ID   SDGD_STRSQ              Reviewed;         358 AA.
AC   Q7X284;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Gentisate 1,2-dioxygenase {ECO:0000303|PubMed:15006746};
DE            Short=GDO {ECO:0000303|PubMed:15006746};
DE            EC=1.13.11.4 {ECO:0000269|PubMed:15006746};
GN   Name=sdgD {ECO:0000303|PubMed:15006746};
OS   Streptomyces sp.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP   PHENOTYPE, INDUCTION, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=WA46;
RX   PubMed=15006746; DOI=10.1128/aem.70.3.1297-1306.2004;
RA   Ishiyama D., Vujaklija D., Davies J.;
RT   "Novel pathway of salicylate degradation by Streptomyces sp. strain WA46.";
RL   Appl. Environ. Microbiol. 70:1297-1306(2004).
CC   -!- FUNCTION: Involved in the degradation of salicylate via a pathway
CC       involving coenzyme A derivative. Catalyzes the oxygen-dependent ring
CC       fission of gentisate between the carboxyl and proximal hydroxyl groups
CC       at positions 1 and 2 of the aromatic ring to form maleylpyruvate. The
CC       substrate specificity is strong, since salicylate, catechol,
CC       protocatechuic acid, homogenetisate, 2,3-dihydroxybenzoate or 5-
CC       aminosalicylate cannot substitute for gentisate in the ring cleavage
CC       reaction. {ECO:0000269|PubMed:15006746}.
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:15006746};
CC   -!- INDUCTION: By salicylate. {ECO:0000269|PubMed:15006746}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate gentisate.
CC       {ECO:0000269|PubMed:15006746}.
CC   -!- SIMILARITY: Belongs to the gentisate 1,2-dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; AB112586; BAC78375.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7X284; -.
DR   SMR; Q7X284; -.
DR   KEGG; ag:BAC78375; -.
DR   BioCyc; MetaCyc:MON-15921; -.
DR   GO; GO:0047922; F:gentisate 1,2-dioxygenase activity; IMP:UniProtKB.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR013096; Cupin_2.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF07883; Cupin_2; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Oxidoreductase.
FT   CHAIN           1..358
FT                   /note="Gentisate 1,2-dioxygenase"
FT                   /id="PRO_0000435738"
FT   REGION          185..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   358 AA;  39720 MW;  2D7E9E6CA420DCF6 CRC64;
     MTDTTSEQTE RKLLDELYAD FEDAGLIPLW TQVDGLMPMS PQPAAVPHLW RWAELLPIAQ
     RSGELVPVGR GGERRAMALS NPGFPGLPYA TPTLWTAIQY LGPREVAPSH RHSQGAFRFV
     VEGEGVWTNV DGDAVAMRRG DLLLTPSWAF HEHQNVTDEP MAWLDGLDIP LVSKLDAGFF
     EFGPDELSTR ETPERSRGER LWGHPGLRPI GRPDQPNSPL NAYRWEHTDA ALTAQLELEQ
     EGVPGVLEPG HAGVRFSNPT TGRDALVTMR TEMRRLRAGT RTAPVRTVGS AIWQVFEGEA
     VARVGDKVFE IAKGDLFVVP SWCEVSLSAR TQVDLFRFSD EPVYEALGLA RTSRGEHK