ID A2QDU0_ASPNC Unreviewed; 3907 AA.
AC A2QDU0;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE SubName: Full=Contig An02c0260, genomic contig {ECO:0000313|EMBL:CAK37791.1};
GN ORFNames=An02g08290 {ECO:0000313|EMBL:CAK37791.1};
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:CAK37791.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK37791.1, 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).
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
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DR EMBL; AM270021; CAK37791.1; -; Genomic_DNA.
DR EnsemblFungi; CAK37791; CAK37791; An02g08290.
DR VEuPathDB; FungiDB:An02g08290; -.
DR HOGENOM; CLU_000022_37_8_1; -.
DR Proteomes; UP000006706; Chromosome 4R.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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:1901566; P:organonitrogen 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; cd05930; A_NRPS; 1.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation 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; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR013120; Far_NAD-bd.
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; 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; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF20; HYBRID PKS-NRPS SYNTHETASE APDA; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 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; PF07993; NAD_binding_4; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-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; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
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}.
FT DOMAIN 6..459
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3430..3507
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2417..2448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3907 AA; 429025 MW; 50EBBEE4E5060C85 CRC64;
MAYPQAEPVA IIGSACRFPG ANSPEELWNL LLRPRDLSKK IPEDRFSAAG FWNAVGSHHG
TSNVTHSYFL EGDSRRFDAN FFNINPREAA SIDPQHRLLL ETVYEALESA GLSLEAMCGT
NTGVYAGLMC ADYLDLQLRD PDTIAQYHAT GTARSILSNR VSYFFDWKGP SMTIDTACSS
SLVAVHLAVQ ALRHSECSTA IAAGANLILG PEMYIAESNL HMLSPTGTSK MWDADANGYA
RGEGIGVVVL KRLGDALRAG DPIECVIRET AVNSDGRTNG ITMPLATSQS SLIQETYRKA
GLNPLSELDR HVPSFPRPCS LNLANLSLRC QFFEAHGTGT PVGDPLEAEA IKCAFFPDQH
PACAEPPRHL LNVGSVKTVI GHTEGAAGIA GLLKASLALQ NGVVPPNLHF NRLNPKIAPF
YANLHVPTVP LSWPKVEVAR ASVNSFGFGG TNAHCVFHGV QQLLPMCGSS LATTAQHESP
LIFPLSACSQ RSLTRLVQRY AAYIAANSSV DLQNVAFTVR SRSALSAKHC FVALSRGSLI
EQLSSYTAPS HSIGQRAHAQ LARVTAGVPR VLGIFTGQGA QWPTMGRNLI LRSPVFAATI
ERLDIVLGRV PNPPDWCLRD ELLADAGSSR CSDSEFSQPL CTAVQIALVD LLHSVGVRFN
VVVGHSSGEI AAAYTAGCLS AEEAITVAYY RGYYSHRASS TTGAKLSMMA AGIGFAEALR
MCDRAEYKGK IFPAASNAPF STTTSGDEKS LHQALSELAS QERFARMLRV DKAYHTPYMR
PCALPYLNSL HQSNVQGRIG DPSCTWISSV HGFEMDISSD PVNSDYWVEN LLQPVLFSEA
LGQAIRDHGP FSLALEVGPH PALKGPTGQN LKAFGHNEIP YHGSLTRGED DTLALGQCLA
SVWATLGPSA VNLSKLASSL GGEAASRPLR IMKALPTYPW DHETIHWRES RRSKQYCSRP
APHELLGACT ERSEGQICWR NIFHVHEISW LRDHKVHGEV VFPAAGYCVM AIEAAMAFLA
QPIRLIELQQ LVIHRGVRIE DNSIGTEMIS TLSLAPTGND SRSSPDLSTA AFNFSLTAGK
