PKIB_EMENI
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 03-AUG-2022, entry version 107.
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; 162425.CADANIAP00009660; -.
DR PRIDE; Q5B7V0; -.
DR EnsemblFungi; CBF82822; CBF82822; ANIA_03380.
DR EnsemblFungi; EAA63348; EAA63348; AN3380.2.
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; 39339at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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: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:0042759; P:long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.470.20; -; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR040899; Fas_alpha_ACP.
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 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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR SUPFAM; SSF56214; SSF56214; 1.
DR TIGRFAMs; TIGR00556; pantethn_trn; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 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 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 REGION 1041..1255
FT /note="Beta-ketoacyl synthase"
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:0000250|UniProtKB:P19097"
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
