ID Q5AX96_EMENI Unreviewed; 2388 AA.
AC Q5AX96; C8VDF2;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 137.
DE SubName: Full=PKS-like enzyme, putative (JCVI) {ECO:0000313|EMBL:CBF79115.1};
GN ORFNames=ANIA_07084 {ECO:0000313|EMBL:CBF79115.1};
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 {ECO:0000313|EMBL:CBF79115.1, ECO:0000313|Proteomes:UP000000560};
RN [1] {ECO:0000313|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
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., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M., 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., Hynes M., Paoletti M., Fischer R., Miller B.,
RA Dyer P., 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] {ECO:0000313|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
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).
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DR EMBL; BN001304; CBF79115.1; -; Genomic_DNA.
DR RefSeq; XP_664688.1; XM_659596.1.
DR STRING; 227321.Q5AX96; -.
DR EnsemblFungi; CBF79115; CBF79115; ANIA_07084.
DR GeneID; 2870061; -.
DR KEGG; ani:AN7084.2; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR InParanoid; Q5AX96; -.
DR OMA; KDVQHYT; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000000560; Chromosome IV.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF18; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 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; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 96..524
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2310..2386
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2388 AA; 260559 MW; 831C974559842A57 CRC64;
MALTGCRTRR VRWTPNAHLV NWSATFGTLW SINTGAYQCG RYIVRWIAAL GRLLISLPSP
QNDLVDICLV SIGAVYYLFK MNGITSTSLP SPRYHFEPIA VIGFACRLPG NNNSPTALWD
FLERGGVASR AVPASRFNLA GHENGSKRPG TMRTPGGMFL ESINPADIDA QFFGLSRAEA
TAMDPQQRQL LEVVYEGLEN AGITLEQLRG QDVGCFVGSY ASDYGDIQAR NPDDRAPNST
VGIGRAMLSN RLSHFLDIKG PSMTIDTACS GSLVSLDVAT RYLQTGEIRA AIVAACNLYM
SPEHCIDISS SIINAASLTG LCHTFDAKAD GYVKAEAVNM VIIKRLQDAI RDRDPIRSII
RGSASNSDGW TAGIASPSSE GQAAVTRQAY RIAGIADFNA TSYVECHGTG TRAGDPIEVK
GVASVFCPER PAERPLLIGS VKSNIGHSEP GAGISGLLKT ILALEKSVIP GNPTFETPNP
EIDFDGLKTR AFQHATPWPS MPFKRASVNS FGYGGSNAHV ILDEAKTGVS ASEMCFKSSY
LPEDHDPFEE CEENEKCFPQ LLVFSANDEK SLQEYIRALR AHLINPRVRI SLQDLAYTLS
ERRSRHFNRA FLITQTSLNL DLHGLVFGKL RSSSPRVGFI FTGQGSQWPQ MGKSLLDMFP
SGRGQLARLD RALQLLPDPP EWSLYGAGHH VLEELLQAHR DSIAVACINS PESVTLSGPL
NVLKTANMVI QEKGYFARLL QVNMAYHNPM FMTDITAQYK QMLHGLGLDS MSSPVSKATK
EQRTVKMFSS VTGLETMGPC NVEYWCSNMQ YPVQFNQAVR MMLSDEKQPI NFLIELGPSG
ALASPTKQII QSMRDKKPDL AIEYHAAYKR DVVTAAMGLF EVAGHLYLSG GAVDIEQVNS
HHAHREKDQH QPSVIVDLPN YAWNHSIKYW YESQSSRDWR FRHYPNHDLL GSKILGTSWF
APSFKKVLRL ADLPWLRDHR VAGQPLFPAA GYIAMAVEAA YQTGQRSGMI DTGLKVSQVP
YRFRNIKFVR ALVLDEAAPS TLMLSMSPER GWYKFSVYTA DGESVPTIHC EGLVSLHVEV
GKAPPSSAFK QLLYPTPARL WYKAMDKVGY NFGSAFQTQL QIESVVGTRQ NRALVSFLEP
QSAYAQSLYS IHPAVLDGCL QSGAPALWNG VRSAVRECLV PAIIEDLVIS ARQTAARSGA
SVCSAEYSGV GSRDEPCSYK SNIIVSDPAT GDTLIRVRGL AYSALDREEA FSQFTPSMRL
EWKPDISFLS RNQLYRILDT CDTRFAPYSA HDDSRALSFI SLLLHKKPAL RVVEFNIAPS
TDSSFFAILG HIPFTAKGAV EYHFVSNNAA ALVAFQGMAD GCGLPNVQLS ALDVSRLDID
SHLLGDKADL AVLNTDHQIC GEKLHNAIVN IAAILRKGGF ILILAHQSST NQVQARPWDG
HSASINDALG RHGFKKSVAF DMGTETHAIV GQLLLPVREP SAELQVSLVL LSSSTDSALA
SQMLAESGVT VAGIHYLPLG EIRKDLIILI TDEMFKPVLA EVTQEQWGAI QRILAFGCKI
VWVTSGAQKD VVSPLQALVS GLSRVVRAED PTISFTLLDV ESPYSKKSFR AIADVLERVD
NGNTSSGLVD EEYEYVERGG IVHVSRVYPD IASGGDGKAV IQNLHNHASC VRLTCQAPGF
LESLQFTETG PSEAVVPDGF VEVEMHAAGL NYKDVATVLG IVPENQYLLG LEGAGVIRRI
RHHAGDSPFY IGQRVAICRR GSFANRVQCP IEGIHAIPDW MSFEEAATIP IVYQAALYSL
VDLANVQWGQ SVLIHSAAGG LGIAAIQLCQ YLGAEIYATV GSDEKREFLI REFNLSPDRL
FSSRDTVFAS CIIEQTGGRG VDVILNTLTG SLLDESWRII AAHGTMVELG KKDILDRNSL
SMEPFNRNAS YRAFDLSHPS ITRPLVARLL KRIFDLIHGG HIRPIAPRTV YAYSNIAAAI
RYMRGGAHIG KIIISRDAPQ NCTDVPVMPV QKSLKLRGDV SYLIVGGLKG LCGSLATYLA
CHGAKHISVM SRSDYTDDKS KAVLRDLTLL GVNCSLVRGD VSVKDDVQKA FCKGSRPPVA
GVIHGAMVLK DTIYTSMTAA QFHDALRCKV QGTYNLHDVA LQLGLDLDFF TLLSSLSGLV
GHKGQANYAA ASAFLDSFAL YRRSKGLAAC SVDLGIIDDI GYMAEHESIT DRLDTETWIP
LNEVQLHRIL YTSILQERDQ RSTGTSQLIT GIAYPAPAVP SALYQDARFT ALCQKSANSN
SASISIKGGA RDMQVQALLT LVQAKADAAV QIAAMIDAAN AHFMRSLALS EPMEAAKPLV
LYGLDSLAAV EFRNWARREL NVVVSTLDVL GAKTLNALCE MMVGRLAG
//
