ID F2J5V5_POLGS Unreviewed; 2444 AA.
AC F2J5V5;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Fatty acid synthase transmembrane protein {ECO:0000313|EMBL:ADZ71209.1};
GN OrderedLocusNames=SL003B_2786 {ECO:0000313|EMBL:ADZ71209.1};
OS Polymorphum gilvum (strain LMG 25793 / CGMCC 1.9160 / SL003B-26A1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Polymorphum.
OX NCBI_TaxID=991905 {ECO:0000313|EMBL:ADZ71209.1, ECO:0000313|Proteomes:UP000008130};
RN [1] {ECO:0000313|EMBL:ADZ71209.1, ECO:0000313|Proteomes:UP000008130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25793 / CGMCC 1.9160 / SL003B-26A1
RC {ECO:0000313|Proteomes:UP000008130};
RX PubMed=21478361; DOI=10.1128/JB.00333-11;
RA Li S.G., Tang Y.Q., Nie Y., Cai M., Wu X.L.;
RT "Complete genome sequence of Polymorphum gilvum SL003B-26A1T, a crude oil-
RT degrading bacterium from oil-polluted saline soil.";
RL J. Bacteriol. 193:2894-2895(2011).
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DR EMBL; CP002568; ADZ71209.1; -; Genomic_DNA.
DR STRING; 991905.SL003B_2786; -.
DR KEGG; pgv:SL003B_2786; -.
DR PATRIC; fig|991905.3.peg.2856; -.
DR eggNOG; COG0236; Bacteria.
DR eggNOG; COG0604; Bacteria.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_31_0_5; -.
DR Proteomes; UP000008130; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
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 Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
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; IPR020843; PKS_ER.
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; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 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; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 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; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Membrane {ECO:0000313|EMBL:ADZ71209.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008130};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000313|EMBL:ADZ71209.1}.
FT DOMAIN 1..338
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2321..2395
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2402..2427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2413..2427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2444 AA; 261729 MW; CB2D88102F81C4AE CRC64;
MDPQQRILLQ LVWEALEQAG LPPSALAGSS TGVFVGASSL DYHHRFVIDP QNADMQFMTG
NTLSIVSNRI SYIYDLRGPS FTVDTACSSS LVALHEAVSA LETGQIDTAI VCGISVLLSP
FAFVGFSRAS MLSPTGLCQA FDANGDGYVR SEGGVAVILQ SARAARLPGT KVHGRIVASG
