ID   TRS1_STRTI              Reviewed;         527 AA.
AC   P80436; B7X8E6; Q5PT48;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Triostin synthetase I;
DE            Short=TrsI;
DE            EC=6.3.2.-;
DE   AltName: Full=AMP-binding ligase;
DE   AltName: Full=Quinoxaline-2-carboxylic acid-activating enzyme;
GN   Name=trsA;
OS   Streptomyces triostinicus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=45399;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-24, AND FUNCTION.
RC   STRAIN=ATCC 21043 / JCM 5046 / NBRC 13836;
RX   PubMed=15569690; DOI=10.1074/jbc.m411026200;
RA   Schmoock G., Pfennig F., Jewiarz J., Schlumbohm W., Laubinger W.,
RA   Schauwecker F., Keller U.;
RT   "Functional cross-talk between fatty acid synthesis and nonribosomal
RT   peptide synthesis in quinoxaline antibiotic-producing streptomycetes.";
RL   J. Biol. Chem. 280:4339-4349(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21043 / JCM 5046 / NBRC 13836;
RX   PubMed=19194935; DOI=10.1002/btpr.34;
RA   Praseuth A.P., Wang C.C., Watanabe K., Hotta K., Oguri H., Oikawa H.;
RT   "Complete sequence of biosynthetic gene cluster responsible for producing
RT   triostin A and evaluation of quinomycin-type antibiotics from Streptomyces
RT   triostinicus.";
RL   Biotechnol. Prog. 24:1226-1231(2008).
RN   [3]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=2354149; DOI=10.1021/bi00466a015;
RA   Glund K., Schlumbohm W., Bapat M., Keller U.;
RT   "Biosynthesis of quinoxaline antibiotics: purification and characterization
RT   of the quinoxaline-2-carboxylic acid activating enzyme from Streptomyces
RT   triostinicus.";
RL   Biochemistry 29:3522-3527(1990).
CC   -!- FUNCTION: Involved in triostin biosynthesis. Activates quinoxaline-2-
CC       carboxylic acid (QA) via catalysis of the ATP-pyrophosphate exchange
CC       reaction dependent on QA, and the formation of the corresponding
CC       adenylate. Also activates structural analogs of QA such as quinoline-2-
CC       carboxylic acid and thieno[3,2-b]pyridine-5-carboxylic acid, but not
CC       quinoline-3-carboxylic acid, quinoline-4-carboxylic acid, pyridine-2-
CC       carboxylic acid or 2-pyrazinecarboxylic acid.
CC       {ECO:0000269|PubMed:15569690, ECO:0000269|PubMed:2354149}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0-9.0. {ECO:0000269|PubMed:2354149};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:2354149}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAV84073.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY825941; AAV84073.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AB366635; BAH04171.1; -; Genomic_DNA.
DR   AlphaFoldDB; P80436; -.
DR   SMR; P80436; -.
DR   PRIDE; P80436; -.
DR   BioCyc; MetaCyc:MON-19596; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 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   InterPro; IPR042099; ANL_N_sf.
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   Antibiotic biosynthesis; ATP-binding; Direct protein sequencing; Ligase;
KW   Nucleotide-binding.
FT   CHAIN           1..527
FT                   /note="Triostin synthetase I"
FT                   /id="PRO_0000089392"
FT   BINDING         187..188
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         230..231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         300..302
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         406
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         421
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         512
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         512
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        411..413
FT                   /note="SPE -> TRR (in Ref. 1; AAV84073)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   527 AA;  57571 MW;  62163DE6936672B4 CRC64;
     MLDGFVPWPD HLADEYRRRG IWLGRPLGDL LHDSCRRHAD RVAVVCDGHR MTYAELSRRA
     DRLAGGLIGL GIRPLDRVVV HLPNIPEFVV LVFALLRAGA IPVLALPGHR KSEISHLCAH
     SGAVAYAVKD EFGGFDYREL AREIPPVRHV LVSGDAQEFT ALESVGGDDV PLPRVDPSDP
     ALFLLSGGTT GLPKLIPRAH DDYAYVMRAT AEAMHVGEEV AYLAVNPVAH QAALACPGVF
     GSLLLGGKAV LTSSVRPDEV FPLIRREHVT VTTVVPSVLR LWADSGQRPD LSHLLVQVGS
     APLDPALARR AGEVLGCRIM RWYGISEGLL THTRFDDPED VIMGTDGRPM SRDDEVRIVD
     ESLNPVPEGE AGEMIARGPY TIRGYYRAPE ENTRSFTPDG FFRTGDLVRR SPEGDITIVG
     RIKDVINRAG EKVSAEEVER QLRTHPSVQD AAVVGVPDTV LGERTYAFLV LTGAQIRTSA
     VKEFLRGCGL ATYKIPDRIV PLDQLPRTPM GKVDKKTLRA LAVSSAR