PKDA_EMENI
ID PKDA_EMENI Reviewed; 2476 AA.
AC Q5BG07; C8VSV1;
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=Non-reducing polyketide synthase pkdA {ECO:0000303|PubMed:22510154};
DE Short=NR-PKS pkdA {ECO:0000303|PubMed:22510154};
DE EC=2.3.1.- {ECO:0000269|PubMed:22510154};
DE AltName: Full=Pkd biosynthesis cluster protein A {ECO:0000303|PubMed:22510154};
GN Name=pkdA {ECO:0000303|PubMed:22510154}; ORFNames=ANIA_00523;
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 that synthesizes 6-ethyl-
CC 2,4-dihydroxy-3,5-dimethylbenzaldehyde via condensation of one
CC propanoyl-CoA starter unit with 3 malonyl-CoA units, as well as 2
CC methylation steps. {ECO:0000269|PubMed:22510154}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + H(+) + 3 malonyl-CoA + propanoyl-CoA + 2 S-adenosyl-L-
CC methionine = 2-ethyl-4,6-dihydroxy-3,5-dimethylbenzaldehyde + A + 3
CC CO2 + 4 CoA + H2O + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:64504, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:133958;
CC Evidence={ECO:0000269|PubMed:22510154};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64505;
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; BN001308; CBF89312.1; -; Genomic_DNA.
DR RefSeq; XP_658127.1; XM_653035.1.
DR AlphaFoldDB; Q5BG07; -.
DR SMR; Q5BG07; -.
DR STRING; 162425.CADANIAP00002162; -.
DR EnsemblFungi; CBF89312; CBF89312; ANIA_00523.
DR EnsemblFungi; EAA66622; EAA66622; AN0523.2.
DR GeneID; 2876299; -.
DR KEGG; ani:AN0523.2; -.
DR VEuPathDB; FungiDB:AN0523; -.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_2_1; -.
DR InParanoid; Q5BG07; -.
DR OMA; LATNCVH; -.
DR OrthoDB; 13314at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
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:0019748; P:secondary metabolic process; NAS:AspGD.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:AspGD.
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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
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; IPR032088; SAT.
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; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF16073; SAT; 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..2476
FT /note="Non-reducing polyketide synthase pkdA"
FT /id="PRO_0000450875"
FT DOMAIN 1650..1724
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:22510154"
FT REGION 22..230
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT REGION 389..632
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT REGION 919..1204
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT REGION 1321..1590
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000305|PubMed:22510154"
FT REGION 1626..1649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1727..1766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1881..2030
FT /note="Methyltransferase (CMeT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT REGION 2094..2340
FT /note="NADPH-binding domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT COMPBIAS 1626..1648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1743..1766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="Nucleophile; for transacylase activity"
