PKHB_EMENI
ID PKHB_EMENI Reviewed; 2544 AA.
AC Q5BBP5; C8VLG3;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Highly reducing polyketide synthase pkhB {ECO:0000303|PubMed:22510154};
DE Short=HR-PKS pkhB {ECO:0000303|PubMed:22510154};
DE EC=2.3.1.- {ECO:0000269|PubMed:22510154};
DE AltName: Full=Pkh biosynthesis cluster protein B {ECO:0000303|PubMed:22510154};
GN Name=pkhB {ECO:0000303|PubMed:22510154}; ORFNames=ANIA_02035;
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: Highly reducing polyketide synthase; part of the pkh gene
CC cluster that mediates the biosynthesis of 2,4-dihydroxy-6-[(3E,5E,7E)-
CC 2-oxonona-3,5,7-trienyl]benzaldehyde (PubMed:22510154). The highly
CC reducing polyketide synthase pkhB first produces the (2E,4E,6E)-octa-
CC 2,4,6-trienyl strater unit for the non-reducing polyketide synthase
CC pkhA (PubMed:22510154). This octatrienoyl starter is then loaded onto
CC the SAT domain of the NR-PKS pkhA to be condensed with 4 malonyl-CoA
CC units to yield 2,4-dihydroxy-6-[(3E,5E,7E)-2-oxonona-3,5,7-
CC trienyl]benzaldehyde (PubMed:22510154). {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 a ketosynthase (KS) that
CC catalyzes repeated decarboxylative condensation to elongate the
CC polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects
CC and transfers the extender unit malonyl-CoA; a dehydratase (DH) domain
CC that reduces hydroxyl groups to enoyl groups; a methyltransferase
CC (CMeT) domain responsible for the incorporation of methyl groups; an
CC enoylreductase (ER) domain that reduces enoyl groups to alkyl group; a
CC ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and
CC an acyl-carrier protein (ACP) that serves as the tether of the growing
CC and completed polyketide via its phosphopantetheinyl arm.
CC {ECO:0000305|PubMed:22510154}.
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DR EMBL; BN001307; CBF86052.1; -; Genomic_DNA.
DR RefSeq; XP_659639.1; XM_654547.1.
DR AlphaFoldDB; Q5BBP5; -.
DR SMR; Q5BBP5; -.
DR STRING; 162425.CADANIAP00008703; -.
DR EnsemblFungi; CBF86052; CBF86052; ANIA_02035.
DR EnsemblFungi; EAA64867; EAA64867; AN2035.2.
DR GeneID; 2874642; -.
DR KEGG; ani:AN2035.2; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR InParanoid; Q5BBP5; -.
DR OMA; IGMSCKF; -.
DR OrthoDB; 19161at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
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:0016491; F:oxidoreductase 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; -; 1.
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; IPR011032; GroES-like_sf.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
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; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
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 Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..2544
FT /note="Highly reducing polyketide synthase pkhB"
FT /id="PRO_0000450877"
FT DOMAIN 2462..2539
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 12..441
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 566..876
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 948..1252
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 1398..1573
