XANA_ASPFU
ID XANA_ASPFU Reviewed; 236 AA.
AC Q4WEE0;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Isonitrile hydratase-like protein xanA {ECO:0000303|PubMed:29844112};
DE EC=4.2.1.- {ECO:0000305|PubMed:29844112};
DE AltName: Full=Xanthocillin biosynthesis cluster protein A {ECO:0000303|PubMed:29844112};
GN Name=xanA {ECO:0000303|PubMed:29844112}; ORFNames=AFUA_5G02670;
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, INDUCTION, 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: Isonitrile hydratase-like protein; part of the gene cluster
CC that mediates the biosynthesis of the isocyanide xanthocillin and its
CC derivatives (PubMed:29844112). The first step of the pathway consists
CC in the conversion of tyrosine into a vinyl-isonitrile intermediate by
CC the isocyanide synthase xanB (PubMed:29844112). Subsequent oxidative
CC dimerization of this intermediate to form xanthocillin may involve the
CC cytochrome P450 monooxygenase xanG, whose expression is coregulated
CC with that of XanB (PubMed:29844112). Xanthocillin can be further
CC modified by the isonitrile hydratase-like protein xanA which introduces
CC N-formyl groups and the methyltransferase xanE which introduces methyl
CC groups, leading to the production of several derivatives including
CC fumiformamide (PubMed:29844112). Finally, fumiformamide can be subject
CC to both oxidative and reductive cyclization to yield melanocins E and
CC F, 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}.
CC -!- INDUCTION: Expressed during copper starvation via the regulation of
CC both aceA and macA transcription factors.
CC {ECO:0000269|PubMed:29844112}.
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DR EMBL; AAHF01000011; EAL86037.1; -; Genomic_DNA.
DR RefSeq; XP_748075.1; XM_742982.1.
DR AlphaFoldDB; Q4WEE0; -.
DR SMR; Q4WEE0; -.
DR STRING; 746128.CADAFUBP00005012; -.
DR EnsemblFungi; EAL86037; EAL86037; AFUA_5G02670.
DR GeneID; 3505405; -.
DR KEGG; afm:AFUA_5G02670; -.
DR VEuPathDB; FungiDB:Afu5g02670; -.
DR eggNOG; ENOG502S8W8; Eukaryota.
DR HOGENOM; CLU_000445_44_1_1; -.
DR InParanoid; Q4WEE0; -.
DR OMA; RVMEYDW; -.
DR OrthoDB; 1165707at2759; -.
DR Proteomes; UP000002530; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002818; DJ-1/PfpI.
DR Pfam; PF01965; DJ-1_PfpI; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
PE 2: Evidence at transcript level;
KW Lyase; Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..236
FT /note="Isonitrile hydratase-like protein xanA"
FT /id="PRO_0000445293"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 131
FT /evidence="ECO:0000250|UniProtKB:Q8G9F9"
SQ SEQUENCE 236 AA; 25661 MW; 2FB78926149D666C CRC64;
MSSTPPKKYY KVAVLLFEGV DILDFTAPME VFTHTSHNRN PDNPDRVFQI NTIARSRTVN
AKKALTVQTD LLLEDAMQGL ADFDIMVVPG GPPSLLNALV ASNPREVELI RSFATLPPKT
PDEPRVLFSI CTGAFLVGAA GLLTGVSVTT HHRAIEKLRE FCIRVNGEGA SPPEVSHKRY
IDAGVLKVGS ARLLTAAGVS SCLDASLYLV SQLTSLDMSA FISRVMEYDW KGQLSE