ADGTEQSSIR FETKISVTLG NPHIATLPAS QRNSAEWPAA DVDRFYLSMQ EIGLEYTGVF
RSMTSCERRW KKASARIAPI PSSMIIHPGF LDTTFQTLFL GMAAPGDESL RTTYLPTKIQ
SIRVNPAILE DGSPVAMPYR IDTTITDLHC PTQESQASFT GDVDVYSDGN CVIQIEGLAC
VALGSLTKAD DRNMFHTTTW ELDILCGMSA SRVSPESEYL ALLEEYESIA RQYVEGRCVS
SSTLSSPTSP GEQLIDALHA GRNNHHTNGI ENRSHSRDYW QSGVGPQRIR KYLAQTAKQI
AHKHPRMTIM QLIHVSDDEG SAVRMILDSL EDSFASYVVT GLSEDVLRHA QACVATPDER
VRFDVFDTFQ RSLNGDSEQG FDLVIANLGQ SPESDKAHQV LNSVRQLLRP GGYVLLQAVT
GRGLFPGLIL DNLVGHSSGP MARSEATWEK TLRNLGYSGI QSMVYDSGMA HPHCHSLILS
QAMTPSLSQI LRPSIVLDPL SSEEKILIIG GETALGSRVV CELQPLLRPW KNSILILPSL
TDIASFDSHV AKHVLCLADF EAPIFRDFSP LHFDALQKLF QQPRNVFLVT RGFNQGDPYS
SMTVGLARVL RTELPSSNVV LLDVDRDDNL DTAQLATLFG QFISGIQLQS DDTRTLLKQE
LEMALENGDL YIPRIKHAKD MNDRFNSAFR QIPATHQPQL TAQLNVPFEK PVPIRVLCRS
SSALMVDDDA SYFLCLGKAR LGNLEQCVLA FTPSADDLVF LEELSLLQCN IDKDMAPKVL
PAVIGFYISA RIQKFASSGR TVIFTNEPLL ARALVSTVEE TEHISITLAT SNLSIALWHE
SIAYWHPYTA TRNIKHLLPP DINLFINLEK EPNSLCDRVL NALSSKCTIR GREHFFSAHA
RQPQSGLSRS YKEYLQFLWS QYNGHANSLP PATEIESLGA TEVCAIEQYR SETLVRRLDA
RAFFRDDATY FLVGMTGELG HSLARWMVAH GVRYLAIASR SPKPARWYQE LEEQGCQVLV
LSLDVCDRED LQRVHAQIHR AMPPIAGIVN GAMVLADGAF VNMSYEDFVR VLEPKVKGTE
NLDQLYNQPG LDFFILLSST ATLIGNSGQS NYSVANMYMQ GVARRRQHRG LAGSCVDIGM
VLGLGVVTRN VTHEKTLRKA GLLAISETDF HCIFAEAMRV GWEGVTDSPC FSTGLHVPPG
QSRPQWYDDP RFAHFHVMED LDSKSQHRTR TQLLQDRLRN PVEMAVAESW IQEAFITMLQ
KLLQLPGPIT NITQPLTQLG IDSLLSTEIK GWFYKELNFH VSVLKLLGGT SIIESKPLPI
PDPYERVLTC SLITTPTRNS EQIQEETESY ADQSEGSSSD QGTSRASQFT PASTLDFTPQ
AVDDPQSSST LSLRNLLPLS VEQEKMYFML ATVDDPTMYN CTIQYELHGN LDMERFKIAV
IHVAQRHESL RTAFVTQAAD GMPRRAILES SQIGWWERTS GDPLEASLEI SRVHSHEYDL
AKGQSMVISI LHTSLQHHIM TFGYHHLIMD GVSWQLLLRE FAAAYQDPDL LAPVISQYSA
FCDEALMRAA SRDDALERSR LLETASPLPL FPFARVSFRQ VHTCYETIQV SSQLDAGTSA
KVKAVSSRTG VTSFHFHVAA IQLLIQKVLD IDKFMIGITN ANRDNPRFEK VIGHMVEVVP
LCCEPQSSCT FTDLLQDTRA RVLAALASPS ASQKPMSAEQ MHTTECNVAV NYIAKFTQDI
RFDQSTLKYS TSQLARQPYD LVFTIRENED GTMLLNFEAQ KYLYYEKDLR ILMSLYTQLT
ETFSMGTESR LESYECIAAS GMPSLHLQQG PVLDHPWSGC LTKRIRKTIT TYPADLAIKD
DSGMRLTYET MHSRSLSIMQ ILLEAGVSFG TPVAVACGPS VDTVCTLLAI WWIGAIYMPV
DLMQGHQRLA HIIDVSRPAA IVCKGPLGQL ETSHIAPVIQ LPQVLQPTTL GHQDYADENS
PAALLHTSGS TGVPKGVLLS HRNLRCHFNA TEQAFPIGRQ VVLQHSSHSF DAGLFQILLA
LLHGGTLVIT NNLKEPGQLA ELMLREHVSV VTAVPSEYAL WIGEAGQLLS ELGSWRFAFC
VGEKLSRATI QAFVSLGLPD LTLINAYGPC ETTMACTMGV IDYERVDGDS QSVSIGEPLS
SYGIAILNSQ LKSVPQGWPG EICIAGAAVA LGYLDVKDEE GRFVELDGVR VYRTGDRGRL
REDGSLEYLG RVDGDSQLKL RGIRLELDEI SNALLQASAG ALVDAATIAK GDPDDLYLVS
FVVLSRAVEI EDNIDLFIKQ LLDTVALPPH AKPAQVSIVT RIPLTSSGKV DRKALGRLPV
GQSGSSSEQP VLEIIERKLL EMWKEYLPST GLPITRETSF FELGGNSLRL LKLQARIRRV
TGISIPITEL FQSSTLGEMA RLAGTVVTRI RASSKAIDWD SETAIPDYLD QIKPLPTQPN
GAVREVILTG ATGYYGRAIL EALVEIPSVA RIHCIAIRPA PDGSPRQELP VKSSKICLYS
GDLSDPTCGL NAVDVDKLTR TVDCVIHNGA DVSFVKPYAA LRKANVLSTK YLFSLCLARR
IPFHYISTAS VTSLSERDTF SAASVAGFPP PSFNNDGHNP LVSGYVASKW ASEVFLERAC
ARFSDLMPDV HIYRPTSITT ASSPHESLSD ASAGNTNIIG AILDVSRFLH AVPDTRDWRG
YIDLIGLNGA VESLVRNITT TRSTALPSAL NEASKENDGL PCQIRYMNVC GETRFKASEL
REFMEGSDQA AYLQLPWGVW LEKARAGEVI DAGVADFLGE WEAATAADYW RTSPSSARSP
FLLPWLE
//
