ID W4V1U1_9FIRM Unreviewed; 1292 AA.
AC W4V1U1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Long-chain-fatty-acid-CoA ligase {ECO:0000313|EMBL:GAE86709.1};
GN ORFNames=JCM21531_30 {ECO:0000313|EMBL:GAE86709.1};
OS Acetivibrio straminisolvens JCM 21531.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=1294263 {ECO:0000313|EMBL:GAE86709.1, ECO:0000313|Proteomes:UP000019109};
RN [1] {ECO:0000313|EMBL:GAE86709.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21531 {ECO:0000313|EMBL:GAE86709.1};
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:GAE86709.1}.
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DR EMBL; BAVR01000001; GAE86709.1; -; Genomic_DNA.
DR STRING; 1294263.JCM21531_30; -.
DR Proteomes; UP000019109; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR CDD; cd08953; KR_2_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 1.10.1240.100; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR049490; C883_1060-like_KR_N.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF21394; Beta-ketacyl_N; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Ligase {ECO:0000313|EMBL:GAE86709.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000019109};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..155
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1171..1246
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1147..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1258..1285
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1148..1171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1292 AA; 144772 MW; 4D999B363A58A142 CRC64;
MKVGYTAPGI EGQAGAISEA HLKAGVDPET ITYIEAHGTG TPLGDPIEIE ALKQVFGKTT
QKKGFCAIGS VKTNIGHLDA AAGVSGLIKT VLALKNKIIP PSLNFKKPNP KLNIHDSPFY
INNSLKEWKS NIGPLRAGVS SFGIGGTNAH AVLEEAPVVD SDICKNDETL LVFSAKTRSA
LDKMTYEFVD FLKKNSDINM ADAAYTLQLG RKEMEHRRFV VCKSREDAIY ALENIDSIPK
RVFDSIEGQN GEERFMEVNP KDYTLEQLGH LWLKGAKIDW GVLYEGTKRR RIPLPSYPFE
GKSYWVDGVK KNKEAEVKGK ISDISKWFYA PVWKQSAKGG LSKSTKYVNA NDVILILTKD
SSFCDSLIKR VKHSNENIIV AKAGESFGKM GDRDFLFRPE QKEDYDSLLK EISKLSNKPD
IVLNLLGVTE DGSNTEDTNG VRCGKQLFYS LVYLAQAFGN QGWNTPVQFK VFTDNTFKLF
NEKTLYYGKT LAVGPCKVIP REYPNIRCSI VDFELQHGES LQQHDIIECF VSEIYEKDTE
LITAYRGLER WIQTFDGTQV EESPDSLLKK NGVYLITGGL GGIGLNLAEY LAKEVQAKLI
LVSRSEFPEM DKWQDWLLEY GKNDSISRKI NKLGTLQNLG SEIMVCKADV TDTKQLEVIR
HNALNRFGRI DGIIHAAGNP GGGMIQMKTK EFCENVLAPK VDGTLALYET FMSSELDFFI
FCSSLNAITG GFGQVDYGAA NVFLDSFAKA HDSYRGTRFI SINWDRWPGV GMAGGTGQKI
DEGEPAVHPL LGKKVLATSE KKVYLAEFSP SKDWVLSEHL VMGIPTIAGT TYLEMARAAY
KEMTSKDSMQ ISDVIFLTPM VVRQDEAREV FTILTKSGNE YDFQVASKLK GAKEEAIWHE
HVRGKIKPLE EENAKQFDLE EIKARCFSKM EISKAQGDKT KEFISFGDRW KSLKGFDLGE
NEGLVEVELA DEFIGDLKDY ELHPALLDVA TGSVRLASGG NFLPFSYEKL TIDRPLPGKI
YGFIRFKNGY SAKQDIITCD IDIMNDKGEQ IVEICNFSMR LTDDDAAKNI RERISGQQKI
GKTAFDDLYK IAVKKESGFL NNGISESEGK EVFRRIVNGL CKSQIIVSVK DLNTAIEQAN
YINQQGMKKE AYEKDSRPKH PRPELDNDYV PPKNDIEQKL ADIWQETLNI EAVGIHDEFF
ALGGDSLLLI QLHSKIKESF STGLAVVDLY KYNTIASLAK YLSSENKEEE QPVFQSVSER
SNRQLEAMKQ KRQEMKLKRQ QMKQIRGVVK VD
//
