XANB_ASPFU
ID XANB_ASPFU Reviewed; 761 AA.
AC Q4WED9;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Isocyanide synthase xanB {ECO:0000303|PubMed:29844112};
DE Short=ICS xanB {ECO:0000303|PubMed:29844112};
DE EC=1.-.-.- {ECO:0000305|PubMed:29844112};
DE AltName: Full=Xanthocillin biosynthesis cluster protein B {ECO:0000303|PubMed:29844112};
GN Name=xanB {ECO:0000303|PubMed:29844112}; ORFNames=AFUA_5G02660;
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, DISRUPTION PHENOTYPE, 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: Isocyanide synthase; part of the gene cluster that mediates
CC the biosynthesis of the isocyanide xanthocillin and its derivatives
CC (PubMed:29844112). The first step of the pathway consists in the
CC conversion of tyrosine into a vinyl-isonitrile intermediate by the
CC 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:0000269|PubMed:29844112}.
CC -!- INDUCTION: Expressed during copper starvation via the regulation of
CC both aceA and macA transcription factors.
CC {ECO:0000269|PubMed:29844112}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of xanthocillin
CC derivatives including a dimethoxyl formyl xanthocillin derivative, the
CC sulfated formyl xanthocillin derivative fumiformamide, a 1,2-
CC diformylamido derivative named melanocin E, and the imidazole-
CC containing melanocin F. {ECO:0000269|PubMed:29844112}.
CC -!- SIMILARITY: Belongs to the isocyanide synthase family. {ECO:0000305}.
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DR EMBL; AAHF01000011; EAL86038.2; -; Genomic_DNA.
DR RefSeq; XP_748076.2; XM_742983.2.
DR AlphaFoldDB; Q4WED9; -.
DR SMR; Q4WED9; -.
DR STRING; 330879.Q4WED9; -.
DR EnsemblFungi; EAL86038; EAL86038; AFUA_5G02660.
DR GeneID; 3505484; -.
DR KEGG; afm:AFUA_5G02660; -.
DR VEuPathDB; FungiDB:Afu5g02660; -.
DR eggNOG; ENOG502RNZ1; Eukaryota.
DR HOGENOM; CLU_015940_0_0_1; -.
DR InParanoid; Q4WED9; -.
DR OMA; FEHLYPC; -.
DR OrthoDB; 934123at2759; -.
DR Proteomes; UP000002530; Chromosome 5.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.60.130.10; -; 1.
DR InterPro; IPR007817; Isocyanide_synthase_DIT1.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR PANTHER; PTHR37285; PTHR37285; 1.
DR Pfam; PF05141; DIT1_PvcA; 1.
DR Pfam; PF02668; TauD; 1.
PE 2: Evidence at transcript level;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..761
FT /note="Isocyanide synthase xanB"
FT /id="PRO_0000445289"
FT REGION 24..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 85867 MW; EB889D4AA1F5D902 CRC64;
MIAVLQNPQN AAISYSGEPQ EHNLLGSYET KAPNVETSEI AASSSSSEAP EDLAEEHHRN
EASLQQPLSE VDRHEQPAAS DNTRSGLDIP PVTVSTPQSS DNPLVESKEA VPVTFKDEGK
GTKADPSHLL TEALETTNGE ENSPISEDEA TAIAVLKVIE RYGVNFEKTG ESWQGLTSFI
PTVVEQVKKR EAVRMILPAF PFKSPNARDK VLGVMPDLGE ELALYHLNGL CENIGRVYEP
GADVYISSDG LVYNDILGVP DETVWEYGEA LRRMAVEKEL HHVKFIRLFE LLEHPWIPLT
SAEQAKSYYL AHAQCLRREL MYRFEDRSFD ADAAIRSDND TCLTYRGYIK FLTKDLAPQM
DTQYTSKKAR AAHIAQIARS MIVRGKMFAA AIKANRADYV RLSIHESNGA RKLSISLVPQ
VRGVLGYTPW HSSIAVDADG TLRAVHAEDV RETHELVYKN GQPYYFREKS KLFDWVEDGL
RVKFEPLYPC GLIIRPSDID DSRPPPSISH LPMHKVRQLS TGLSPVVLRG FRETLKEELY
VQKASELGTI LPWSFGIIQK VRDAGRTDKL GNNVTSNEAM PMHYDGMFKF EEETDPVTGE
VKRVQKPPGY QFFTCPATAP KGSGYTLFAS SRLFFRYLPL PWTTERLQKV TWGMDNDGFW
DAKLKNLPLV VPHPVTGLPC MRWHQPWDST KTKFSTCAVT IENDEQELAS VVDDLTYDYR
VCLRFSWEQG DLLVSDNTAM LHTRTGYKTN CERELWRIHF D