FT /note="Methyltransferase (CMet) domain"
FT /evidence="ECO:0000255"
FT REGION 1826..2142
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255"
FT REGION 2169..2356
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255"
FT ACT_SITE 182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2499
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2544 AA; 277372 MW; F7E0CD846B916F25 CRC64;
MDTDSEWASE PIAIIGMSCK FSGGASNPDK LWDLMASGKT GWSEIPEERF NLKGVYHANH
ERTSTTHVKG GHFLDEDVAV FDAAFFNYSA EMAQVVDPQF RLQLESAYEA LENAGLPLSR
VLGSQTSVFA GVFAHDYQEG IIRDEDRLPR FNVVGTWSPM SSNRISHFFD FRGASMTLET
GCSTTLVALH QAVQTLRNRE ADMSVVTGAN VMLNPDTFKA IGSLGMLSPD GRSYSFDSRA
NGYGRGEGVA TIIIKRLSDA LAANDPIRAV IRETAVNQDG KTDTITTPSG AAQVDLMREC
YSRAGLDPRG TQYFEAHGTG TPTGDPIEAQ AMATIFSEGR DDKNHYLRIG SVKTNVGHTE
AVSGLAAVIK GVLCLEKGLI PPTVNYEMPN PKLKLNEWRL KVVRTIEHWP DSLIDGPCRM
SINNFGYGGT NAHVILESAD PWTLTPDLDF ELVNGKGLKG NGDASDDVSD AKVLILSARD
ERGCQQMVSD LKGYLEKHKP LDRKASKQLL QNLSYTLCER RTLFQWVATH QVRLDSGALD
SVIQGLDSPC FKPTRRASES PRIGMVFTGQ VFRRSIEEAE TYLNALGADW SLLEELQRDK
KTTKVHETKI SIPICVALQI ALVRLLESWG ITASGVASHS SGEISAAFAV GALTHHQAIA
IAYFRAIIVA DGTQRAPGSA KGAMAAIGLG VGTVQPYLDR LTEGKAVVAC VNSPQSVTIS
GDEDAIDEIT DLCKQDGVFA RRLKVQQAYH SHHMDPFADT YRERLRIEMD RSVVKGDKQK
LKAVFSSAVT GGRITDIKEI ASPDHWVGSL IRPVEFVDAL TELVLGDPDD PTGRSVDVLL
EVGPHTALGG PIREILSLSE FGGIELPYWG CLVRDEHAGD SMRSAAINLF REGQSLAMDK
INFPVPAYDG EGPQVLTNLP SYPWNHTMRH WQESRVNRAI RERGQPPHEL LGMPVAGNDP
SASVWRRVLR VTETPWLRDH MVQGSIVYPG AGYICLAIEA VRQLTDQDKS VSGLRLRDIN
FLFALVIPDN ADGVEIRTTL QSVPEREIGA QGWWRFEVSS VTLENRWTLH ATGMVGIEES
AVLETERRRR PLSIYTRQPN PQDLFANLRA HSVYHGPLFQ NTNRIIQDGR EPRSICDITI
RHEASSDTDP EVAAQNSLLH PITLDAVFVA FYSALPSVGA LQEEPKLPRS VRAMWISSNI
SHQIGHTLQC DTSLLNDDPQ RGRADITVFD GKTDATVLKI QGVELAALGR GSSASTSTEV
CSRVVWEPDL SFRNPLAFEQ IKKHLASTNS DQEADVVRDL QRLCIAYASD ALRELTPGDV
AGLQEQPHLA KYYAFLRGLV NKTTEEPGKP QQSMESVDEK VVCRLGPLLP SILRGERSVE
EVRSLMDEYN TNSRRQLSSL RQLSALLQTI AHKSPGARVL QIGSSTGALA TRRILETLDT
NLVASWHITE PSSELLDNAR AQLADWADLL QFEQLDIEQS PFKKKFIPES YDVVVSLHAL
HAIKNPASAL GNVRTLLKPG GTLLLVETTK NQVDVDFVFA LRPGWLQDKN PLTSWDAVLQ
DGGFSGLDLE IYDSESDIHT NSVIMSTVPA KDQKADLSKV KDSFAVVSSI KTPPSSPIVD
QLCQRIQALT GTATTHLVLE KTSGNTYKDK ICVFIGELDR PILADLDAVQ MEGLRAMVTQ
CSGLLWVTTG GTVEREAPER AVHQGFLRVL RNEYISRYFI SLDLDPAHAD AGAAGWSSGA
NPAVSAIVQA LEEGFGHGST RTGPAEFEYA ERNGVLHIPR YYKDEKYNNM VTCPLAPSWS
DHDERSIPLE RLFQDRQLRL QVGIPGHLGT LAFAENEANH ADLPPELMEI TPRAHGACSR
DVMAAMGQLK DQAMGFECAG IIARLGSEAY SKGYRVGDRV MALSAGASFA SNVCVPWHGV
IQMPKDMDFV SAASLPLAFT VAYFGLVRSA SLTTGQSVLI HAAAGAFGQA AIMLAKHLGV
TEIYATVGSP EKQDILEREY GIPSERIFSS RDASFAPAIL AATKGRGVDL VLSSLSGPLL
QESLSTVAPL GYLVNIGKAD IERNSLMALE SFSRGISFVS MDVPTLLQRR GPDVHRTLGE
ITSLVEQQVL KPVYPVTVYP MQDVQAAFRF VQTGDQMGKV VLSAGSDEQV YVVPRPKGLT
TQSQLRPDAS YLIVGGVGGI GRSVAHWLVA HGAQHLILLS RSAGNLDLDQ NKNSDGAFFI
NELRHMGCRV KPVSCDVSLA SSLTVALRAC EDDGFPPVRG VIQGAMLLRD AIFEQMTLDD
WRSGLSPKLY GTWNLHTEFS QPDSLDFFIM LSSVSGVAGI ASQSNYAAGG SYEDAMARWR
QSQGLPGVAI DLGPISDIGY VSTDPRVAER LRKDGEFAML DEGIVLRALN AAILHPLGRS
QIIIGLTSSP GPHWDPNGRS QLGRDARYAT LRPHTKVSAR QDGESTSASL ATQLADTNDP
QEGARLIGAA IAEKLADIFM TPIAEIDLSK PPAHYGVDSL IAVELRNMLA LQAAADISIF
NILQTASLAA LAGLVAEKSR HFQA
