ID E7AYA8_PAEPO Unreviewed; 1102 AA.
AC E7AYA8;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Polymyxin synthetase B {ECO:0000313|EMBL:CBY05532.1};
GN Name=pmxB {ECO:0000313|EMBL:CBY05532.1};
OS Paenibacillus polymyxa (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1406 {ECO:0000313|EMBL:CBY05532.1};
RN [1] {ECO:0000313|EMBL:CBY05532.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M1 {ECO:0000313|EMBL:CBY05532.1};
RA Niu B., Vater J., Rueckert C., Chen X., Blom J., Lehmann M., Puehler A.,
RA Wang Q., Borriss R.;
RT "Polymyxin P, produced by the plant growth promoting rhizobacterium
RT Paenibacillus polymyxa M1, is the active principle in suppressing
RT phytopathogenic Erwinia strains.";
RL Submitted (NOV-2010) 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}.
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DR EMBL; FR727736; CBY05532.1; -; Genomic_DNA.
DR AlphaFoldDB; E7AYA8; -.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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; cd17643; A_NRPS_Cytc1-like; 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; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 1.10.287.490; Helix hairpin bin; 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; IPR001242; Condensatn.
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; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00824; PKS_TE; 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; 1.
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}.
FT DOMAIN 778..853
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1102 AA; 123178 MW; CE77B5F0F606B20D CRC64;
MKSLFEKEER YWSGKFDADD SLSFLPYSQS SKLSADGEAA AEPGLLHRTL PSELSERIIC
LANGSDLALY MIVLAGVKSL LFKYTGRDQV LIGMPSYSAD PDGTPPPHDI LVIKTSVSRQ
TTLKTLLGGI KASIGEALEH QHLPFRKMVE PLHLDYTGDG LPVVNTVASF ASIHPEPLVN
RVAADTVFRF DRQNHSIELE ISFDGQRYER AFVEQAADHL VRLLSVLLFQ PDLELGQADV
LSPDERETLL KRFNDTETEF ERGKTIYGLF EEQAELYPDN VAAVMNERQL TYRELNERSN
RLARKLRETG VEADQLVAIL AERSLDMVVG ILAILKAGGA YVPVDPDYPE ERIRFMIEDS
GAPLLLIQKH LHEKTNFAGT RLELDDFVWG DRGADSADAL DASNLEPISG PGNLAYVIYT
SGTTGRPKGT LIEHKNVVRL LFNDKNLFDF GPSDTWTLFH SFCFDFSVWE MYGALLNGGK
LVIVPPLTAK NPADFLALLG REQVTILNQT PTYFYQLLRK VLADHPYDLR IRNVIFGGEA
LSPLLLKGFK TKYPETKLIN MYGITETTVH VTYKEITWVE MEAAKSNIGK PIPTLRVYVL
DENRRPVPIG VAGEMYVAGE GLARGYLNRP DLTAEKFVDS PFAEGEKLYR SGDLAAWLPD
GNIEYLGRID HQVKIRGYRI ELDEIETQLL KIAAVQEAKV LDRDDANGHK QLVAYYVAET
RLAANELKEE LAKQLPGYMI PSHLVQLSGM PLTPNGKIDR KALPAPEEAA AGGAEYVAPR
TLLEMKIARV WQDTLGVPQV GVKDNFFELG GNSLSLMRLV QAVYDETGIE IPLNRQFHNV
TVEAMAFGES DLGLDKGGNS FIKLNKAGDL NVFCFPPGSG FGIGYRELAS RLDGRFVLYG
IDFIDDAVDY EAMLNRYVDE IVRIQSEGPY VLLGYCFGGN LTFEVAKTME KRGYSVTDVL
MVDSWIKDAL TPSETSEKEL EEMLADFDEE EKELMSNPLV RERVHRKVKA TLAYEAQLIN
SGTIPARIYE LIAKDSEAFR LEHQLPSWRG ATTQAYSDYR LEGAHEELLE LARVEETAVV
IRDILEQVKR QIEAEAGVLH GS
//
