PKIA_EMENI
ID PKIA_EMENI Reviewed; 2493 AA.
AC Q5B7U4; C8VHN6;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Non-reducing polyketide synthase pkiA {ECO:0000303|PubMed:22510154};
DE Short=NR-PKS pkiA {ECO:0000303|PubMed:22510154};
DE EC=2.3.1.- {ECO:0000269|PubMed:22510154};
DE AltName: Full=Pki biosynthesis cluster protein A {ECO:0000303|PubMed:22510154};
GN Name=pkiA {ECO:0000303|PubMed:22510154}; ORFNames=ANIA_03386;
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 DOMAIN, 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: Non-reducing polyketide synthase; 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=AH2 + decanoyl-[ACP] + 3 H(+) + 4 malonyl-CoA + S-adenosyl-L-
CC methionine = 2,4-dihydroxy-3-methyl-6-(2-oxoundecyl)benzaldehyde + A
CC + 4 CO2 + 4 CoA + H2O + holo-[ACP] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:64528, Rhea:RHEA-COMP:9640, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:17499, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78468, ChEBI:CHEBI:155864;
CC Evidence={ECO:0000269|PubMed:22510154};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64529;
CC Evidence={ECO:0000269|PubMed:22510154};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250|UniProtKB:A0A0K0MCJ4};
CC Note=Binds 1 phosphopantetheine covalently. {ECO:0000255};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:22510154}.
CC -!- DOMAIN: Multidomain protein; including an N-terminal starter unit:ACP
CC transacylase (SAT) domain, a beta-ketoacyl synthase (KS) domain, a
CC malonyl-CoA:ACP transacylase (MAT) domain, a product template (PT)
CC domain that controls the immediate cyclization regioselectivity of the
CC reactive polyketide backbone, an acyl carrier protein (ACP) domain, a
CC methyltransferase (CMeT) domain responsible for the incorporation of
CC methyl groups, and a reductive NADPH-binding domain that is required
CC for NADPH-dependent product release. {ECO:0000305|PubMed:22510154}.
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DR EMBL; BN001306; CBF82812.1; -; Genomic_DNA.
DR RefSeq; XP_660990.1; XM_655898.1.
DR AlphaFoldDB; Q5B7U4; -.
DR SMR; Q5B7U4; -.
DR STRING; 162425.CADANIAP00009654; -.
DR EnsemblFungi; CBF82812; CBF82812; ANIA_03386.
DR EnsemblFungi; EAA63354; EAA63354; AN3386.2.
DR GeneID; 2874069; -.
DR KEGG; ani:AN3386.2; -.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_2_1; -.
DR InParanoid; Q5B7U4; -.
DR OMA; NVNCHPA; -.
DR OrthoDB; 13314at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.150; -; 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; IPR013120; Far_NAD-bd.
DR InterPro; IPR041068; HTH_51.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW Phosphopantetheine; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..2493
FT /note="Non-reducing polyketide synthase pkiA"
FT /id="PRO_0000450878"
FT DOMAIN 1588..1662
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 129..243
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT REGION 404..821
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT REGION 926..1261
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT REGION 1297..1558
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000305|PubMed:22510154"
FT REGION 1822..2063
FT /note="Methyltransferase (CMeT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT REGION 2128..2366
