ID R7ZIG8_LYSSH Unreviewed; 1450 AA.
AC R7ZIG8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Pyochelin synthetase F {ECO:0000313|EMBL:EON73878.1};
GN ORFNames=H131_04414 {ECO:0000313|EMBL:EON73878.1};
OS Lysinibacillus sphaericus OT4b.31.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1285586 {ECO:0000313|EMBL:EON73878.1, ECO:0000313|Proteomes:UP000013911};
RN [1] {ECO:0000313|EMBL:EON73878.1, ECO:0000313|Proteomes:UP000013911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT4b.31 {ECO:0000313|EMBL:EON73878.1,
RC ECO:0000313|Proteomes:UP000013911};
RA Pena-Montenegro T.D., Dussan J.;
RT "Draft genome of the heavy metal tolerant bacterium Lysinibacillus
RT sphaericus strain OT4b.31.";
RL Submitted (APR-2013) 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:EON73878.1}.
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DR EMBL; AQPX01000008; EON73878.1; -; Genomic_DNA.
DR RefSeq; WP_010857847.1; NZ_KB933398.1.
DR PATRIC; fig|1285586.5.peg.894; -.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_000022_2_15_9; -.
DR Proteomes; UP000013911; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic 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; cd19535; Cyc_NRPS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 1.10.10.1830; Non-ribosomal peptide synthase, adenylation 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; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR041464; TubC_N.
DR InterPro; IPR044894; TubC_N_sf.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR PANTHER; PTHR45527:SF15; PYOCHELIN SYNTHASE PCHF; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR Pfam; PF18563; TubC_N; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
FT DOMAIN 1029..1113
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1450 AA; 166860 MW; 64BA1B5F0B19189D CRC64;
MNKTLKHFKN EIYKLKAQGI ELWTSDGKLN FKAGKHQISE EIMTFLKTYK DELMDVLEQE
GQDNTFPLTP IQSAYLLGSM DSFEYGGVSS HIYMELEYLH LDKEKVEHVW MSLIDRHEML
RTTINHNGYQ GELEQMPKLE IYYEDLTTNG VDDWNRLDAI RQQLGSKRYS PDCWPLFDIA
LSKRMHGTTM HISFDFLIVD WASIWILIKE FEVLYFNENA TLPNNDFTFK EYVKLEEERS
YQEKYKEDKA YWYHRVLDLP TSPTLPKLPL SQDEKSFERY FIQLEKNDWD KLKLAIANKG
ITATSVLFTL YSQCLAKWSV NKHFIINLIL LNRLPVHPDV NHIVGDFTSI NLTEADFRNA
QAPFINNVNT IQQQMFRDLD HSSFSGVEVL REITRQKGQT HAFMPFVFTS AINLIDSHGL
IGKMNEYGIS QTPQVFIDCQ VMDDDNGLRV NWDVRKGVFP ANLIQDMFLS FETALKRLVH
DDKAWESTAL VTLPKQQIKQ RESVNFTKNT NERKRLLHQG FFDQAWKQPN KIAMIEGNHH
HSYQDLRVMV FKLGTLLQKH QVKEGDKVAI ISDKPVYQVT SVLAILSLGA VYVPIDKAQP
ISRIKKIIDQ SQVTAILIDE RNSMYDCLDW RLIICSQLEE VKTTSAYDVY KGDPDTLAYI
IFTSGSTGEP KGVAMSHAGA MNTIQDINRR FCMTSNDRVL ALSKLHFDLS VYDIFGLLSV
GGTIVYPEQE HLYDASYWLE CIRTKNITLW NTVPALMKML LSSVDEIEQI NIKTMKTILL
SGDWIPPKMV KHCSTVFPES SIVALGGATE AGIWSNYHLC CEEDFVRETI PYGYPLANQR
FYVLDEKDED CPNWVRGELY IGGESLALGY YNNPQLTKER FITNIKQERI YKTGDFVRYM
DNGEIEFIGR LDNQVKLRGN LVNLGEIESL LNKYERIDTS CVVVLDDTHL YAVVKLVNHD
SQSIIHSNDL IDYLANLLPQ YMVPVKIFIV AELKLNANDK LDRQFIKNHV QQLVAECTKD
DEIGVKQTGM ENQLQQTLIH FATEVLNVEH IQVSKNLYDY GADSLTLSQL AGKIKKTIEN
DNQYQDITFD FILRQLLNEP IIESIAQKLN QSAARETNGS EQIGELNSSQ SIGLLKEESF
SYGDPLRIVV HAGLGTMNAF QYLNKHLAKQ GVGTVVSISV QDINKYLAID SSVLIDCLAD
DYVLQIMDRE PSQVQLIGYC MGGLIALEIA RRLMERGVEI IDFTLIDSAP VLYEIEDSIP
LELIFITNFY ITVEDVYEGA SNNELMDAIM YVFYQNNESL SASNLEELKN EPKYETIYRF
LKKLSQLSRK QRFKDYKAVI EQKTGQIIAD EMLEGYYNIY LQSFKGSNIR PMAYFGDIRY
LVAKEDMDFI FTNKQDTLKF WKELCIGDFE ETSIEGNHIT CIEDDENACK VAEKLLEPIN
KLMGSINRHE
//
