ID C3XS40_BRAFL Unreviewed; 1705 AA.
AC C3XS40;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE RecName: Full=Fatty acid synthase {ECO:0000256|ARBA:ARBA00018769};
DE EC=2.3.1.85 {ECO:0000256|ARBA:ARBA00012873};
DE EC=3.1.2.14 {ECO:0000256|ARBA:ARBA00012480};
GN ORFNames=BRAFLDRAFT_71891 {ECO:0000313|EMBL:EEN69508.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN69508.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN69508.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN69508.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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DR EMBL; GG666456; EEN69508.1; -; Genomic_DNA.
DR RefSeq; XP_002613499.1; XM_002613453.1.
DR STRING; 7739.C3XS40; -.
DR eggNOG; KOG1202; Eukaryota.
DR InParanoid; C3XS40; -.
DR GO; GO:0016297; F:acyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
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; cd05274; KR_FAS_SDR_x; 1.
DR Gene3D; 3.40.50.980; -; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR036736; ACP-like_sf.
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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR001031; Thioesterase.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF47; OLEOYL-[ACYL-CARRIER-PROTEIN] HYDROLASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00823; PKS_PP; 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 SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 359..435
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1559..1586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1705 AA; 189616 MW; 88B5D0F553070BDE CRC64;
MADNIQQLLS KFDKSDNSLS SLIPSVQTNM DLSSLSKILH HQQKGLKMPD IVTVDDREVQ
LGLDIKQNQF KAVDKATYIV TGGLKGFGLA LLEWLAKCGA CHLVVLARSE PTEEAKIKLE
ALSSRSVDVR VLKVDVTDKK AVEEALTWAR DTMPQIDGIF HCAAVYADKL MDQTAQEDWE
RVMHPKAVGA IILHDATKKL HARLKHFVLI SSVVALLGNT GQAGYCAANS TLIALGEARR
HEGLPATVAS FGVINTVGFA ERSGLIQMWE RMGLQSVSPQ DALEILGCMM ENQYPHFGIS
TAFDIRKYCS THKSLTLQHL QAADTCFSRF TTLIPNDVLS GSVSLSEKVV TSTKNNGLGI
IKEELIAYLC QQLGIEDSAE IADETSPVSL GLDSLLSVNM SNEITDKFEV TVTSVELLSD
KMTVQMLSET IYDKMANLAG SQGIATSSTN PVVTAEGNAW LHFFGKLQNP ILTVVCFPAN
GGGPSLFHQW GEHFSKHNIE VVTATLPGWE SRERESPISS LQQIVEALGS QIMETLMNDK
MAFYGHSMGA LIAFEVAHFI HTKGNRCPSH LFVGGWYAPS LPYPHPQELR VSPALFDPLT
GTQQVMEKAK TFSFLPEGVV NNPAHLRRLL PCLQAGIEIC KSYICEHTES LPCRVVALGG
QNDPFVSPDH LDNWELVASD SPASEPAFRK LIVQGGHFFI TTSRQDVLNK LTRVLQEDNV
IIKPSFKSQQ NAPEVFSMET KPSPALAISA LSPVKSAPVI HKAAAYLRYQ IKHPTFYTKN
LYIMFRTQNI PADVDSWRSV FVQLMDRHET LRSTYHASSD VQHPSGAEAR YYNTIAGFEV
LTGYQEKQAE EAVYQRTKVP FQLDKEYPAR CIVAPTGKRS AVVGLVLHHI ATDSTSFNIL
FRDFGEIMRA HFKKKTLQKP MTTLTYCDFI QYYYSYLQQN QNELQDFWRA ALPPTIPSIN
LSFAKPRPPT LCTEGGSLQV DLSKEQVHGI KEYAKSIGTT VYSIIATTYQ LLLHIYTAHD
DIVIACPFDM RMLAPQFSHI HGLCQHHLPL CASFKNKEQP YRQVLLQSFY KLQECKKHGI
YPIDEIMKLV SYEKHPTMDP IMQHIVVQND QTDLNKMSND KITILKNDYH DYANDFVLHL
FQDTNTKSVS CSVRYAKSLF DEEVAQCMVN DYVTLLSTCL KNPEWSLSKI INSLEMTALN
CSPGAVHSMN DDHQDRVNGR PMQEETIHGY FQLQAARTPA SRAVSFNGTE ISYRSLDEQS
DHLASVLIGM TSSERSEDDV LHGCTLNIDH IWDEARDNSS TGTCPTEVSK YAFVMTTVTT
PARLVRGTHA GLLNRLKSTW QEFPHQVTDV CCLKSPLAGR VDAMLELFGP LLQGVPVVII
PTALLLNPAQ LLEFISMCNI TRLSGVHDRF WNALLQELHG TARRKRWKQL SLKYVFTDAG
STKSSTLIEL SRALSHATIV STYSTLEVYS GGLIASGTKS APFNRDKIPM KPMDSTKVTV
LADSENGHGT LCISVPELSE NVEEFPALTI VKDGIPYYIT ERQASVTPSG MVLLAKECEN
GDSKEGSSRS SSPVPRQLIT SPDEPHALND GLLQMLQKGT TVRKMTSKGW AHRRLLQLVV
ENDSTANLLW GSNNKSRQLS VSSISSIQSS TVEGKPSLHL ITEERDFTFL FNSSQDQESW
RHALWTLINT TTEPQGDSES EDTHL
//