ID B8LV34_TALSN Unreviewed; 1631 AA.
AC B8LV34;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE SubName: Full=3-oxoacyl-[acyl-carrier-protein] synthase, putative {ECO:0000313|EMBL:EED22655.1};
DE EC=2.3.1.86 {ECO:0000313|EMBL:EED22655.1};
GN ORFNames=TSTA_061450 {ECO:0000313|EMBL:EED22655.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED22655.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC Evidence={ECO:0000256|ARBA:ARBA00001572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain
CC fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+);
CC Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:83139; EC=2.3.1.86;
CC Evidence={ECO:0000256|ARBA:ARBA00000343};
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Fungal fatty acid
CC synthetase subunit alpha family. {ECO:0000256|ARBA:ARBA00007485,
CC ECO:0000256|PIRNR:PIRNR000454}.
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DR EMBL; EQ962652; EED22655.1; -; Genomic_DNA.
DR RefSeq; XP_002340042.1; XM_002340001.1.
DR STRING; 441959.B8LV34; -.
DR GeneID; 8106637; -.
DR VEuPathDB; FungiDB:TSTA_061450; -.
DR eggNOG; ENOG502T74T; Eukaryota.
DR HOGENOM; CLU_000114_0_0_1; -.
DR InParanoid; B8LV34; -.
DR OMA; CCVSEAF; -.
DR OrthoDB; 2725016at2759; -.
DR PhylomeDB; B8LV34; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:RHEA.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd00828; elong_cond_enzymes; 1.
DR CDD; cd08950; KR_fFAS_SDR_c_like; 1.
DR Gene3D; 3.30.70.2490; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.25.70; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR040899; Fas_alpha_ACP.
DR InterPro; IPR047224; FAS_alpha_su_C.
DR InterPro; IPR026025; FAS_alpha_yeast.
DR InterPro; IPR041550; FASI_helical.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR10982:SF23; FATTY ACID SYNTHASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1.
DR Pfam; PF18325; Fas_alpha_ACP; 1.
DR Pfam; PF18314; FAS_I_H; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR PIRSF; PIRSF000454; FAS_yeast_alpha; 2.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:EED22655.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450,
KW ECO:0000256|PIRNR:PIRNR000454};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW Transferase {ECO:0000256|PIRNR:PIRNR000454, ECO:0000313|EMBL:EED22655.1}.
FT DOMAIN 1040..1563
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 115..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1275..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1226
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-1"
FT MOD_RES 207
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-4"
SQ SEQUENCE 1631 AA; 180350 MW; 3C90A2A074654848 CRC64;
MASGKLDEQI ATKKEVRGAK NKRAIAHTLL IELLSYQLSL PVRWIETQKQ LFNAPESVRK
YVEIGAKTTL ATMVKRMADR QPTAEKLSKA MEFYSYSDQK SDLYYEYRPN AGISPQSSSQ
LEAQQSIPSP AATESSITNA TISEAPVSAK PGLLASDNPT VHKRAVKAVP NLSPTHIVIA
LTAQKVNKAF DTLPMQKSIQ ELSGGKSTLQ NELMGDLSVE FSSVPNGGEY MPLETLGEML
QQGFNGKPGK QMSTLISKFI SRKMPPSFNQ VTMQNYIETS WGFGKENSII PICFAVTMEP
ATRFEHADSA KQFLDDVVNR LASFFGIPLS LQLSDDGSTS SAQSAIIVGS SALDRIRQEQ
RNYHLEEFNR LSDHLKIDCR SSDKLQNLIS STKAMEDKLN RWATEFDENF FDGIGPLFDP
KKTRNYDSSW NWIREETIRI FNQFSLGHID YNDQALKLIS RKWDSSCVQI AQDFLQKIEK
VDPEVTIKAR GFLRLESPVL GLQPVYRYSG KAMMPLTYVS STTSNIEYKE LPREVTDYVC
FLKQGRITTH GEAVPYVHLR RRQPANGEYR YNAALTRTMM DMFELGSSSG LSFATKTILV
TGAGPKSIGS GVVEGLLNGG AKVIVTTSRD ISTSADFFAN MYRKHGAHGS SLTVIPFNQG
SRTDCEDLVK YIYGADSPVG GDVDYIVPFG AIPEKDNISN LGSMSELAHR VMLTNVLRIV
GLVYQNKKDR RIDSRPTNVI IPLSFNKGGF GGDGLYPESK LGLESLFNRF YSGNWQQYIT
ITGAVIGWVR ETSLSQTLSL VGYAIEQIPG LNVCTFSRTE MAFNILTLMT PAITELAEDH
PLYADLTGGA KEITNIKDIM SDSRSKFTTE SNIRRALFAE KSREQNVLGG AASSVKASFI
SAPRVQRSNL NLQFPVLSSH ADLTGNISGL EGMIDLARTP VVVGYSELGP WGNARTRWDV
EHLGDFTLET YVEMAWILGL VKHYEGEING QVYVGWVDSK TKEPVCEDNF KQLYGDHIKK
HSGIRFIEPE LLNSYDPAKK EFLQEIVVEE DLPSFATSEA SADAFKLRFG NKVSIEPVSD
SEECRVTVHQ GAHFMLPKSV PFDRAVAGLL PSGWDPLRYG IPEDIVQQVD PVTLYTLCCV
SEALLSAGIS DPYEFYNHIH VSELTNCIGT GAGAMLAGRG LYRDRFLDRP VQSDILSESF
LNTTAAWVNM LLFSASGPIK TPVGACATAI ESLEMGCEAI KTGKSKVAIV GGYDDFQEEA
SYEFAMMKAT VSSEEELAKG RRPEEMSRPS TTTRSGFVES AGCGVQIVMN AELAIKMGLP
IYAVVAYSQI AADQNGRSIP APGQGILTAA RERTGRHYSK LLDLSYRRKL FDEDIAAIDK
WWQEKSQTAG LSETDLNEIQ ALARSKIRQA QYIWGNDIRS QDPLISPMRA ALATWGLTVD
DIQVTSMHGT STNANDTNEA QVINEQMKHL GRRPGNPLLA VCQKSLTGHP KGAAGAWQMN
GCMQMIQNGI VPGNRNADNI EIKLKQNTYI VYPKEAIQVR EIKATMLTSF GFGQKGGLVI
AVASRYLYSA VAAGTYEEYR QKATRRQRAA NSVFISGVIK NSLVRLKDQA PWGKSDEKMR
KVFLDPASIE F
//
