ID   A0A1Q5L6F5_9ACTN        Unreviewed;       858 AA.
AC   A0A1Q5L6F5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Malonyl-CoA:ACP transacylase (MAT) domain-containing protein {ECO:0000259|SMART:SM00827};
GN   ORFNames=AMK31_06570 {ECO:0000313|EMBL:OKJ89574.1};
OS   Streptomyces sp. TSRI0107.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703942 {ECO:0000313|EMBL:OKJ89574.1, ECO:0000313|Proteomes:UP000185813};
RN   [1] {ECO:0000313|EMBL:OKJ89574.1, ECO:0000313|Proteomes:UP000185813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSRI0107 {ECO:0000313|EMBL:OKJ89574.1,
RC   ECO:0000313|Proteomes:UP000185813};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OKJ89574.1}.
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DR   EMBL; LIVZ01000002; OKJ89574.1; -; Genomic_DNA.
DR   RefSeq; WP_073939439.1; NZ_LIVZ01000002.1.
DR   AlphaFoldDB; A0A1Q5L6F5; -.
DR   STRING; 1703942.AMK31_06570; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000185813; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
PE   4: Predicted;
KW   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185813}.
FT   DOMAIN          508..823
FT                   /note="Malonyl-CoA:ACP transacylase (MAT)"
FT                   /evidence="ECO:0000259|SMART:SM00827"
FT   REGION          313..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   858 AA;  91615 MW;  441836642C8DA7D3 CRC64;
     MDRVPMRLVC FHHAGGDASL FSGWQHRLAD DVEVVPVTLP GRGGDQRVED LNELVDRLEE
     SLTPLLNGPH LVYGHSFGGL VGYELVRRRA ARGLRAPEAL FVGAFPAPDV AHTLDSLELD
     EDSLIEFMLE ISGMPREVLA YPDWVDSVTA SLREDLLLWR THRDEPGSRI PCPIHVFSGT
     EDWLVPRDHM AGWADRTTAT YRLHQVDGGH FFVRENRAEF LELLRTVLTP YTAAPAAVPS
     PARVHSLASP FRGFGTRRAV PMPFDAAAFT LGPGTPVSGR DSVLATTAWQ LLERVMIPPA
     STRGRQVGVF VERSLTPEAG DGDDGRPGGA GRSAARLSAT YGWQGPVGAP DAGTSPGRAA
     LAAAHRALRR GECDLAMAAA APDTWAEEPL RILRRQEAGH ADRPAPSASG EPATAPRALP
     WVLSAHDAPT LLRQADRLRT YVTEHPDLDL GAAAYALAAG RTPLAHRAAL VAADRSEVLA
     GLEAIADDGF AVNVVPPARA ADEPTAFLFT GQGSQRPGMG RELHAEYPVF AAALEEIAER
     FDRHLDQPLL DVMFAEQGTE QSDLLNLTLY AQPALFALEV ALFRLVTDWG LTPSQLIGHS
     LGELVAAHVA GVFSLDDACD LVAARARLMQ SAPAGGAMIA VAADEATVTR ALERHGDGRV
     DIAAVNTATA TVISGDEEPA GAVAAALAEE GFKTTRLRVS HAFHSLHMEG ILEEFRTVAS
     KVDYHAPRIP VVSNLTGMRA GDDELGDPDY WVEHIRRPVR FAQGIGWLAG KGVTSFLELG
     PSPVLSAFAR MAAPEGGFAY ALRPGLPEGA TLSTAVATLF TRGAQPDWEA VFGPAAEPGA
     ARRAAADLPA YPFPAADH
//