ID   GNTDO_HALSB             Reviewed;         358 AA.
AC   Q330M9; O73956;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Gentisate 1,2-dioxygenase;
DE            EC=1.13.11.4;
GN   Name=gdoA;
OS   Haloferax sp.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax; unclassified Haloferax.
OX   NCBI_TaxID=2253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-41 AND 76-85,
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   ACTIVITY REGULATION.
RC   STRAIN=D1227 / ATCC 51408;
RX   PubMed=9827334; DOI=10.1007/s007920050090;
RA   Fu W., Oriel P.;
RT   "Gentisate 1,2-dioxygenase from Haloferax sp. D1227.";
RL   Extremophiles 2:439-446(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA], FUNCTION, AND INDUCTION.
RC   STRAIN=D1227 / ATCC 51408;
RX   PubMed=16802151; DOI=10.1007/s00253-006-0509-0;
RA   Fairley D.J., Wang G., Rensing C., Pepper I.L., Larkin M.J.;
RT   "Expression of gentisate 1,2-dioxygenase (gdoA) genes involved in aromatic
RT   degradation in two haloarchaeal genera.";
RL   Appl. Microbiol. Biotechnol. 73:691-695(2006).
RN   [3]
RP   FUNCTION, AND ACTIVITY REGULATION.
RC   STRAIN=D1227 / ATCC 51408;
RX   PubMed=10086844; DOI=10.1007/s007920050098;
RA   Fu W., Oriel P.;
RT   "Degradation of 3-phenylpropionic acid by Haloferax sp. D1227.";
RL   Extremophiles 3:45-53(1999).
CC   -!- FUNCTION: Catalyzes the oxygen-dependent ring fission of gentisate
CC       between the carboxyl and proximal hydroxyl groups at positions 1 and 2
CC       of the aromatic ring to form maleylpyruvate. No activity with cathechol
CC       and protecatechuate as substrates. Part of a 3-hydroxybenzoic acid-
CC       degradation pathway. {ECO:0000269|PubMed:10086844,
CC       ECO:0000269|PubMed:16802151, ECO:0000269|PubMed:9827334}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,5-dihydroxybenzoate + O2 = 3-maleylpyruvate + H(+);
CC         Xref=Rhea:RHEA:18237, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16727, ChEBI:CHEBI:58044; EC=1.13.11.4;
CC         Evidence={ECO:0000269|PubMed:9827334};
CC   -!- ACTIVITY REGULATION: Inhibited by 2,2'-dipyridyl.
CC       {ECO:0000269|PubMed:10086844, ECO:0000269|PubMed:9827334}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=95 uM for gentisic acid {ECO:0000269|PubMed:9827334};
CC         Vmax=187 umol/min/mg enzyme toward gentisate
CC         {ECO:0000269|PubMed:9827334};
CC         Note=Highest activity in the presence of 2 M KCl or NaCl. 60% loss of
CC         activity in the presence of 1.5 M KCl.;
CC       pH dependence:
CC         Optimum pH is 7.2. {ECO:0000269|PubMed:9827334};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.
CC         {ECO:0000269|PubMed:9827334};
CC   -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9827334}.
CC   -!- INDUCTION: Up-regulated in cells grown on benzoic acid, 3-
CC       hydroxybenzoic acid, phenylpropionic acid or cinnamic acid, but not in
CC       cell grown on pyruvic acid. {ECO:0000269|PubMed:16802151}.
CC   -!- SIMILARITY: Belongs to the gentisate 1,2-dioxygenase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC25761.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAC25761.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF069949; AAC25761.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AY297456; AAQ62856.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q330M9; -.
DR   SMR; Q330M9; -.
DR   BioCyc; MetaCyc:MON-10867; -.
DR   BRENDA; 1.13.11.4; 2567.
DR   UniPathway; UPA00082; -.
DR   GO; GO:0047922; F:gentisate 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR013096; Cupin_2.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF07883; Cupin_2; 2.
DR   SMART; SM00835; Cupin_1; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Direct protein sequencing;
KW   Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9827334"
FT   CHAIN           2..358
FT                   /note="Gentisate 1,2-dioxygenase"
FT                   /id="PRO_0000428927"
FT   DOMAIN          239..358
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   358 AA;  40591 MW;  3709CC9AA3A3F3E3 CRC64;
     MAEQEPKELL EMSTDTERLL EENDLRPLWE VEKDFGNQFG GFEADIWKWE DIQASIDAIE
     RDVPIADLPP GFQRRVAVPV NTGYRNAISN TIYVGVQTVS PGETAPAHRH GANALRFTID
     GSEDMKTVVA GEEFPMRDND LITTPQWEWH DHVNDGDETA AWLDVLDLPL VLDSLNARNT
     FENHELDRQP VTKSQGYWES QYGRARPFED TKEDGIPGPF EGNCAATPPY RFSWKDTLQT
     LRQRAENDDP DPHDGYSLSY VNPATGQPPL FPTMSFRAQL LQEETDPHFH NAVDAYFVIE
     GEGATHVGDD VLEWSERDIF VIPPDEIHHH DPDGEAILLG MTDRPVFEAF NFYAEAEP