ID A2R4Z4_ASPNC Unreviewed; 2622 AA.
AC A2R4Z4;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE SubName: Full=Contig An15c0100, genomic contig {ECO:0000313|EMBL:CAK42316.1};
DE EC=2.1.1.- {ECO:0000313|EMBL:CAK42316.1};
GN ORFNames=An15g02130 {ECO:0000313|EMBL:CAK42316.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK42316.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK42316.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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DR EMBL; AM270337; CAK42316.1; -; Genomic_DNA.
DR RefSeq; XP_001396752.1; XM_001396715.1.
DR EnsemblFungi; CAK42316; CAK42316; An15g02130.
DR GeneID; 4987814; -.
DR KEGG; ang:An15g02130; -.
DR VEuPathDB; FungiDB:An15g02130; -.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000006706; Chromosome 3R.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
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; IEA:InterPro.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd05274; KR_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
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; 1.
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; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR018201; Ketoacyl_synth_AS.
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; 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; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
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; PF08242; Methyltransf_12; 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; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Methyltransferase {ECO:0000313|EMBL:CAK42316.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAK42316.1}.
FT DOMAIN 16..440
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2541..2618
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 453..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2622 AA; 286812 MW; CD04B27641942841 CRC64;
MEDPTTTLPE LDGIDSNDIA ICGFSLKFPQ DATTPEALWD MMLQRRCAMT EFPADRVNVD
GFYDQRSRPN TMPLKGGHFI KGDLAEFDAG FFSIAPTEAA SMDPMQRLLL EASYHALENA
GIPMEHVNGS PTAVYCGSFG MDYMLQLVRS AEVPPPYAAL GFGLSMLANR ISWFFNFRGP
SMAVDSACSS SAMALDTACA ALRNGNCSMA LVAGSNMASA PEPYVWMSNV KFLSPDSCCY
SFDERANGYA RGEGLAVTVL KRVSDAVRDG NTIRAVIRAT ACNEDGRTPG ITQPNRKAQE
ELIKRTYEQA RLSMEHTRFF EAHGTGTPAG DPREAQAIGM AFMRHRSNDD PIYVGAIKSN
VGHLEGASGL AGLIKAVLVL EKGIIPPNAN FQKVNPKIDV EFLNISFPQK ARPWPANGLR
RASVNSFGYG GANAHVVIDD AYNYLRIRGL NGKHNTAKRP PQLREQSDKM PLSPALTPPR
QENVQRLFVW SASDKDGIGR IIKQYSTGYS PIKQLLQKYQ QLRQQGGKES IDATNDITNL
MANLAYTLDT HRSHLQWRSF ALMNTIEDFE NISSLMSTPV SAQAKSPPRI GFVFSGQGAQ
WQGMGRELAC YGSFRTELVQ ADAYLRSLGC AWSVVNHIVY PDPSNDIDNP ELSQSLCTIL
QVALVNLLRR FGVRPAAVVG HSSGEIAAAY ASGHISLELA WRLAYFRGVC SAKLDRDGHL
ADSGERVSGA MMAVGLSEAS GKELLSAHGH VASSVSVACI NSPQSITLSG DDAAIDYLQG
VLEEQKIFAR KLRVKVAYHS RHMDSIAVDY VSMINAYADA NDMVPFSSEI PMVSSVTGKV
VSDASVAEAS YWASNMVSPV QFSQAVSVMC RQGAKDVTKK LDQSHLLVPA VDGLLEIGPH
ATLKSSLRDI LETSPRGQLG YNAVLFRKKS AVDTLLSTLG QLHCEGVNLE FRAINEPSGS
VMTRSMLTTL PEYPFDHSQR YWHDSRLSRS YKQRSKRPSD FHGTRSNDWN RSDARWNWKM
DLSDMPWVEH HIVNGMTLYP ATGMLVMAIE AGKELCEEEG YAVNAFTFED VHFKTPINFT
ASNDGPEAQV SLREELPQDR SSASKFSFII RTFGNDDWSE NCQGHITIHH RGKEEGWLSD
HEARQQKNMA KTLLDNASAC SQQISAKQMY EYLKETGYEY GPIFARCDEQ RIHSTLKHAT
ATTSLYNSPN QGHVVHPASL DAILHLAFTA LTSGGRSSMA TSVPSRIGCL WLSASGLSSL
ETDRLTCLSR VTSVTGRGFT VAGGSVSVDA ANDLRVWFQD FELANITSTP SSLAFVADPK
QFCMNVEQKP AIDKLDNCQL SEYLHKIHPE TGDLTAFYED VTLLINHSVH TLLASVDPRV
ITADSGKGDW KRRYLHWANY HVTEGRLGAS PALTESIDTV CDRVKSANRV GRLYTEVTLH
LGEFFRGSVT PLDRLMQTGL LGEYYDELMT YRCMKQVITF VDLLAHQNGG MKFLEVGGGT
AAATRHLINA LSMNGPSGVT ESSNSPGSLR CEQYCFTDVS ATFLEKARDE FSDHQSQMSF
QTLDIEKDFS EQGVSDGTYD VVVANAVLHI TADLENTFRN VRKSMKTGGK LILTEFLQPD
GWALGFIFGL FPGWWVGPEA DRPLSPLWSA EGWGRILQSC GFSGVDMVFK DFDGPAHQLG
CVISTAVDVP SSVPRSLASP TYHSGTIVKL NNFPQQQSLA ASLVTSLQDM FTEPLEIVDA
NMLAPSTSLA VSSNRLCIAL VDYGAPFLSS MTEQDWAVLK VLAQACPGML WVSAGGGASA
APEYGLIDGL SRTLRAENYS LHLVSVALDM NRNGTSGHIH HLKQIVREML SRKPSQEYEQ
EYIEVDGCLH TRRLVEARYL KANMESNILP WQMTSANAID ASFELSAACP EDNNGIPYLV
EVPAPIIEDA LPINVRAISL QYQDQLAARG LAPKGTQLGN FCSGIVTETL PGSSFAQGDR
VFAVHKNCFR SVAAVQPSSA VKLPDYLSFE DACWAIPSVL TAHHALSDIG RVRNRDCVLV
MDGCSVLGEA AVGLLLNEGV AEIWLTADSI EDCQRASKKF NIPEKYIIPT SAMGTAFSST
WSDLQPKFDI VFATTSVAKG LGEQTFRGMM QKNGRVVLVS DDASQSAFRF GSSSLHVSFM
ASDELQVSQE SLEYAVSTPI LQLLLDSRGQ VPMFPISRLD EIMAFLKQST SSDAAVVQLT
ESDTVNVRSM RKKIDYIDSN ATYIISGGLG GVGRSIARWL ANNGAQYLVL LSRSGPKTHE
AQSLALEFQD RGVRCEMPAC DVTNPSALRA LLDKYSTTMP PVKGCIQAAM VMEEGIFSEL
SLSSWKGTLQ PKVQGSWNLH AMLPSNMDFF IMLSSVMGTL GTGSLAPYNA GNTYQDALAR
YRVSQGQRAI SFNLGAVPDA GYLVTNAEYA TGRRQIHETA KYTPTYIRDI VALLEIFCDP
SNKLATHPST CHPIVGIRPP SHWGHLEEVS FVLSQPFWQH MHHIPLPAGE AGDVDNVHGP
RPGRQAKDVV AKLAAATSVN ERTELVSEAL AARITALLGV PEGQLDLHRP MHSYGLDSLS
AIEVRNWIGK TFSVDVPVFM ILGGITFEGA AATIVHQFQS QN
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