ID   SDGC_STRSQ              Reviewed;         517 AA.
AC   Q7X281;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Salicyloyl-CoA 5-hydroxylase {ECO:0000303|PubMed:15006746};
DE            EC=1.14.13.209 {ECO:0000269|PubMed:15006746};
GN   Name=sdgC {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, AND INDUCTION.
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 aromatic hydroxylation
CC       of salicylyl-CoA to yield gentisyl-CoA. {ECO:0000269|PubMed:15006746}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hydroxybenzoyl-CoA + H(+) + NADH + O2 = 2,5-
CC         dihydroxybenzoyl-CoA + H2O + NAD(+); Xref=Rhea:RHEA:48008,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67148,
CC         ChEBI:CHEBI:88147; EC=1.14.13.209;
CC         Evidence={ECO:0000269|PubMed:15006746};
CC   -!- INDUCTION: By salicylate. {ECO:0000269|PubMed:15006746}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to degrade
CC       salicylate. {ECO:0000269|PubMed:15006746}.
CC   -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB112586; BAC78378.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7X281; -.
DR   SMR; Q7X281; -.
DR   KEGG; ag:BAC78378; -.
DR   BioCyc; MetaCyc:MON-15920; -.
DR   BRENDA; 1.14.13.209; 1284.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IMP:UniProtKB.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; NAD; Oxidoreductase.
FT   CHAIN           1..517
FT                   /note="Salicyloyl-CoA 5-hydroxylase"
FT                   /id="PRO_0000435737"
SQ   SEQUENCE   517 AA;  56572 MW;  E74499C0DCCD4CD5 CRC64;
     MKVACIGAGP GGLFFATLLK RSRPDAEVVV FERNRPDDTF GFGVVFSDAT LDAIDAADPV
     LSEALEKHGR HWDDIEVRVH GERERVGGMG MAAVVRKTLL SLLQERARAE GVQMRFQDEV
     RDPAELDDFD LVVVCDGANS RFRTLFADDF GPTAEVASAK FIWFGTTYMF DGLTFVHQDG
     PHGVFAAHAY PISDSLSTFI VETDADSWAR AGLDAFDPAT PLGMSDEKTK SYLEDLFRAQ
     IDGHPLVGNN SRWANFATRR ARSWRSGKWV LLGDAAHTAH FSVGSGTKMA MEDAVALAET
     LGEASRSVPE ALDLYEERRR PKVERIQNSA RPSLSWWEHF GRYVRSFDAP TQFAFHFLTR
     SIPRGKLAVR DAAYVDRVDG WWLRHHEAGP LKTPFRVGPY RLPTRRVTVG DDLLTGTDGT
     GIPMVPFSGQ PFGAGVWIDA PDTEEGLPLA LDQVRETAEA GVLLVGVRGG TALTRVLVAE
     EARLAHSLPA AIVGAYDDDT ATTLVLSGRA DLVGGTK