88JX5; -.
DR   BioCyc; MetaCyc:G1G01-2702-MON; -.
DR   BioCyc; PPUT160488:G1G01-2702-MON; -.
DR   Proteomes; UP000000556; Chromosome.
DR   GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB.
DR   GO; GO:0036238; F:gallate dioxygenase activity; IDA:UniProtKB.
DR   GO; GO:0019396; P:gallate catabolic process; IDA:UniProtKB.
DR   CDD; cd07923; Gallate_dioxygenase_C; 1.
DR   Gene3D; 1.10.700.10; -; 1.
DR   InterPro; IPR034940; Gallate_dioxygenase_C.
DR   InterPro; IPR036622; LigA_sf.
DR   InterPro; IPR011986; Xdiol_dOase_LigA.
DR   InterPro; IPR004183; Xdiol_dOase_suB.
DR   Pfam; PF07746; LigA; 1.
DR   Pfam; PF02900; LigB; 1.
DR   SUPFAM; SSF48076; SSF48076; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..340
FT                   /note="Gallate dioxygenase"
FT                   /id="PRO_0000418495"
FT   ACT_SITE        45
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        113
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   340 AA;  38459 MW;  AB4C6FEF2021E56C CRC64;
     MADEGGNPRD LPPVGGHAAL SRHIGQSLMA DEFDMSFFRD KPLDHGFFSP MSALLPCDES
     WPVQIVPLQV GVLQLPIPTA RRCYKLGQAL RRAIESYPED LKVAIVATGG VSHQVHGERC
     GFNNPEWDAQ FLDLLVNDPQ RLTEMTLAEY ATLGGMEGAE VITWLIMRGT LSANVERKHQ
     SYYLPSMTGI ATLLLENRDQ ALPAPVNERH RQHMQHQLAG AEQLEGTYPY TLERSAKGYR
     LNKFLHRMIE PQWRQRFLSE PEALYREAGL SEEESDLLRR RDWRGLIHYG VIFFVLEKLG
     AVLGVSNLDI YAAMRGQSIE DFMKTRNQQV RYSVAGKAPN