PKIC_EMENI
ID PKIC_EMENI Reviewed; 1872 AA.
AC A0A1U8QK63; C8VHP1; Q5B7U9;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Fatty acid synthase beta subunit pkiC {ECO:0000303|PubMed:22510154};
DE EC=2.3.1.86 {ECO:0000269|PubMed:22510154};
DE Includes:
DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase {ECO:0000250|UniProtKB:P07149};
DE EC=4.2.1.59 {ECO:0000250|UniProtKB:P07149};
DE Includes:
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000250|UniProtKB:P07149};
DE EC=1.3.1.9 {ECO:0000250|UniProtKB:P07149};
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] acetyltransferase {ECO:0000250|UniProtKB:P07149};
DE EC=2.3.1.38 {ECO:0000250|UniProtKB:P07149};
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] malonyltransferase {ECO:0000250|UniProtKB:P07149};
DE EC=2.3.1.39 {ECO:0000250|UniProtKB:P07149};
DE Includes:
DE RecName: Full=S-acyl fatty acid synthase thioesterase {ECO:0000250|UniProtKB:P07149};
DE EC=3.1.2.14 {ECO:0000250|UniProtKB:P07149};
DE AltName: Full=Pki biosynthesis cluster protein C {ECO:0000303|PubMed:22510154};
GN Name=pkiC {ECO:0000303|PubMed:22510154}; ORFNames=AN3381;
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 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 beta 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:P07149};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA;
CC Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78446; EC=2.3.1.38;
CC Evidence={ECO:0000250|UniProtKB:P07149};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449; EC=2.3.1.39;
CC Evidence={ECO:0000250|UniProtKB:P07149};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC Evidence={ECO:0000250|UniProtKB:P07149};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;
CC Evidence={ECO:0000250|UniProtKB:P07149};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) +
CC holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14;
CC Evidence={ECO:0000250|UniProtKB:P07149};
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:P07149}.
CC -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BN001306; CBF82821.1; -; Genomic_DNA.
DR EMBL; AACD01000055; EAA63349.1; -; Genomic_DNA.
DR RefSeq; XP_660985.1; XM_655893.1.
DR AlphaFoldDB; A0A1U8QK63; -.
DR SMR; A0A1U8QK63; -.
DR STRING; 162425.CADANIAP00009659; -.
DR EnsemblFungi; CBF82821; CBF82821; ANIA_03381.
DR EnsemblFungi; EAA63349; EAA63349; AN3381.2.
DR GeneID; 2874361; -.
DR KEGG; ani:AN3381.2; -.
DR eggNOG; ENOG502SK0D; Eukaryota.
DR HOGENOM; CLU_000114_5_0_1; -.
DR OMA; EQYVCSG; -.
DR OrthoDB; 8490at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008693; F:3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.366.10; -; 3.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR016452; Fas1/AflB-like.
DR InterPro; IPR013565; Fas1/AflB-like_central.
DR InterPro; IPR040883; FAS_meander.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR039569; MaoC-like_dehydrat_N.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR032088; SAT.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08354; DUF1729; 1.
DR Pfam; PF17951; FAS_meander; 1.
DR Pfam; PF13452; MaoC_dehydrat_N; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR Pfam; PF16073; SAT; 1.
DR PIRSF; PIRSF005562; FAS_yeast_beta; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SUPFAM; SSF52151; SSF52151; 2.
DR SUPFAM; SSF54637; SSF54637; 2.
PE 1: Evidence at protein level;
KW Hydrolase; Lyase; Multifunctional enzyme; NAD; NADP; Oxidoreductase;
KW Reference proteome; Transferase.
