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XAND_ASPFU
ID   XAND_ASPFU              Reviewed;         156 AA.
AC   A4DA06;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Xanthocillin biosynthesis cluster protein D {ECO:0000303|PubMed:29844112};
GN   Name=xanD {ECO:0000303|PubMed:29844112}; ORFNames=AFUA_5G02650;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=29844112; DOI=10.1128/mbio.00785-18;
RA   Lim F.Y., Won T.H., Raffa N., Baccile J.A., Wisecaver J., Rokas A.,
RA   Schroeder F.C., Keller N.P.;
RT   "Fungal isocyanide synthases and xanthocillin biosynthesis in Aspergillus
RT   fumigatus.";
RL   MBio 9:0-0(2018).
CC   -!- FUNCTION: Part of the gene cluster that mediates the biosynthesis of
CC       the isocyanide xanthocillin and its derivatives (PubMed:29844112). The
CC       first step of the pathway consists in the conversion of tyrosine into a
CC       vinyl-isonitrile intermediate by the isocyanide synthase xanB
CC       (PubMed:29844112). Subsequent oxidative dimerization of this
CC       intermediate to form xanthocillin may involve the cytochrome P450
CC       monooxygenase xanG, whose expression is coregulated with that of XanB
CC       (PubMed:29844112). Xanthocillin can be further modified by the
CC       isonitrile hydratase-like protein xanA which introduces N-formyl groups
CC       and the methyltransferase xanE which introduces methyl groups, leading
CC       to the production of several derivatives including fumiformamide
CC       (PubMed:29844112). Finally, fumiformamide can be subject to both
CC       oxidative and reductive cyclization to yield melanocins E and F,
CC       respectively (PubMed:29844112). {ECO:0000269|PubMed:29844112}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:29844112}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
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DR   EMBL; AAHF01000011; EBA27256.1; -; Genomic_DNA.
DR   RefSeq; XP_001481489.1; XM_001481439.1.
DR   AlphaFoldDB; A4DA06; -.
DR   EnsemblFungi; EBA27256; EBA27256; AFUA_5G02650.
DR   GeneID; 5077151; -.
DR   KEGG; afm:AFUA_5G02650; -.
DR   eggNOG; ENOG502S3VC; Eukaryota.
DR   HOGENOM; CLU_094297_2_1_1; -.
DR   InParanoid; A4DA06; -.
DR   OMA; ICYQALP; -.
DR   OrthoDB; 1173611at2759; -.
DR   Proteomes; UP000002530; Chromosome 5.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR025423; DUF4149.
DR   Pfam; PF13664; DUF4149; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..156
FT                   /note="Xanthocillin biosynthesis cluster protein D"
FT                   /id="PRO_0000445294"
FT   TRANSMEM        131..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   156 AA;  17170 MW;  B7C89E1E33E74013 CRC64;
     MQAILETVSN LLPYHLLSYG ALLGTELFQS FVNTKICYQA LPMKEFLALQ KRVFPAYFRC
     QVGLVVLTAV TRPPYSILSF SQHIWDSVPL IAVGVTGALN CAMNEDNSST TDPAKIQQAN
     KTFSRNHAMS IHLNAIALVA TVWYGFTLSS SLLNGL
 
 
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