ID   SDGA_STRSQ              Reviewed;         553 AA.
AC   Q7X279;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Salicylyl-CoA synthase / salicylate adenylyltransferase {ECO:0000303|PubMed:15006746};
DE            EC=6.2.1.65 {ECO:0000269|PubMed:15006746};
GN   Name=sdgA {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 conversion of salicylate
CC       to salicyloyl-CoA via the formation of a salicylate-adenylate
CC       intermediate. The substrate specificity is strong, since benzoate, 3-
CC       hydroxybenzoate, 4-hydroxybenzoate, gentisate, 2-aminobenzoate,
CC       aminobenzoate, salicylamide, salicylaldoxime and 2-hydroxyphenyl
CC       acetate cannot substitute for salicylate.
CC       {ECO:0000269|PubMed:15006746}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + salicylate = 2-hydroxybenzoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:61668, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:30762, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:67148, ChEBI:CHEBI:456215; EC=6.2.1.65;
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 ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AB112586; BAC78380.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7X279; -.
DR   SMR; Q7X279; -.
DR   KEGG; ag:BAC78380; -.
DR   BioCyc; MetaCyc:MON-15914; -.
DR   BRENDA; 6.2.1.65; 17525.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IMP:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; ATP-binding; Ligase; Nucleotide-binding.
FT   CHAIN           1..553
FT                   /note="Salicylyl-CoA synthase / salicylate
FT                   adenylyltransferase"
FT                   /id="PRO_0000435739"
FT   BINDING         203
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P40871"
FT   BINDING         246..247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P40871"
FT   BINDING         320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P40871"
FT   BINDING         342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P40871"
FT   BINDING         426
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P40871"
FT   BINDING         441
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P40871"
FT   BINDING         533
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P40871"
FT   BINDING         533
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P40871"
SQ   SEQUENCE   553 AA;  59350 MW;  8127A58D18715749 CRC64;
     MTREGFVPWP KEAADRYREA GYWRGRPLGS YLHEWAETYG DTVAVVDGDT RLTYRQLVDR
     ADGLACRLLD SGLNPGDAML VQLPNGWEFV TLTLACLRAG IAPVMAMPAH RGHELRYLAA
     HAEVTSIAVP DRLGDFDHQA LGREVAEDTP SVGLLLVAGG TVGTDATDLR ALAEPADDPV
     TARARLDRIA PDSGDIAVFL LSGGTTGLPK LITRTHDDYE YNARRSAEVC GLDSDSVYLV
     ALPAGHNFPL ACPGILGTLM NGGRVVLART PEPGKVLPLM AAEGVTATAA VPAVVQRWID
     AVASGRHPAP PALRLLQVGG ARLAPEVARR AEPVLGGTLQ QVFGMAEGLL NYTRPDDPDD
     IKIETQGRPM CPDDEILVVD ASDNPVPPGE MGALLTRGPY TPRGYYRAAE HNARAFTPDG
     WYRTGDVVRL HPSGNLVVEG RDKDLINRGG EKISAEEVEN LIYRLPGVAR VAAVAKADPD
     LGERVCAVVV VEPGTQLSLE SVRAALTAMQ VARYKLPEDL LVVDELPLTK VGKIDKKRLR
     DVVRGKADSV EAV