ID   D3W8L4_9BACT            Unreviewed;      1518 AA.
AC   D3W8L4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   13-SEP-2023, entry version 48.
DE   SubName: Full=Putative non-ribosomal peptide synthetase {ECO:0000313|EMBL:ACX33963.1};
OS   uncultured bacterium RM35.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=672207 {ECO:0000313|EMBL:ACX33963.1};
RN   [1] {ECO:0000313|EMBL:ACX33963.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20081001; DOI=10.1128/AEM.02169-09;
RA   Craig J.W., Chang F.Y., Kim J.H., Obiajulu S.C., Brady S.F.;
RT   "Expanding small-molecule functional metagenomics through parallel
RT   screening of broad-host-range cosmid environmental DNA libraries in diverse
RT   proteobacteria.";
RL   Appl. Environ. Microbiol. 76:1633-1641(2010).
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GQ869385; ACX33963.1; -; Genomic_DNA.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd19531; LCL_NRPS-like; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR029058; AB_hydrolase.
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; IPR020806; PKS_PP-bd.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          116..191
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1159..1234
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          94..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1518 AA;  165374 MW;  72223A53482FD8A9 CRC64;
     MLDVDQQLTL TIPFGGVGVS LEATCVWAAQ GRVGVRVTSE SARIAELARR VQSIAEERGF
     TPRALREYLA QRIPEYMVPS VVVPLDALPV TSNGKVDRKS LPEPRSEASA GLHAGVPRTP
     LEAALTRIWA DVLDVAAVGP NDDFFALGGH SLLAIKVAAR VRETLGVEMP IRMLLEARTP
     GALADRLELD GGRARLPRVE RLTHPEGRVE LSYGQERLWF ISKLAPESTA YHGGFILRLV
     GELDEDRLEG AFSAVVARHE ALRTGIVDEE GRPAGRVMAP KEVTLLRQEV ADEPALRQRV
     SEELRRPFDL GVEPLFRTRL YRLGPEERAL VVGVHHAAWD GWSAGVMLRE LSAAYAGREL
     PPLEVQYGDF AAWQKRWLSE ESLHEQLIRW KERLRGAPLV SSFPMDRPRG TVKSSVGKVV
     KFQIPNQVVD GIHRLSRVEG VTPFMVVLAS FQVLLARTTG QRDVCVGTPI AGRRSAEVEG
     LIGFFVNMLV MRLNLEGEPT FLEVLSRVKE FALEAYADQD VPFERLVAAL QPPRDTSTSP
     LFQVGVAWQN ALTGARLELE GVKVEEIALD DVPAPYDLML EIVEGEAERG LHGRLTYDAA
     RYDRETIERL GTHFVTLLSA AVERPESGAR HLPLLDPEER RRIVDGWNET ARERPKAATA
     GECFEQRVAE GPARLALVSG AEEVTYREID RRANRLARYL TRKGVGPEIR VGICLDRSSE
     LIVAVLGVIK AGGAYVPLDP AYPRERLAWI VRDAGIEVVI TKAEVWRAVG LDGSDVVRLD
     EDRLAIEKES EAPTPTRVGA RNLAYIIYTS GSTGTPKGVM IEHGSLCNLI AREAEELALR
     PGKRVLQFAS PSFDASVWEL FGALGTGATL CLAPREALLP GPPLAETLRQ LQVTTATLPP
     SALRLLSPDG APSLELVVSA GEACSDDLIS AWMAGRGFIN AYGPTETTVC ASLWHARSGD
     PSSIGTPLGN CRIYIVDAEL EPVPVGVAGE LVVGGAGVAR GYLGRPTLTA ERFVPDPFSR
     VPGERMYRTG DLARWRADGQ IEYLGRIDDQ LKIRAFRIEP GEIEAALREH PDVTDAAVVA
     REVTRGGEKQ LVAYVVGQDG VASARGALRD FLRGRLPEHM VPSRFVSLPN LPLTPNGKVD
     RTALLRSEQR DEAAVPSSAA RDAVELRLAA LWEDLLGIRP SSPGENFFDA GGDSLSLVRL
     VFSISEQFGV ALPLSQAHAQ PTLEALAEGI RQHLDSSASG VSVHLPLAIP LRHGDGSQHP
     IFLVHPGMGE VVAYQELADA LPPSRAVWGI RGHGLYGTER VAATLEEQAR HYLGAVREVQ
     PRGPYLLGGW STGGVLAYEM ARQLQAEREE VAWLGLMDTV TPDAPALQSI DTSRLPLEVI
     LDIGKRFSLP VTARLAAASS LEEQRLELMQ AAHTAGMSES LARFVIERVS GFFVDLHRLV
     HAYRPRDVFA GKMTLFRVAG ANLGAGVLDA YGWQRLVASP PTIVAIPGDH MTMMSRPHVL
     ALAEAIAVTL EHLAKSSV
//