FT /evidence="ECO:0000250|UniProtKB:A0A0K0MCJ4"
FT ACT_SITE 261
FT /note="Proton donor/acceptor; for transacylase activity"
FT /evidence="ECO:0000250|UniProtKB:A0A0K0MCJ4"
FT ACT_SITE 554
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1684
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2476 AA; 271658 MW; A886999650797965 CRC64;
MASSSSSTQA ENLILIFGPQ DPNLNDAYLQ SLRTNLLDSP FLQWIVHTLI QLPQEWQRIA
PTHTELGSFQ GQKYLQLLSE WMRKGTLPGN IFPLPNILVT PLVVTTHLAQ YTKLLEQLNP
AIATNDMLSG IVKHDIQTVG LCTGLLSSAA VASSATLAEL EKHGAAAIRM AMAIGALVDA
GDTEVEDGDK WQSLAVGWTT QNGDAELEGI SKQFSHAYVS VISEARLATL TMLKNDANAI
QRELTNAGFI YTKTALRGPF HCGSREDQAV SLMRLFDSDP SFQFPGASTL VFRTRAPDGE
EFPLDRSLHG AAARAMLTDQ ADWHKLYTKL HESTNSHPGI VITFGSQRFI PQWFLRKLGP
RLAHVLDLDV GSGHWPAPLY TLQDSGQDES IAVVGMACNF PGGSDLDEFW DTVCAAKSQC
TEVPPERVDF DYEAWRENDT QRKWFGNFIR EYDTFDHKFF QKSPREMIST DPQHRIMLQV
AYQAVQQSGY FNRPGRSKHV GCYVGIGVTD YENNVACHPP TAYTATGNLK SFAAGKISHF
FGWSGPGVTV DTACSSSALA IHLACKAILS GECDASLAGG VNVITSPEWY QNLDGASFLS
PTGQCKPFDA AADGYCRGEG AGAVFLKRLS SAVEDGDQIV GVIRATSVNQ NENCSAITAP
SVRSLANVFN GVIRKARVDP KQISVVEAHG TGTQVGDRAE YDSIRTVLGG PGRAYPLSLG
SVKGLIGHLE CASGIAALIK VLLMVQNGII PPQPGFSKIN PKLEALPSDN IEIPTSLRPW
NPGFRAALLN NYGASGSNAS LVVTQAGVPH LNQSAIPKGA SAGRRPFWLS GTDVQSLRSY
AAKLVQMLRS RKADDPRFTV ANLSFQLARQ SNRNLGQALI FSCASVDELE AKLADFASGG
NTLTSVPRPD SSRPVILCFG GQRSSFVGLD REAFDSFKLL KSHLTHCHET SLALGLGGIL
PAIFDRTPRS SIVELQLMQF ALQYSCAKTW IDSGIHVAAL VGHSFGELTA MCVSGTLSLQ
DTLRMIAGRA RIIEEKWGPD RGSMMAVDGE LELVQRLLHN AHEASPNEPA VNIACFNGPR
LFTLAGTTKA MRVVREVLSK DNRLSSIKVK SLETSHAFHS TLVEPLIPDL EELGEESIFR
KPVVVHERAT QNSVAGPPPF SIFASHMRDP VYFDRAVQRL ANRYPSSIWL EAGSGSGVTN
LASRAAGSRA MAFQSINITS SSAVQNVADA TLNLWKEGLQ VMFWEHVRPS PKFPLLLLPP
YQFAKSRHWL ERRKLKTKVF VPASPVQEAQ KGLWTFVGYQ DSDRCQARFQ IHITSDEFQN
YVSAHVIAQT APICPSMFQQ VIARDALATL VDGDMIPELE GMENDTPLCL DGSKSVWLVA
ERPSDRSSAW DFRITSSDSG NTTQHVSGRI TFQTPKQSMQ AFAAYERLVD HRRALALLNG
QEAEQTIQGS RNIYKLFSNV VNYKEDGYRG LQKLAATSNE SAGRIIKQDS SKSILGVGLG
DTFCQVAGIF LNCMTDCDEG KMYLSNRVER WIRSPTVPLD LRPEQWEVYA RHHQPSPKEY
VSDIFVFDAT NGKLVWVILG LHFVEVSIAG MSRFLTRLSG GQLEPQEKCL ATVEFKEVPE
PVFTKDVSKN EKDAKAPSKK KESTSKSPGH DILARVRTLF CNLLGLEPVE IQPGADLVEL
GIDSLLAMEV AREVEKEFSI KFELDELMDM TDVHSLVKCI GANMMASDTS RTGDDSSDDL
ETASAESETS SGINNEDSHN IDRQQIPASS IVDSFTETKL LTDRFIEANK LSGYSNNVQP
RLTELVIVHT LDAFDQMGCS IRAAQPGQTV RRISHLPKHN QVVAVLYGLL EKASLVDVDG
PRMTRTAVPV PSKSAEQILQ ELLRQYPEHA YDHKLTSLTG CKLADCLTGK TEAIQLLFGT
PEGRDLAAGM YGKSPINVAW LRQLQHFWEH FLAQLPQHRT EPINILEMGA GTGGTTAALV
PLLSRSRIPV RYTATDISPS LVAGLRKRFK DHTWMRFEVV DCEKTPSSHL FESQHVVLAV
AIIPPAPSKM STADIASRQA IIDTLVEKHT SHFSAPTCLP PNQVIDGSPH CVLVTGATGS
LGSHLVAHLV KQSSVTKVVC LNRVSGSDAT SRQLDAFQSK GLILDSESLS KLEVIETDSS
APSLGLVPER YQHLVNTVTD VVHNAWAMSM TRPVRGFEPQ FKTMRNLIDL CRDCANRRHS
DTGKVGFQFV SSVSVVGCHP FITKKAIVPE QPVNAESALP MGYADAKLVC EHILDETLHM
HPDIFRTMSV RVGQISGSKI NGYWNPVEHL VHLIKSSKTL NVLPDLEGVL SWCPVDDVAA
ALGDLLLTNK PAYSVYHIEN PVRQPWPDML TILADALDIP RTNAVPFKEW LRRVRHFPPS
LGFSENPAAR LADFFETDFL RMSCGGMILD TTRSREHSAT LRSLGPIDQD LVMKITFKRI
YAIFAKSSEV KIKKSS
