ID W4V1U6_9FIRM Unreviewed; 1327 AA.
AC W4V1U6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Long-chain-fatty-acid-CoA ligase {ECO:0000313|EMBL:GAE86714.1};
GN ORFNames=JCM21531_35 {ECO:0000313|EMBL:GAE86714.1};
OS Acetivibrio straminisolvens JCM 21531.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=1294263 {ECO:0000313|EMBL:GAE86714.1, ECO:0000313|Proteomes:UP000019109};
RN [1] {ECO:0000313|EMBL:GAE86714.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21531 {ECO:0000313|EMBL:GAE86714.1};
RA Yuki M., Oshima K., Suda W., Sakamoto M., Kitamura K., Iida T., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequence of Clostridium straminisolvens Strain JCM 21531T,
RT Isolated from a Cellulose-Degrading Bacterial Community.";
RL Genome Announc. 2:e00110-14(2014).
CC -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004789}.
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:GAE86714.1}.
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DR EMBL; BAVR01000001; GAE86714.1; -; Genomic_DNA.
DR STRING; 1294263.JCM21531_35; -.
DR Proteomes; UP000019109; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
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; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:GAE86714.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019109};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 473..548
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 585..1009
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 1327 AA; 147187 MW; 659301FBAEFB85A7 CRC64;
MAHLLKSKGV KPESIVGIML ERSMEMIIGI MAIEKAGGAY LPIDPHYPED RINYILEDSG
VSVLLTSGKF HDMNIQGNIQ RIFLEDKSLY QGESNNPANA VLPNSLAYVI YTSGSTGKPK
GTLIEHHSLV NRINWMQKKY PIGPNDTILQ KTPFTFDVSV WEMFWWSTQG AKVCFLEPGG
EKDPGKILEA IEKNNITVIH FVPSMLNIFL EYLKETGQAQ RAKSLRQVFA SGEALTSQQV
KLFNSLLGTN GTRLSNLYGP TEATIDVSYY DCPTDEVPDI IPIGKPIDNI QLLIMDKNMQ
PQPIGVPGEL CIAGVGLARG YLNRPELTSE KFVASPLVPC KRIYRTGDLA RWMPDGNIEY
LGRMDFQVKL RGLRIELGEI EGALLSHPSV KECVVTAWEK EPGNVHLVGY IVCDKENPVE
SGELQAFLAK SLPEYMVPRI YVFLDALPLS SNGKADRKAL PVPVLSKESN YAAPQNEVEK
ILADIWKEEL GLESVGVNDN FFEVGGHSLL LTKIHSRIKK QFNKDFPLVD MFTYSTISSL
AKFIKGEQEQ PSFVKNEERL RKQKQARQNK FGNFDCCELP KNKSSGCVAI IGMSGRFPGA
KNIDEFWENL KNGVDSITTF SKEEAIKSGA SDEDVNDPNY VLAGGILEDI EYFDASFFGF
NPRETENMDP QHRLFLECAY EALENAGYAK NEYEYPVGVY AGSNMSTYFL YHLMAKVGLK
DNFNMLLSND KDYLASRVSY VFNLKGPSIN VQTACSTSMT AIALACEGLL NYNCDMAIAG
GAAIKLPQKL GYLYQPGMIA SPDGHARPFD ADAQGTVFTN AVGVVVLKRL EDAIADGDNI
YAVIKGIAVN NDGSTKAGFA APSREGQSEV IAAAQSLAGV NPDDIGYIEA QGTSTLFGDQ
IEVDALNKVF SQKTQRKNFC ALGAVKGNVG HTTSAAGAVA IIKTALALKN KQIPPTVNYK
TPNPNIDFEN SAFYVNTKLT EWESNGKPRL AGINSFGFGG TNVHAILEEA PEIETSAKSR
SHQLLTLSAR SKTALDRMAH NLGEFLKKNT DINFADTVYT LHVGRKEFEH RRTLVCKNAE
EAICLLLNEN RESSLCDFSG GTNPSIVFVF AERERLKPNT AIELYNNFDV FKEEFNRGAE
ILKSYLREDP VGILFSQDTP KNLSEKYLND KKISRSINMI IEYAMAKLWM SWGIKPYTAI
GKGIGQYTAD LTRGVLSLED ALIRAFSDDG SGSYGSFDNE IETLAKDNTV IFLHMGVPFE
LKDAHSAKVF LSLPGEESNQ SEVQTVLYTL GKLWEKGFKI SWEDFHSGEK RRRIPLPTYP
FERKKYW
//
