(data stored in SCRATCH zone)

SWISSPROT: A2Q7B6_ASPNC

ID   A2Q7B6_ASPNC            Unreviewed;      1862 AA.
AC   A2Q7B6;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 103.
DE   SubName: Full=Aspergillus niger contig An01c0020, genomic contig {ECO:0000313|EMBL:CAK36857.1};
GN   ORFNames=An01g00060 {ECO:0000313|EMBL:CAK36857.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK36857.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {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: Belongs to the thiolase-like superfamily. Fungal fatty acid
CC       synthetase subunit alpha family. {ECO:0000256|PIRNR:PIRNR000454}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM269949; CAK36857.1; -; Genomic_DNA.
DR   RefSeq; XP_001388458.1; XM_001388421.2.
DR   PaxDb; A2Q7B6; -.
DR   EnsemblFungi; CAK36857; CAK36857; An01g00060.
DR   GeneID; 4978430; -.
DR   KEGG; ang:ANI_1_6014; -.
DR   HOGENOM; HOG000177974; -.
DR   KO; K00667; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR   GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.47.10; -; 3.
DR   Gene3D; 3.90.470.20; -; 1.
DR   HAMAP; MF_00101; AcpS; 1.
DR   InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR   InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR   InterPro; IPR002582; ACPS.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR040899; Fas_alpha_ACP.
DR   InterPro; IPR026025; FAS_alpha_yeast.
DR   InterPro; IPR041550; FASI_helical.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR   InterPro; IPR002347; SDR_fam.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF01648; ACPS; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   Pfam; PF18325; Fas_alpha_ACP; 1.
DR   Pfam; PF18314; FAS_I_H; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   PIRSF; PIRSF000454; FAS_yeast_alpha; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
DR   SUPFAM; SSF56214; SSF56214; 1.
DR   TIGRFAMs; TIGR00556; pantethn_trn; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   3: Inferred from homology;
DR   PRODOM; A2Q7B6.
DR   SWISS-2DPAGE; A2Q7B6.
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000454-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000454-3};
KW   Phosphopantetheine {ECO:0000256|PIRNR:PIRNR000454,
KW   ECO:0000256|PIRSR:PIRSR000454-4, ECO:0000256|PROSITE-ProRule:PRU00258};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000454, ECO:0000256|SAAS:SAAS01225069}.
FT   DOMAIN          144..219
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          584..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1280
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000454-1"
FT   METAL           1748
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT   METAL           1749
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT   METAL           1750
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT   METAL           1848
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT   METAL           1849
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT   MOD_RES         179
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000454-4,
FT                   ECO:0000256|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   1862 AA;  204608 MW;  97F2591D5C65A542 CRC64;
     MRPEIEQELA HTLLVELLAY QFASPVRWIE TQDVILAEKR TERIVEIGPA DTLGGMARRT
     LASKYEAYDA ATSVQRQILC YNKDAKEIYY DVDPVEEEEA QPSAEAAASA PAAAPAGAPA
     VAAAPAAAPP PSAGPAAAIE DAPVTAVDVL RTLVAQKLKK SLSDVPLSKA IKDLVGGKST
     LQNEILGDLG KEFGSTPEKP EDTPLDELGA SMQATFNGQL GKQSSSLIAR LVSSKMPGGF
     NITAVRKYLE TRWGLGSGRQ DGVLLLALTM EPPSRIGSEA EAKSYLDDVA NKYAASAGIS
     LSAPAAGGDS GAGGGGMLMD PAAIDALTKD QRALFKQQLE IIARYLKMDL RAGQKAYITS
     QESQKTLQAQ LDLWQAEHGD FYASGIEPAF DALKARVYDS SWNWARQDAL SMYYDIIFGR
     LKVVDREIVS QCIRIMNRSN PLLLEFMQYH IDNCPTDRGE TYQLAKELGE QLIENCKEVL
     GVAPVYKDVA VPTGPQTTVD ARGNIGYKEV PRASARKLEH YVKQMAEGGP ISEYSNRTKV
     QNDLRSVYKL IRRQHRLSKS SQLQFNALYK EVIRALSMNE NQIMPQENGS GKKTGRNGVK
     RNGSPRAGKV ETIPFLHLKK KSEHGWDYNK KLTGIYLDVL ESAARSGLTF QGKNVLMTGA
     GAGSIGAEVL QGLISGGAKV VVTTSRYSRE VTEYYQAMYA RYGGRGSQLV VVPFNQGSKQ
     DVEALVDYIY DSKKGLGWDL DFVVPFAAIP ENGREIDSID SKSELAHRIM LTNLLRLLGC
     IKTQKQSNGF ETRPAQVILP LSPNHGTFGN DGLYSESKLA LETLFNRWYS ENWNNYLTIC
     GAVIGWTRGT GLMSGNNMVA EGVEKLGVRT FSQQEMAFNL LGLMAPAIVN LCQLDPVWAD
     LNGGLQFIPD LKDLMTKLRT EIMETSDVRQ AVIKETAIEN KVVNGEDSEV LYKRVIAEPR
     ANIKFQFPNL PNWEEDVKPL NDNLKGMVNL DKVVVVTGFS EVGPWGNSRT RWEMEAYGKF
     SLEGCVEMAW IMGLIKHHNG PLKGKAYSGW VDAKSGEPVD DKDVKPKYEK FILEHSGIRL
     IEPELFKGYD PKKKQLLQEI VIQEDLDPFE ASKETAEEFK REHGEKVEIF ELPESGEYTV
     RLKKGATLLI PKALQFDRLV AGQIPTGWDA KRYGIPDDII EQVDPVTLFV LVCTAESLLS
     AGITDPYEFY KYVHLSEVGN CIGSGIGGTH ALRGMYKDRY LDKPLQKDIL QESFINTMSA
     WVNMLLLSST GPIKTPVGAC ATAVESVDIG YETIVEGKAR VCFVGGFDDF QEEGSYEFAN
     MKATSNAEDE FAHGRTPQEM SRPTTTTRAG FMESQGCGMQ LIMSAQLALD MGVPIYGIIA
     LTTTATDKIG RSVPAPGQGV LTTARENPGK FPSPLLDIKY RRRQLDLRKK QIKEWQESEL
     LYLQEEAEAM KAQASDDSFD VSGYLQERAQ HIEREAIRQE KDAQYSLGNN FWKQDSRIAP
     LRGALATWGL TVDDIGVASF HGTSTVANDK NESDVICQQM KHLGRKKGNA LLGIFQKYLT
     GHPKGAAGAW MFNGCLQVLE SGLVPGNRNA DNVDKVMEKF DYIVYPSRSI QTDGINAFSV
     TSFGFGQKGA QVIGIHPKYL YATLDRAQYQ TYKAKVEARQ KKAYRFFHNG LINNSIFVAK
     DKAPYEDAQQ SKVFLNPDYR VAADKKTSQL KFPAQPPKAN DKGLESTKTM IESLAKANAS
     EDSKVGVDVE NIESFNIENE TFIERNFTAS EQEYCQKAAS PRSSFAGRWS AKEAVFKALG
     VSSKGAGAPL KDIEISSDST GAPVVNLHGA AAEAAKQAGV KQVSVSISHS DTQAVAVAVS
     KF
//

If you have problems or comments...

PBIL Back to PBIL home page