INADGRTVGL SLPSPYAQAA LLEEIYGGLE IAPDRLAFVE AHGTGTRVGD PAEADALGKV
IGQKRSTPLA IGSVKTNVGH LEPVSGLVGL LKSILALKHD LLPKSLHFRT PNPDIPFEDL
NLRVAAEPVP LQKDGSPRLA GVNSFGFGGT NAHVVLADGD APEVSAEPSD PTTPLVLSAR
GKAALKALAE RYREALDGKD DPSAGAISAS AAYTRDLLSD RLVVLGASAE EKRQALDDFL
ADRKSPNIVQ GATVRANQKI AFVFSGNGSQ WAGMGCEAYQ KDPDFQAAFE RVDRKFMGVG
GWSLLTMLFS EDLETEIERT EIAQPLLFGI QVALVEALAR RGIRPSAVAG HSVGEVAAAW
CCGALTLDQA VKVIHARSTQ QEVIRHLGSM AALLLPADKA REAIAEAGFP RIELAAINSP
RSVTISGPVE SLDAFAKFAR KKRWAMRRLN LAYPFHCALV EPIREPLLEA LSGIEPKAAD
LLFFSTVDPD AEEIRLDSDY WWRNVRQPVL FADAIERMAG QTIGVFVEIG PKPVLGTYMN
DVLREGGHRT DVLPSLDAPV KGGEHALNPV ETAAAGILAH GGEVDLEEFF GEPPRAFVGL
PSYPWQNVDY KPEATAESID YMFGTTWPLL GYRLRQDVGE WFNHVDPALL PWLADHKVEE
SIVFPAAGFA EMALRAAIRW TGADEIELRD FDILRPLVFD GSEIWETQVR ISSDDRVVEV
LSRPRLQGAD WSLNARGHFV SVVRNARKST LSVPDNVGTT LETAALYALT QTFGLRYGEA
FQRAEKVLAH DARTATVLLK PQTDAVARGK FALCPTLMDA GFHGLFALLD GVEEIPAQTS
FLPIRLGSLR LLQPEVAPTS VLIRVTRATP RSIEATFEYL DAAGDVVARL SQARFRAVRL
GRETRQSDLV YRTIATLLPD ADRVAPIQAV MPDGFAAFAE RCGVACDDAP EPGDTLLLVE
ALGRTIAHDT LWQLSGAEPL RLDALVEQGL IAQSALPLVH SLLGWLSDSD LATETDDGWR
IEDPAEGPTA SDLLRTIAVE ASGHIAEAAL LSRLSLRLKD ILRDGLAERA QGYFAGGLFD
AYQTASPAAA DLMAAVKRVA VDLITSWPSD QALKILVFGA TSADLLLTLD RLIDPRHASV
VVTDPVATSL GRAERQWTGS NAIRFVDFED GEALAARGPF DIILSGGHLS ESSNQDIARV
GACLSRDGLL FSAEFLPSPL TDLIRGIGAD WWRETAVDAF PLSRLRTPEE WQGDLAAAGL
ERVETTNLDS DVAEAILIAA RAPADGKTVV QADAEQAAEE PQKASTLLVI ADRDGASRKV
AEALKSTLAE AAIAVTVAVI GERTGPDENG DWSIDPDQPD DALKALLAEC AAGIVHLAGA
YAAEGDALAV TDSRTWSLTQ LLKTIGFDDT RLWIVAPGGV QDIAGGSSHR PDQCGVWAYG
RVAMNEFPNA GIRLIDLSPA IEPGVAAVRL ADEIRNGGDE REIIIDGRRR AGLRIVKGGL
LPEAAVSETA EPVMRLDILR QGSLDQLAWH AIDRQLPRDD EIEIAVEASG LNFRDVMWAL
GLLPEEALED GFAGPTLGME CCGTVVSVGP AVTRFQPGER VITFAPACFA SHVTVSEAAC
APMPSTVTSE EAATIPVTFL TAYYALVHLA RLGEGETVLI HGGAGGVGLA ALQIAKWRGA
RTITTAGSEE KRSFLKLLGA DLVLDSRSLA FVDDIMEATD GQGVDVVLNS LFGEAMERSI
EVLKPFGRFL ELGKRDYYGN TRIGLRPFRQ NLTYFGIDAD QLLTRQPKLA KDLFIELVRL
FENGTLAPLP YRVFEADGVI DAFRLMQQAG HIGKIVLRPP AVPAAVPRRR SLALRPDATY
VVGGGFGGFG AELLRRMTDL GARNLLVLSR RGTDSDDARA VAAELETRGV RVVAPACDLT
DEATLAKTLA DCRSTMPPIR GVFHTAMVLN DGLLANLDHD GLTRVLAPKI RGAELLDVLT
AGDPLDHFVL YSSATTLVGN PGQANYVAAN GYLEALARKR RAEGKPGLAV AWGAISDAGY
LARNDDVNEL LARKLGRHAL TAREALDGLV ALMAEPQDSL ETAAVGYARI DWQSARRDLA
LLATPLVDLL GLGSGEDSGP VEGAIDLHAM LKGMDKVKAA QTVANLLAGE IGKILRIAPE
EIDPHKPLSE VGMDSLMALE LRMSAERQLG IDIPLMSLAN GATLIDLSAR VANRVLGGEA
DNGVSGEARQ LASQHMTDDR TETEDLSDIA EQVEAKSREL RSLL
//