UniProt: A0A100IKN7

Database: UniProt
Entry: A0A100IKN7_ASPNG

LinkDB:  A0A100IKN7_ASPNG 
Original site:  A0A100IKN7_ASPNG

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Ontology (8)   
   GO (8)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (45)   
   InterPro (25)   
   Pfam (10)   
   PROSITE (4)   
   SMART (6)   
Literature (1)   
   PubMed (1)   
All databases (55)   

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ID   A0A100IKN7_ASPNG        Unreviewed;      2417 AA.
AC   A0A100IKN7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:GAQ42521.1};
GN   ORFNames=ABL_05182 {ECO:0000313|EMBL:GAQ42521.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ42521.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAQ42521.1}.
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DR   EMBL; BCMY01000007; GAQ42521.1; -; Genomic_DNA.
DR   PaxDb; 5061-CADANGAP00008761; -.
DR   VEuPathDB; FungiDB:An11g05940; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1111323; -.
DR   VEuPathDB; FungiDB:ATCC64974_87180; -.
DR   VEuPathDB; FungiDB:M747DRAFT_369591; -.
DR   OMA; WHESAVA; -.
DR   Proteomes; UP000068243; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion 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:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd05195; enoyl_red; 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; 3.
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; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
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; 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; 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; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 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; 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; PS00059; ADH_ZINC; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          9..434
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2330..2407
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2417 AA;  264071 MW;  0B150D18C57ACF8A CRC64;
     MPGTQDSPVM PIAIVGIGGR FPGDASNPDR LWELLLNAKS TLSETPEDRF SADAFYHPQP
     DRPGTSNSCG GHFMNQNIEE FDAPFFSITP SEARAMDPQQ RMCLEVAYEA MENAGITMDR
     ISGSRTSCYV GCFNHDYQLL QNLDLDSLPF YHATGTESSC LSNRVSWFFN LAGPSMTVDT
     ACSSSLIALH LACQSIRLGE SETALVGGVN IISFPEIYMK LSNLQMVSPD SKSQTFDEKA
     NGYGRGEGTC FVVLKPLDKA IEDNDVIRAV IRNTGSNEDG NTPGLTLPSK NMQKALIEKV
     YEEAGLQMRD TGYFEAHGTG TVAGDSIETQ ALGETIGKLR PPGQPLWVGS LKANIGHLEG
     GSGLASLIKT VYVLEKGVIP PQIWLDKLNP RIRAEEWNLA VPTEVIPWPD QGPRRASVNS
     FGFAGANAHV ILEDACSYFE ANVGRGRHNS KVPAKLAENP DLCRDKHDAN SLTLSRDTHG
     HVQPFPKLIL WSAHEQGGLK RISESWKEFL GERSGMLTQV ERAKLLSDLA YTAVKRRTQF
     PWRSFTVCSD PGEIASGEVD IAPAVRSSQR PRLALVFTGQ GAQHHAMGRR LMHYDVYANS
     MRTADQYLKS LGCPWSLVEE LSRDAESSRI NPPEFSQPLC IALQVAMVDL LKSWDIWPPE
     AVIGHSGGET AAAYAKGALT REAAWTVAYY RGQVCSMAPD VDPDHPLDGD MLAAAISEQE
     AQSYIQQVSS GKLVVACVNS PNSVTLSGDV PAIIDAAKLI KSDGHLAKKL GVNRAYHSAH
     MKVVEDMYRD LLKDVHGLPE TPDSPKMFSC VTGASIDNCD LGGNYWVTNL INQVKFSQAM
     QALINHSDSR RSKRPKGYSY VNLMLEIGPH GALQGPVKQN LKAMQVDCTS VSALDRNKDA
     AQSLLEAIGV LFQHGYDSNI IAANTPDPNE TTQLLVDLPP YPWNHSNRYW HESAVASAYR
     FKKFPRKDLL GIRDNEGNNA HARWRHFLRP SENPWIEDHQ VQGKVIYPAA GMLVMALEAA
     RETADPDKAI KAYEIRDVSI KNAIIIPKGE DEAETMVHFH RKSSGWQEFS IYSRVGHNPW
     SQNCTGVLRV QYKVNQDMGS FTNEEEKITI LYRSEYEQVQ KRCSRSMSSE NFYAEQSELD
     LRFGETFQNV SNIRLNQGEM VFDVQTPDVR SKMPQNFTHD HLVHPCTLDP VIHASLAILN
     HGEGEKGPAI PTSIGRLVIS AGISAGPGTV LKAHSSATRH GLRDAELNIR AFSEDREKPL
     IILDRIKVTR LGGGVSSEGQ DGLDTAQKRI ASEIHWEQDA LHLKSQGLRK LDLPNPAADG
     PDKMGPLESF IRLLGHKFSD LKILEIGAGD GNVTERLLDA LEGHDGESVP LLEQYTATGS
     NDEAALLKKR MHSRGPYLHA TPLALSQDWQ EQGLSSQTYH CIIINAGDGR TAAGNAIEQS
     KGLLKANGVL IVLLAKDSSE SRETWIQNLA ERGLTNIEYV ASEDHNSAAS SIPFLSSGLA
     LYLDSALPKD ILLVGPCCPG ELSRSLTEQL QSHGIRLHHA TLCDTERIDL GDKFCLFLPE
     LEHPILFDLN AKDFLLLKRL LLESKGTLWV TAGATFECSD PKASLVTGLF RSVSHEHPEL
     SLTTLDLDTE DSHSHVGASI VMDVLKRIAN GDIDHEFTAR GGQILIPRIR MNKRLNDFYS
     VLRDGPQPVL GPLKQPGRSL ALCLGAPGVF NSIHFRDDLS HQESLSPDTV EIEVKATGLN
     SHDLLSALDQ VADPTFGHEC SGIIRNVGEA VTKYRIGDRV MAWSSGAFAN FTRVPETMVQ
     PMPFGMPFPV AASLPISYCV AYHSLVECAR LQRGESVLIH MGAGGVGQAA IMIALNLGAK
     VYVTVGSEEK KFHLMDTYGV QDDHIFYSRD LSFSQGVSRL TRGSGVDVVL NSLSGEQLQH
     SRSCVASFGR FVDIRLNSTA ENTGLDMGPL PKNVASFSVN VHELHDKCLP RASKLFENAM
     RFYFENNCYP PSPLHVMAFP EIPDGLRLLH SGKQMGKIVF QANDEDQVLA IPPPIKATKL
     DADATYIIAG GFGGLGQHIA KWMVQRGART LVFLSRSGSD HLDAPRVLEE IATAGANGVA
     YKCDICDLEQ VETAMKQMAT DGLPAVRGIV QAAMALADST FEQMTPDQWE LSTKIKALGS
     WNLHLTAPAE IDFFVMLSSA SGIAGLRGQG NYAAGNTFID ALAHHRHARG LPAVSIDVGP
     VTDIGYMAQR SDITELIRSL GFVGLNGDEL LGILQTTMGS DENTRKSSDP QIILGLPTGG
     HLAAEGLDMP YTLSNARLAR LSRIGAISQD DGESGPALSE QIKKAPSRMS ATEAVTDALR
     ARLANQMMVE VEDVDASKPV SGYGVDSLTA VDIRVWCLKE AQADVSILDI VNYSSIMELA
     QTIVANSRLA SNDKWED
//

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