FT CHAIN 1..1872
FT /note="Fatty acid synthase beta subunit pkiC"
FT /id="PRO_0000450879"
FT DOMAIN 1518..1617
FT /note="MaoC-like"
FT /evidence="ECO:0000255"
FT REGION 174..425
FT /note="Acetyltransferase (AT) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA1"
FT REGION 591..836
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA1"
FT REGION 1111..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1597
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA1"
SQ SEQUENCE 1872 AA; 207117 MW; B1DC54B76380678B CRC64;
MALEEVPSVS RDLDHSALRA LSSASPSSLP SSCSRSTTSL LFQSKGIEFR LSIPDTFLSL
VEPHRNAFLA SYSTQGNTQS PLELALSFLY FLLDQKVSPL VLSSVLRAFN LEFLGNRSEI
HSLIADLTPI PKQRQRWLGI YYRFLEASDD KRAEIPLSSI FQHARTNEFQ LMAVFGGQGE
CSRTCLNEFA ELYSSYEPML RRLVGVIGPC LYNLSTSDEY SSYYRNQPLD LKAWITDENH
VPDLGFVASA PVSVPVIGAL SLARYCVTCH ITGCNPGLMR SMLRTATGHS QGLLAAIVVA
VSHSWDSFYQ ATEEVIELLF RLGWECHHAA PCSMVPAANY ADVDGANGPS YMLSLRGLKR
QETEATIDHV NASLPEDKRL YLALINAYDQ FVVAGPVASL LRLESHLVEI TSKDIDQSRI
PFRDRKPYIQ HSFLPVSTPF HTPYLTRAAA RVKKQFAARP IPTRRLAIPV YHTHTGLDLR
KQGGCALSIA IDAIASEPCN WPCAVASYHA SHILTFDRGG LAPLIKRVRE GCGVRVVQVA
DLDTRDSEMA TMRDLFATKL LPTSTKLQSW GQQFRPGLAS GPKIQLETRL NRVLGAPPIM
VAGMTPTTVH PDFVAAIMNA GYHAELAGGG YHNASAMEAA IYDLVSSIPK ERGITCNLIY
ANPRSISWQI ELLRRLSNGN VRIDGLTIGA GVPSLTVASE YIETLGLRHI SFKPGSVAAI
RKVVEIAREH PDFPVILQWT GGRGGGHHSF EDFHAPIIAT YGIIRQEPNV YLVAGSGFGD
SDSVYPYLTG SWSVAMGHPA MPFDGILLGS RMMVAKEAHT SPAVRRIIAA TPGVSDSEWE
KTYSGPAGGV ITVTSEMGEP IHKIATRGVC LWADLDKTVF SLSRRDRLTY LAQHRRSIIQ
RLNADFAKPW FGCNSDGEAV DLEDMTYLEV LKRLTALMFV PNKQWIDASY IEFTMTIAQR
WLQRLQFDSE AAASLTISLL RKAPDRFLAI FADVCPTAEG DLLNPEDISF FLMQCKTPGR
KPVNFIPALD DDFEFYFKKD SLWQAEDVDA VLDQDAERVC ILHGPIAARY SKSDSEPAGY
ILDSILNGVV ARLRETSTAE MLLPKLERGH TTPASWSTLS LTERDTSEET SDTSITSLSE
LIENHSFSSG GVDSVPRPSH PLWMRALLED DVVLQGTLRQ KNPFRDLIQS SPNTVVNYNQ
DSSELMVTAQ EPYHISSFMR AVCHDGVMDK RNERIKSFYS LLWFGHDCDT SQSLNGVFYG
PDITLTEDLL DEYNATIGPA YSDHRQMVPS TDVLPISMGI IIAWDVISRP LILRQIGGDL
LRLVHRSNTF EYYSDTRLRL GDSVSSRSEV QAVYDDDGGR VVIVEAQILR SRVPVMTVTS
TFLFRGSKGT TVPAFRRARE QKWTYDVTSE FEESILLSRN WFRPCDPSLT LVGKSMIFDL
NSLVKYHDDG NMELHVQGTA MSQTNGQQQK LAIVDFRNTC TGNPVLDFLQ RRGKLAEPRT
EFKIPGWAGK STMDIQMPPS NEPYAQLSKD FNPIHTSPIF SSLAGVPGTL CHGMCTSAIA
ERVLEHLGLG GDRERLRRFE ARFTDMVMPL EKLVVEIKHT GMVDGRMCFS ILAKRKETDE
RVLEGDAEVE QPRTAYLFTG QGSQSKGMGM DLYKTSTGQF LLTNKGGLFW TSCKTTQSPL
PIRQKYLDIT TEVVLPNGKR VQKPVFPGLT PTSTSYTFRH PRGLLYSTQF AQPAILLFEA
AAFAELRAKG YVSHGAVYAG HSLGEFGALS ALSRSVPTGA LVELAFYRGS VMQASVASDN
DGGTTYGMVA MNPKRVGTFF TQTTLDRLVS QIAAQSQELL EIVNFNIEGE QYVCSGTIDR
PISGGTWPSL SG
