ID   PKIB_EMENI              Reviewed;        1771 AA.
AC   Q5B7V0; C8VHP2;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   24-JAN-2024, entry version 113.
DE   RecName: Full=Fatty acid synthase alpha subunit pkiB {ECO:0000303|PubMed:22510154};
DE            EC=2.3.1.86 {ECO:0000250|UniProtKB:P19097};
DE   Includes:
DE     RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase {ECO:0000250|UniProtKB:P19097};
DE              EC=1.1.1.100 {ECO:0000250|UniProtKB:P19097};
DE     AltName: Full=Beta-ketoacyl reductase {ECO:0000250|UniProtKB:P19097};
DE   Includes:
DE     RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase {ECO:0000250|UniProtKB:P19097};
DE              EC=2.3.1.41 {ECO:0000250|UniProtKB:P19097};
DE     AltName: Full=Pki biosynthesis cluster protein B {ECO:0000303|PubMed:22510154};
GN   Name=pkiB {ECO:0000303|PubMed:22510154};
GN   Synonyms=fasA {ECO:0000303|PubMed:15050539}; ORFNames=AN3380;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [3]
RP   INDUCTION BY FATTY ACIDS.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=15050539; DOI=10.1016/j.fgb.2003.12.009;
RA   Wilson R.A., Chang P.K., Dobrzyn A., Ntambi J.M., Zarnowski R.,
RA   Keller N.P.;
RT   "Two Delta9-stearic acid desaturases are required for Aspergillus nidulans
RT   growth and development.";
RL   Fungal Genet. Biol. 41:501-509(2004).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=22510154; DOI=10.1021/ja3016395;
RA   Ahuja M., Chiang Y.M., Chang S.L., Praseuth M.B., Entwistle R.,
RA   Sanchez J.F., Lo H.C., Yeh H.H., Oakley B.R., Wang C.C.;
RT   "Illuminating the diversity of aromatic polyketide synthases in Aspergillus
RT   nidulans.";
RL   J. Am. Chem. Soc. 134:8212-8221(2012).
CC   -!- FUNCTION: Fatty acid synthase alpha subunit; part of the pki gene
CC       cluster that mediates the biosynthesis of 2,4-dihydroxy-3-methyl-6-(2-
CC       oxoundecyl)benzaldehyde (PubMed:22510154). The first step in the
CC       pathway is the generation of the decanoyl starter unit by the FAS
CC       composed of subunits pkiB and pkiC, which is then transferred directly
CC       from the FAS to the SAT domain of the non-reducing polyketide synthase
CC       pkiA (PubMed:22510154). PkiA condenses the decanoyyl starter unit with
CC       4 malonyl-CoA units and performs one methylation step to yield 2,4-
CC       dihydroxy-3-methyl-6-(2-oxoundecyl)benzaldehyde (PubMed:22510154).
CC       {ECO:0000269|PubMed:22510154}.
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:0000250|UniProtKB:P19097};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC         + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC         EC=2.3.1.41; Evidence={ECO:0000250|UniProtKB:P19097};
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:0000250|UniProtKB:P19097};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:22510154}.
CC   -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC       (alpha and beta). {ECO:0000250|UniProtKB:P19097}.
CC   -!- INDUCTION: Induced by oleic acid and stearic acid, but not by linoleic
CC       acid. {ECO:0000269|PubMed:15050539}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Fungal fatty acid
CC       synthetase subunit alpha family. {ECO:0000305}.
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DR   EMBL; AACD01000055; EAA63348.1; -; Genomic_DNA.
DR   EMBL; BN001306; CBF82822.1; -; Genomic_DNA.
DR   RefSeq; XP_660984.1; XM_655892.1.
DR   AlphaFoldDB; Q5B7V0; -.
DR   SMR; Q5B7V0; -.
DR   STRING; 227321.Q5B7V0; -.
DR   EnsemblFungi; CBF82822; CBF82822; ANIA_03380.
DR   GeneID; 2874362; -.
DR   KEGG; ani:AN3380.2; -.
DR   eggNOG; ENOG502T74T; Eukaryota.
DR   HOGENOM; CLU_000114_0_0_1; -.
DR   InParanoid; Q5B7V0; -.
DR   OMA; CCVSEAF; -.
DR   OrthoDB; 2725016at2759; -.
DR   Proteomes; UP000000560; Chromosome VI.
DR   GO; GO:0005835; C:fatty acid synthase complex; IBA:GO_Central.
DR   GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
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:UniProtKB-EC.
DR   GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite 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; 3.90.470.20; 4'-phosphopantetheinyl transferase domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR   InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
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; IPR009081; PP-bd_ACP.
DR   InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR00556; pantethn_trn; 1.
DR   PANTHER; PTHR10982:SF23; FATTY ACID SYNTHASE SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1.
