DBAI_EMENI
ID DBAI_EMENI Reviewed; 2605 AA.
AC Q5AUX7; A0A1U8QHY2; C8V4K3;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Non-reducing polyketide synthase dbaI {ECO:0000303|PubMed:23001671};
DE Short=NR-PKS dbaI {ECO:0000303|PubMed:23001671};
DE EC=2.3.1.- {ECO:0000269|PubMed:23001671};
DE AltName: Full=Derivative of benzaldehyde biosynthesis cluster protein I {ECO:0000303|PubMed:23001671};
GN Name=dbaI {ECO:0000303|PubMed:23001671};
GN Synonyms=pkeA {ECO:0000303|PubMed:22510154}; ORFNames=ANIA_07903;
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, FUNCTION, AND PATHWAY.
RX PubMed=23001671; DOI=10.1128/aem.01808-12;
RA Gerke J., Bayram O., Feussner K., Landesfeind M., Shelest E., Feussner I.,
RA Braus G.H.;
RT "Breaking the silence: protein stabilization uncovers silenced biosynthetic
RT gene clusters in the fungus Aspergillus nidulans.";
RL Appl. Environ. Microbiol. 78:8234-8244(2012).
RN [4]
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).
RN [5]
RP INDUCTION.
RX PubMed=25701285; DOI=10.1534/genetics.115.174342;
RA Oiartzabal-Arano E., Garzia A., Gorostidi A., Ugalde U., Espeso E.A.,
RA Etxebeste O.;
RT "Beyond asexual development: modifications in the gene expression profile
RT caused by the absence of the Aspergillus nidulans transcription factor
RT FlbB.";
RL Genetics 199:1127-1142(2015).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of the antibiotic 2,4-dihydroxy-3-
CC methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives
CC (PubMed:22510154, PubMed:23001671). The direct non-reducing polyketide
CC synthase dbaI product is 2,4-dihydroxy-3-methyl-6-(2-
CC oxopropyl)benzaldehyde (DHMBA), produced by condensation of one acetyl-
CC CoA starter unit with 4 malonyl-CoA units and one methylation step
CC (PubMed:22510154). The FAD-dependent monooxygenase dbaH is responsible
CC for the synthesis of yellow pigments derived from the oxidation of
CC DHMBA (PubMed:23001671). The roles of dbaB, C, E and F have still to be
CC determined (Probable). {ECO:0000269|PubMed:22510154,
CC ECO:0000269|PubMed:23001671, ECO:0000305|PubMed:23001671}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + AH2 + 3 H(+) + 4 malonyl-CoA + S-adenosyl-L-
CC methionine = 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde + A +
CC 4 CO2 + 5 CoA + H2O + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:64508, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:155860;
CC Evidence={ECO:0000269|PubMed:22510154};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64509;
CC Evidence={ECO:0000269|PubMed:22510154};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:22510154, ECO:0000269|PubMed:23001671}.
CC -!- INDUCTION: Deletion of the conserved eukaryotic csnE deneddylase
CC subunit of the COP9 signalosome leading to defect in protein
CC degradation results in the activation of the silenced dba gene cluster
CC (PubMed:23001671). Expression is positively regulated by the dba
CC cluster specific transcription factor dbaA (PubMed:23001671).
CC Expression is also controlled by the transcription factor flbB
CC (PubMed:25701285). {ECO:0000269|PubMed:23001671,
CC ECO:0000269|PubMed:25701285}.
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 domain, a
CC acyl carrier protein (ACP) domain, a methyltransferase domain and a
CC reductive NADPH-binding domain that is required for NADPH-dependent
CC product release. {ECO:0000305|PubMed:22510154}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF73494.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA59557.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000135; EAA59557.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001302; CBF73494.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_681172.1; XM_676080.1.
DR AlphaFoldDB; Q5AUX7; -.
DR SMR; Q5AUX7; -.
DR EnsemblFungi; CBF73494; CBF73494; ANIA_07903.
DR EnsemblFungi; EAA59557; EAA59557; AN7903.2.
DR GeneID; 2869225; -.
DR KEGG; ani:AN7903.2; -.
DR VEuPathDB; FungiDB:AN7903; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_16_2_1; -.
DR InParanoid; Q5AUX7; -.
DR OrthoDB; 19161at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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; 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; PF08242; Methyltransf_12; 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; 2.
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; Transferase.
