ID D8FWT7_9CYAN Unreviewed; 1311 AA.
AC D8FWT7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Multifunctional peptide synthetase (Modular protein) {ECO:0000313|EMBL:CBN54827.1};
GN ORFNames=OSCI_1100006 {ECO:0000313|EMBL:CBN54827.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN54827.1, ECO:0000313|Proteomes:UP000004532};
RN [1] {ECO:0000313|EMBL:CBN54827.1, ECO:0000313|Proteomes:UP000004532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6506 {ECO:0000313|EMBL:CBN54827.1,
RC ECO:0000313|Proteomes:UP000004532};
RX PubMed=20675499; DOI=10.1128/JB.00704-10;
RA Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.;
RT "The genome sequence of the cyanobacterium Oscillatoria sp. PCC 6506
RT reveals several gene clusters responsible for the biosynthesis of toxins
RT and secondary metabolites.";
RL J. Bacteriol. 192:5264-5265(2010).
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:CBN54827.1}.
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DR EMBL; CACA01000106; CBN54827.1; -; Genomic_DNA.
DR Proteomes; UP000004532; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR013217; Methyltransf_12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR041464; TubC_N.
DR InterPro; IPR044894; TubC_N_sf.
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; PF08242; Methyltransf_12; 1.
DR Pfam; PF18563; TubC_N; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000004532}.
FT DOMAIN 22..71
FT /note="TubC N-terminal docking"
FT /evidence="ECO:0000259|Pfam:PF18563"
FT DOMAIN 86..542
FT /note="Condensation"
FT /evidence="ECO:0000259|Pfam:PF00668"
FT DOMAIN 562..915
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 981..1022
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT DOMAIN 1096..1193
FT /note="Methyltransferase type 12"
FT /evidence="ECO:0000259|Pfam:PF08242"
SQ SEQUENCE 1311 AA; 146384 MW; 118769420EAAC3FD CRC64;
MPEPKMSSLP PQVGDSVKEG LVEFLSRLRS LDINIFIEGE TLRCNAPEGV MTAEMRAEIL
NKKSEIISLL KAANSTTTNL VPVSREGIIP LSFAQQRLWF MDKLVPNNPF YNVPAAVRMT
GAVDFGALQQ SFDEIVCRHE ALRTTFAVVN GQPVQKIAAA VNVPIALLDL RNLPSAKREI
EAQRLITEEA QRPFNLSVCP LLRVTLLQLD ATEYLLILNM HHIVSDGWSI GVLVQELGAL
YPAFASKKSS PLRELSIQYA DFAGWQRDRL QGDVLETQLT YWRRQLEGIS MLNLQTDRPR
PAVQSYRGKR LFLQLPKQLS EALEAFSQRE GVTLFMTLLA AFQTLLFRYS QQPDIAVGTP
IANRNRSEIE SLIGFFVNSL VLRTDLSGNP TFRELLNRVK EVALGAYAHQ DVPFEKLVEE
LHPDRALNQN PLFQVVFALQ NAPADKLELP GLTLRPQQLD AGTARFDLEF HLWERSPDNK
LWVDCADGIS GFVIYSADLF DEATIVRMLG HFEMVLSSIV ANPDAQIANL EILTDAEREL
LLVKWNKNQI NYPKGLCLHQ LFEIQAEQTP DAIALVFGEE KISYRELNIR SNKLAHYLQK
IGVGAEVLVG ICVERSPDAI VGMLGILKAG GAYLPLDPTY PRDRLNLMLE DARVPVVLTH
QGFKLQANSE SRSESGETYN PIVVDLDKSG ESSDRENPDC AIAPVAAENL ACVIYTSGST
GKPKGVQIEH CSLLNLIFWH QQEFAISACD RASQVAGIAF DAFGWEIWPY LAAGASIYFA
DDDIRRSPDR LQEWLLSNEI SVSFLPTPLA EQVLLLDWPA DSALRILLTG GDKLRQYPSA
RHPFKVVNNY GPTETTVVAT SGTIPVREQA DTAPDIGRAI ANVQVYVLDK YLQPVPVGVA
GELYLGGCGV ARGYLNRPEL TQEKFIPNPF TIQSELKQPR EHSQLYKTGD LVRYRNDGNL
EFLGRLDEQV QIRGFRIELG EIESVLAQHP AVQQTVVMAS QDGEGEKRLV AYVALNPECN
LAEETDIQQL QAEQVLQWQM LYGETYKQPA SGTDPTFNIT GWNSSYTGEA IAPEQIREWA
NNQAAQILKL QPDRVLEIGC GTGLLLFQIA PHCTQYWGTD FSPQSIDYIQ QHLRDRDLAN
VTLLPKMATD FDGIEAATFD MVVLNSVVQY FPSLDYLLQV LEGAVKAVAP GGSIFIGDVR
NLPLLAAFHA AVELYRSPPS ATIEQLQQRV QMQIFQETEL VIDPDFFRAL KHQFPQISDV
EIQLLRGTFH NELTQFRYNV ILHLAGEIDS ANPPSVPPLV RGEGERKKRY G
//
