ID   A0A0M1NIW2_9BACL        Unreviewed;      1492 AA.
AC   A0A0M1NIW2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Thioester reductase {ECO:0000313|EMBL:KOR82042.1};
GN   ORFNames=AM231_20990 {ECO:0000313|EMBL:KOR82042.1};
OS   Paenibacillus solani.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1705565 {ECO:0000313|EMBL:KOR82042.1, ECO:0000313|Proteomes:UP000036932};
RN   [1] {ECO:0000313|Proteomes:UP000036932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-22460 {ECO:0000313|Proteomes:UP000036932};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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:KOR82042.1}.
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DR   EMBL; LIUT01000005; KOR82042.1; -; Genomic_DNA.
DR   PATRIC; fig|1705565.3.peg.119; -.
DR   Proteomes; UP000036932; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd19534; E_NRPS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
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_com.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR010060; NRPS_synth.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   NCBIfam; TIGR01720; NRPS-para261; 1.
DR   PANTHER; PTHR45398; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR   PANTHER; PTHR45398:SF1; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 2.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036932}.
FT   DOMAIN          953..1027
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1492 AA;  170006 MW;  4537095A759CBCD6 CRC64;
     MEAGKLYPLT HPQKRIWYVE NIYPGTSIHN IGGLIKIYGP VDFTLLEEAI NQFIRLNDAV
     RIRLVEQAGS VHQIVTEYRR RTFPLIDFTV LESDVDAWVN AEFARPLALD GERLYDFVLV
     KVSDTESAYL TKFHHIISDG WSFQLMTTHI NQIYTQLMEG EEVRQEPRPT YLDYIGQEQK
     YLSSPRFMKN QSYWNQKFDH IHDLELHNTS IGTAGNRKKF LISRSTSGAI HDFAQTHHIS
     LNTFFVATML LYLHKANQQN RLLIGTPVLN RTGAKEKNTF GMFTSTMPFL IDIEHEMSFS
     SFIHNVNQEL IQCYFHQKYP YNLLIQDLQL QQRGLDQLFQ VCVNYYNTAF DRSFGPGWKM
     QQIEVNNGNQ LYSLQLIVTE WSSDKELELY FDYKEGDYTE RQIDELYNRF LFLIDQVLSR
     PDAALHNVEL LLPDERAKLL YTYNTTDCEY PSHQTILQLF EEQVERNSER IAVSCMGQSL
     TYGELNERSN RLARTLLERG ISPHTPVAIM GRHSLSIVVG IWAVIKGGMA YLPIDPEYPK
     ERIEYILRDS RASLLLTHGM EWEQLSYNGE VLALDDERLY NKDGSNLPVK VSPDDLVYII
     YTSGSTGNPK GAMIEHRGLL NYIWWAGKTY VRSQNDVFAL YSSIAFDLTV TSIFTPLISG
     CRIEIYEDDG SDFIVKRIVE DNKATIIKLT PAHLALIKDM DFREHTVRTF IVGGEDLKCS
     LVRDIHENSR GGIEILNEYG PTETVVGCMI YRYDPASDEG VSVPIGQPID NMQIYLLDRQ
     LEPVPNGSIG EIYISGAGVA RGYLHREELT QDRFLPNPFL TGNRMYRTGD LAVRHDSGSI
     VYLGRIDHQV KIKGYRIELG EIEHQLLEMN GIEEVVVIDR TGEDGQQQLA AYYVAEGHLT
     ALELRMKLAE VLPSYMIPAY FVRLDQLPLT PNGKVDRRLL PAPEQYQETS EAGTTSGVEA
     LLMNIFKDVL RTDEIKVQDN FYRLGGDSIK AIQIVSKIKA AGYQLKVQQI MSYPVIRELA
     EFIELNTAAP IEQGPSCGEV KPLPITSWFF SRQWNNPHYY AQSVLLRLTP EITRDQLQDA
     LYALIGHHDT LRLQVDETPG RLVYRTVGRE DVELAHFDLT SIPEEKRAAV LKKQAESFKA
     SVRLGQGLLF KALVFDKGNQ GQRLLLTAHH LIVDGVSWRI MLEDLDQLLK AALTGSVWSL
     PNKTDSIQTW SDAIDAYGCE KALEHLDYWH SVLEKTENSL ETDYPSDDDR IAVCDTLVQD
     LSEQETSRLL GEANTAFRTQ TSDLLIASLA MAVSDITGKN KFSIELEGHG REELFENVDV
     SRTVGWFTSL YPVNFEMTET RTAEIIKSIK GRLRSIPNKG IDYGILAYGS GDIPKMGGNL
     LRFNYMGEID NLLHSPVLAI SGDDTGRETC PSNRLSCLVN VVAMITDKRL QIRMTYSTAM
     FSRDTMNAFI QVFMQRLAEV IQLGSDRGQT DFTPSDFETV KLAQEELDIL FN
//