ID   A0A1I7YLQ4_9BILA        Unreviewed;      1491 AA.
AC   A0A1I7YLQ4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Fatty acid synthase {ECO:0000313|WBParaSite:L893_g17621.t1};
OS   Steinernema glaseri.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC   Steinernema.
OX   NCBI_TaxID=37863 {ECO:0000313|Proteomes:UP000095287, ECO:0000313|WBParaSite:L893_g17621.t1};
RN   [1] {ECO:0000313|WBParaSite:L893_g17621.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   WBParaSite; L893_g17621.t1; L893_g17621.t1; L893_g17621.
DR   Proteomes; UP000095287; Unplaced.
DR   GO; GO:0004312; F:fatty acid synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd05235; SDR_e1; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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; 3.
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; IPR042099; ANL_N_sf.
DR   InterPro; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
DR   NCBIfam; TIGR01746; Thioester-redct; 1.
DR   PANTHER; PTHR44845:SF6; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR   PANTHER; PTHR44845; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF07993; NAD_binding_4; 2.
DR   Pfam; PF00550; PP-binding; 2.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR   PROSITE; PS00061; ADH_SHORT; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          590..665
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          669..747
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1491 AA;  165892 MW;  638DB2B8D85EC5A3 CRC64;
     HWEAEGHPMS PSRSRPLLQV PLRALSLRGG GHRRLQRLLR AAYLPLDISY PPHLLESILD
     EVRPAAVCTT PEYAKRLPES APVFTFSGAS VEQSLPDSNN ISLPSDIGPD DLAYIVYSSG
     TTGKPKGIQC PHRGAVLSYK YRFEHYPYVE GDIVACNVFF VWELFRPILQ GVKMCIIPDD
     VIYDPYPLCK FLEEQRVTRM LFTPSLLETV LDTQSRETIV AAFKHFRVIW LCGEVVTCAL
     LKRTMDVLPN VQVANLYSIS ECHDVSVEDL TKFHKSGVER KYAPAGTLIP GVKVAILDNN
     HKRVPIGMPG EIYVGGPTLA IGYLNRPELN RSRFLDVPEE LRAEVGDKMY RTGDWGYVLG
     NQTLEICGRC DTMVKIRGYS IEIQXXXXIR PSRSVDAATR WSRSEATVSR FRDGKSRIAP
     KILLGRRKSS KSPAQIVRGL RFFRRTLVGS HNENTSPPSP GRGVDHPAPA VXXXXCLLSL
     HLQTGTIELP DGTYAVESTI LHLPWIASCA VVSIGAEGED KQLAAYLVLQ EPVTRKALRA
     ELKRKLPFYM VPTYFVFLDK LPVLAASSKV DRKALPPVDP ERDIVEASAL PQTPTEVKLA
     AIWADVLQRS ALDVQESFFD LGGHSLLAAR LLGKVAADFG VELSMRDLFA SPTVSAMAKL
     LDGSERNSPE TVVDLEQQVE THDYKDHVMD LHLRAFWRST XXXRFHSLLA ARLLGKVAAD
     FGVELSMRDL FGSPTVSAMA KLLDGSERNS PETWDNRFSR ATVLLTGVTG FLGSHILAAL
     LNSTQVRVIC LVRESTNETV DSRLESALKR RGLLTHTVKE QLGDRVKAMS GDVALVHFGL
     SDEHYHLLTY DVDVVIHAAA YVNLIYPYQA LHGINVLGTW NVLDFCHKNK VKPLHXXXXS
     RTPDRVKAIS GDVALVHFGL SDEHYHLLTY DVDVVIHAAA YVNLIYPYQA LHGINVLGTW
     NVLDFCHKNK VKPLHYISTD AVIPAGLNDV DEDFDIELVK EKLADGYGQT KYVAEVMVRR
     SQARGLPSII YRLGNQSAST SAGYWNDQDF TYLMLQAVIH TGKTPDVDWT IELTPVDFAA
     KFVSSLVTKH FCAQVGKTFH LTNSQGPKWS DLMDWLRSFG YRIEKVDAER WMQLVLNSTD
     AKLQQIQKLV AVMIRDESFF ATQSTYLRSN TDRFVREAKW RYPTVDERLV RHWLQLLVER
     HVLPSPSVNV GTALVDKVCV ITGASEGIGA AIARILAIDG GARVVLAARQ EEKLKALALR
     LQADGCPEAS ILPIPCDVTS DEQVQRLYET TMERFGRVDV LVNCAGCMYY CMMKNGPTAE
     WKRQIDVNCH GTMNMIGAVL PHMIERRQGH ILNITSDAGK RGFAGLAVYS GSKFFLEGMS
     QALRQEMVEF GIRVTNIQPG DVATELAGRS TDEEVXXXXA RRWWSSAFAS PISSPETWPP
     SSLARSKFDG SNAGHRILDP EDVGRSVLYA LSQPAHVAVN EILIEPQAAP I
//