FT /note="NADPH-binding domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT ACT_SITE 160
FT /note="Nucleophile; for transacylase activity"
FT /evidence="ECO:0000250|UniProtKB:A0A0K0MCJ4"
FT ACT_SITE 274
FT /note="Proton donor/acceptor; for transacylase activity"
FT /evidence="ECO:0000250|UniProtKB:A0A0K0MCJ4"
FT ACT_SITE 567
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1622
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2493 AA; 275025 MW; 3F53D0FBD3C55F84 CRC64;
MVTPAASQDP PAIPARQNAS ATAAMAVNAK DTVEQERNVV LLFGCQWLTF TASDFRQLRK
AVLDNPELHW MLDVLSELPG YYRAAAGTSC VPSLRAIRGE EDLRELERWF RCDDLSTAKF
PLCYTQLAPL LMMTHFVQYS QWLKMQPNGR NPVVEIVGFC IGLLSSIAVS ATRMGSLKMY
GSVAMRLAML LGAMGDLQQA GEEYTSLAIG WKRPELEDEL PAERALTEQS YITVQYDENR
ATIMAPRRSV AALQQTLQSA GFSANAVEYN GRYHWPGHEK SLTPLIHLCN THSGLQLPDA
SELLHPPRAN STAEPVRSGC LHELVLRAVL AQQCLWHKTF SAVYREHLTT PSSIVVEFGP
ERCVPPTLFR RLPQRIVHFA DVELPATISR DHELATRPPA ETDIAIVGMA CRVAGADDLD
EFWDLLCSGQ SQHREMPRER YANYETPWRP EASHRSWLGN FVRDIDAFDH KFFRKSPREA
MSQDPQQRLM LQVAYQALES AGYFSQPSPG KDIGCFIATC TVDYEHNVNC HPASAYAATG
LLRSFLAGKL SHHFGWRGPS LCVDTACSGS AVALHHACRA ILSGDCTAAL VGGANAITSP
LAYDNLAGAS FLSPTGPCKP FDAKADGYCR GEGFAAIYIK KLSHAIADGD QVLATIASTA
VEQNDNCTPI VVPDTASLAG LFKKVTQRAH LHSRDISIVE AHGTGTQAGD PAEYESVRDV
LGGPRRVGNL ALGSVKGLVG HTEGVSGIIA LCKVVLMILN GQIPPQPGFH SLNPHIRAMP
DDHIEIGTRV KPWEVGFRAA LINNYGACGS NASMVITQGP QKDEVQERGI HAENVALPFR
VCGLDKARLQ AYAARLRRFL SRSERGISFA NIAFNLTRKS NPALECQCVF QTRSESELKD
ILTGLEEGDN KYIIQVKKPK RPLVLCFGGQ VGRSIGLDRT FYNAFPLFKH HLDSCDDILK
ANGDSSIYPG IFATAPVLDI VQLHTQLFAL QYACARSWMD CGVEVTAVIG HSFGELTALC
ISGALSLPDA LTLIVRRAVL IRDKWGADPG AMLAVEGDRS TLEKHLESSS ANIACFNGPR
SFTVAGPTAV IDFLQEELGA DSAFRLKRLE VTNAFHSTLV DPLLPALASA IDGLALNTAT
IPIERATEHQ AADTIPLSIV ADHLRQPVYF NNAVQRLAAR HGPAIWLEAG SNSTITSLAR
RALGLGVSGN TFHSVNVTST SALMNLTDVT VGLWSDNVPC TFWGYHARQT REYAPLLLPP
YQFERTRHWM ENKPLPLKYN QAQAVMEVSG HTAAKTAPIA PATLLLDYAI ELLRSLPNNQ
RKIPRVFDVG SDAPLLLDSN REVWIEVSAE DDKRTWALRF QSQTKGGQSD SRLLHCTAHI
SMHDVRCSRL QTEFTQYARL VSHARCADLL TDPEVDDILQ GRNVYRSFAE IVEYSEQYQG
VKRLVGKGRE SAGRVVKSYS GKTWADPFLC DSFSQCAGFW VNCMTDRAED EVYVASGIEQ
WMRTPLYADM ATARPDTWHV WARHQQSEGL YTSDVFVFTP DGELVEMFLG LRYSRVAKSL
FTRLLRGSTL KVDCRTKDTA NQENNSIKDL VSRVKAVVAE ICAVKPSEIQ DDSHLADAGV
DSLMAMELAR ELEVAFKCTI ALEALVEAET FHDLVQAVQS ALGETYEDSS VCSGNQCSTT
DEATEFPSTS WSITSVSDTA DLVLPLDGVL DALDETKGLT DQFLADNKCS GRLLNFTPLM
VEMCIVLTLE ALEELGSNIR SARANDRLPR IEFDTQHGPL VEYLYGRLLE AGLIKLDGST
VIRTEICAPT ESSSTLLHKI EREYPEYGGA SKLTFYTGSR LASVLRGEQD GLQLIFGTAE
GQRLVSWMYG DEPHNVAGYK LMGEFIRRLV DKLPPAAARE GMTLRILEMG AGTGGGTKWM
LPLLAALPVP VEYTFSDISP AFLAQARRKF RDYQFVRYCV HDIEKPPSED LGKYHIIMAS
NAVHATSNLQ VSTGNMRQAL RPDGVLMLLE MTRPVFAIDL VFGLFRGWWV FNDGRTHAIT
NEQRWKDDLQ AVGYGHVDWT DGESNEVGVQ RVIFATAGGE QYHPVSPQED AARLRTVVEY
VYQHTAGFTM PALPPRIRAP ANHACILVTG ATGSLGSHLV ARLVQLSNVQ AVICLNRVSR
MGPRVRQKEA VAARGLSLES KEETKLMVIE TDTANDRMGL SVEQCRYLQE NVTHIIHNAW
PMNGAAPLSK FEGQFRALRN LIDLARCIAT AQRHPVRFQF ISSIGTVNGG GALEERTRIE
QVMSNGYNEA KFVCERMIHE TLQRYPAVFQ ATIVRPGQIS GSEETGYWNT AEHFPAMVKS
SQSLGAFPSL AGRLGWTPVD VAARIIAELL LDEGIPEEIY HVDHPTGQNW TTVVDVLAEE
LEATEVPFKD WIQRVRNRGG SRENPAGFMA DWLETNFERM SCQGPLDTRV ARRHSKTLRE
MGGGGGDEHV RRVVRSWKEC GFLTQAQTRQ GIP