DR   Pfam; PF01648; ACPS; 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; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Magnesium; Metal-binding; Multifunctional enzyme; NAD;
KW   NADP; Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..1771
FT                   /note="Fatty acid synthase alpha subunit pkiB"
FT                   /id="PRO_0000419253"
FT   DOMAIN          143..221
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1011..1531
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   REGION          108..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..771
FT                   /note="Beta-ketoacyl reductase"
FT                   /evidence="ECO:0000250|UniProtKB:P19097"
FT   COMPBIAS        108..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1197
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        1416
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        1457
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   BINDING         1650..1652
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:P19097"
FT   BINDING         1650
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P19097"
FT   BINDING         1651
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P19097"
FT   BINDING         1652
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P19097"
FT   BINDING         1676
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:P19097"
FT   BINDING         1686
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:P19097"
FT   BINDING         1695..1705
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:P19097"
FT   BINDING         1719..1722
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:P19097"
FT   BINDING         1753..1755
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:P19097"
FT   BINDING         1754
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P19097"
FT   BINDING         1755
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P19097"
FT   MOD_RES         181
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   1771 AA;  194939 MW;  AFD90A5A2137EED1 CRC64;
     MAISSTADLA PSRKARGSES NDRALKLFIE LLSVETQQQL FRGEPCIQRF VEIGPRTILS
     TMAKRSASIQ KDQRSSASCY SPEFLSYHDN QPEILYQYQN DQAIYPLSQP TQPQFEPTSP
     SHLTKRSPSP SKALPMSAIP SAELTLQAGH VILAMTAQKL RRRFDQVPVE KTIRDLSGGK
     STLQNELTGD LVAEFGRVPE GVEDQPLSSL AESFQPEFSG IPGKAMSTLI SRFISGKMPA
     GFNQSAIQEY LNSRWGLTKS HATIPLCFAP TMEPARRLAN ADEARAYLDD LVEKHAAFQG
     ISLVPSNQVA DGHESLAPVV MNVADVDEMN KRTKLYRAQF DSLASYLGVD YFASEKAMSE
     SESRIAELEE TIRLLNTELD EQFIKGIKPS FNIKQVRKYD SWWNWSREEL IRLLNEICQD
     SSSACPPDME NRLQNLLNKW DANCSEIVRA HLIGLQSRSS APMNKLQLIL EEIFTLGNQT
     LSIDPLFVHN LPPMGPQTII TDAGCLEYHE LPRQISHYPE AMAYGPPWPQ GHTSAPFIHI
     KTREDGQDWM YDSKATSIYH AMLDVGVTTG LTFTHKAVLV TGAGPSSIAA SVIQGLLSGG
     ARIIVTTSRS ISQSADFYQQ MYRQYGAKGS SLSLFPFNQA SKQDCEQLVQ HIYGPDSPTD
     GDLDYILPFA AIPQVGEPDA FGGRQELALR AMLVNILRLI GFVRQEKERL RIENRPTMIV
     LPMSCNEGTF GGDGLYSEAK IGLKALFNRF YSENWSKYLT ICGAVIGWTR GTAIMQTSNA
     VAEEVEKLGV ITFTQAEMAF NILALMTPAL TALAEDTPIY ADLTGGLGSM WNIKQEISAA
     RKRISERQIL QIAIAEEDAR EQAMICSAST DVESGLPTTR HARLGLQFPP LPDVNEGYPN
     IEGMIDLTRI PVIVGYSELG PWGNARTRWE IEHRGDFSLE GYIEMAWIMG LIKHVDGHAK
     GRPYVGWVDA DTETPIQDYE VPHKYHKHIM AHAGLRLIKP TKLDSYDPSR KELLHEVAVE
     EDLAPFETSK STAEAFKLRH GDCVTLLPIA DSDNCRVYIK KGAVLMIPKA VPFDQVVAGR
     IPEGWDPARY GIPEEIVQQV DVTTLYALCC VSEAFLSAGI KDPYEIYQYI HVSELANCLG
     SGGGPMKVIQ NMYRDRFLDR QIRGDIILEH FVNTMGAWVN MLLLSATGPL KTPVGACATA
     IESLDIGCEA IQNGRCKVAV VGGCDDYGEE LAFEFANIKA TANSTEELSK GRTPADISRP
     TASSRSGFAE SAGCGVQILM SAALAIEMGL PIYGVVAYTH MASDQIGRSI PAPGKGILTA
     ARENGQAKES PLLDLNFRRA VFDAEVALIN KSHPKQATTL KPDHSETSNA ASLRIRDAQN
     RWANNIRLSD PSISPIRASL ATWGLTVDDI KVVSMHGTST KANEVNEGNV INTQMRHLGR
     QMGNPLLAVC QKSLTGHPKA GAGAWQLNGC LQMMQENIVP GNRNADNIDK QLREFEHIVY
     PMESLRVPEI KATLLTSFGF GQKGAINIMV SPRYLFASLS NSDYEDYRSR TTKRQRSATP
     TFVSRIMKNN LVQVKTRPPW NDPEAMQNFF LDPNSRVVDG QITRAPRTAY KHQDISVPQS
     AAVSVNEALH AMLATTDHSS PAASASVGVD VEEISSINVD NPIFISRNFT LLERDYCLSA
     PDPRASFAGR WVAKEAAFKS LQTTSTGAGT AMDQIEILEV GGIPKVVRLT SQLHGHAHEV
     AFAQGITNIQ ITISHCNNTA IAVALALRKN D
//