FT CHAIN 1..2605
FT /note="Non-reducing polyketide synthase dbaI"
FT /id="PRO_0000446352"
FT DOMAIN 1665..1739
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 97..243
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT REGION 385..801
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT REGION 908..1195
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT REGION 1316..1594
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT REGION 1742..1780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1963..2151
FT /note="Methyltransferase domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT REGION 2230..2473
FT /note="NADPH-binding (R) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22510154"
FT COMPBIAS 1745..1773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /note="Nucleophile; for transacylase activity"
FT /evidence="ECO:0000250|UniProtKB:A0A0K0MCJ4"
FT ACT_SITE 262
FT /note="Proton donor/acceptor; for transacylase activity"
FT /evidence="ECO:0000250|UniProtKB:A0A0K0MCJ4"
FT ACT_SITE 547
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1699
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2605 AA; 288997 MW; D720ECCE904A1C6E CRC64;
MLGHRDFTTL PLSRREFLLF GPLALSFDQA AFEHLRKTIV NSEEHRWALE VLGSLPQYYA
TIVNAFPGIN GRNEVQLEDL KGALHSGKPL ATSFPLPNTL LIPLVMVLHL TEYSRFLQEI
SEELESGIDL FDASRHNKET VGFCTGLLSA MAVSSAGSRE DFRKYAAVAV RLGLLVGVVV
DSHDISSAQG PSKSISASWN SAQKREDARR IMDEFPQAYI SVYYDEDRAT ITAPASEISD
LHRRLRASGI VTAEIGLNGC FHADCYLDQL DPIIQFCDSQ PDFQLPDASK VVIPTRSNAT
GELIRDGALH QHALRSILVE PPQWFESFTA VRDACAEDEG AIIFSFGPER CVPPSLLRVL
SQKVVTVEDL DVLKRYQYSY SENDIAVVGM SCKVAGANNL EEFWDLLCTG KSQHREVPKE
RFSFETVFRD VDSKRKWFGN FIDGHDQFDH KFFKKSPRES ATMDPQQRHL LQIAYQAVEQ
SGYFHSANPD RQIGCYMGVC ACDYENNIAC HAPNAFSATG NLQGFIAGKV SHFFGWTGPG
LTIDTACSSS AVAVHQACKA IITGECTAAL AGGTHVMTNP LWFQNLAGAS FLSTTGQCKP
FDAKADGYCR GEGIATVFLK KLSAAVADGD QILGVITATA VQQNQNCTPI FVPNVPSLSD
LFRVVVKQSR LQPSDVTVVE AHGTGTAVGD PAEYDSIRSV LGGSSREKTL ALSSVKGLVG
HIECTSGIVS LIKVLLMLQK RMIPPQASFT TINPAIKATP ADKINIPTTV KTWDAEFCAA
LINNYGASGS NASIVVTQPP VGTVKPSAET SGLKYPFRFC GMDEQSLRRY SKIFRQFLNR
KSYSAQDLSL RNISFNVNRQ SNRQLDRTLL FSVKTLEELE QKLVTFENDN DSITSLALPK
SKPVVLCFGG QVSTFVGLDR TVYERVAILR KHLHTVDAVA RSIGLKSIFP RIFETTPVSD
TVHLQIMLFA SQYACARSWI DSGIQPVAVV GHSFGELTSL CVSQSLSLED AVKMIAARAT
LIRDAWGPEK GAMLAVEADL EDVQKLLAES SAGCQDVQPA TIACYNGPRS FTLAGAVAAI
DAVAEALATP AFSSMKNKRL NVTNAFHCAL VDPLLDRLEE SARELTFRAP VIPVQRATEY
QTEELPTSRF VADHIRSPVF FNHAIHRLAD KYPSCVFLEA GSNSTVTNMA SRALGNPSSS
HFQAINITSH NGWNNLVDAT MNMWKSGLGV HFWAHQPSQT KEYALLLLPP YQFEPSRHWI
ELKNPPKLTA APAIEEVKKE EAKVPNTLLT FVGYQDSERQ QARFRVNTMI PKYDKLIRGH
IIAQTAPICP ATVQLDLVIE SIRSIRPELA STEHEPQIHA VENLAPICVN PLRAVWVEVT
ADDVAQGTSW NFQVYSDDLQ NGFSKTIHTT GRVIFRSISD VSLKYEFARF ERHFRHQTCV
ELMRGGEVDE VLQNRNIYKM FAEIVDYGED YRGLQKLVSK GNQSAGYVVK KYNPESWLDG
HLADSFCQVG GIYVNCMTDR VPNDMFIANG IEQWMRSPKM RQQDPRPESY HVLATHHRPS
DKAFLTDVFA FDSTTGVLIE VILGISYVKI PKASMSKLLS RLTVNDSASC PTNMPLLSKS
ASVNLFDAPE NLSTPSLSVA PTQQSAPALS LSKVKKVKND GPDKGQLTQR IKSILAELSG
LEIAEIKDDS ELADLGIDSL MGMEMAHEIE KAFTISLPES DLMEVVDVPS LIKCVRKAMS
GDADSAEYTT EQSTSEAADS DDKSTNYTTP STPGEEALDM DKSMREFLGK EGTELNLPFE
TVMKAFNETK NMTDDRIAEY QQTRYVESVL PMQSQMCVSL VLEAFDQLNM RIRTAPAGEK
FTRISHPKEH TRLVDYLYKM LEDASLINID GEVITRTAIQ VPRPSKEIFD ELVSQHPDQN
AADKLTFYTG SHLAEVLKGE TDGIKLIFGT QDGRELVSKL YRDWPLNRLF YRQMEDFLER
LTSKLDISQG VIKILEMGAG TGGTTKWLVP LLAKLNIPVE YTFTDIAPSF VAAARKKFSK
QYPFMKFRTH DIEKAPADDL IGSQHVIIAS NAVHATHSLS ESGKNIRKAL RPDGVLLMLE
MTGTLHWVDI IFGLFEGWWY FDDGRTHAVT HESRWAKDLQ AVGYGHVDWT DGVRPENKLE
KLIIAFASGG RYERLHIPRP LESASADCAA RQAVVDRYVQ EMTAGFGAAT GVSPSAPLAH
QEPKGCCVLV TGATGSLGCH LLAALTSLPT IASVVCLNRR SRQDPLERQH RSLLEKKIFL
SEETAARVRV IETDMSKPQL GLLEEEYNYL LNSVTHIVHN AWLMNAKLPL RRFEPQLQIM
RNLLDLAYGI SLQRPMEKVS FQFISSIATV GHWPIWTGKS SVPEERMAIE SVLPTGYGDA
KYICERMIDE TLHKYPDRFR AMVVRPGQVA GSSTSGYWNT MEHFSFLVKS SQTLNALPDF
DGVLSWTPVD VVASTLVDLL LLPEDKTPYS IYHIDNPVRQ PWKEMNVVLA DALHIPRSNI
IPFEKWIQRV KDYPRQVEGA EGDNPAILLV DFLDNNFIRM SCGGLLLETK KSREHSKTLA
NLGPVSAETA RLFIKSWIDM GFLSP
