ID   XANG_ASPFU              Reviewed;         538 AA.
AC   Q4WED5;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Cytochrome P450 monooxygenase xanG {ECO:0000303|PubMed:29844112};
DE            EC=1.14.-.- {ECO:0000305|PubMed:29844112};
DE   AltName: Full=Xanthocillin biosynthesis cluster protein G {ECO:0000303|PubMed:29844112};
GN   Name=xanG {ECO:0000303|PubMed:29844112}; ORFNames=AFUA_5G02620;
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.
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: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:29844112}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AAHF01000011; EAL86042.1; -; Genomic_DNA.
DR   RefSeq; XP_748080.1; XM_742987.1.
DR   AlphaFoldDB; Q4WED5; -.
DR   SMR; Q4WED5; -.
DR   STRING; 746128.CADAFUBP00005006; -.
DR   EnsemblFungi; EAL86042; EAL86042; AFUA_5G02620.
DR   GeneID; 3505488; -.
DR   KEGG; afm:AFUA_5G02620; -.
DR   VEuPathDB; FungiDB:Afu5g02620; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_031576_0_0_1; -.
DR   InParanoid; Q4WED5; -.
DR   OMA; SEIDMSH; -.
DR   OrthoDB; 1247045at2759; -.
DR   Proteomes; UP000002530; Chromosome 5.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Iron; Membrane; Metal-binding; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..538
FT                   /note="Cytochrome P450 monooxygenase xanG"
FT                   /id="PRO_0000445298"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         489
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P04798"
FT   CARBOHYD        378
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   538 AA;  61951 MW;  6366D5E5E7A4AB17 CRC64;
     MTWMRVMPRC QNRTYKRPRG PPLSIHPLEF FQAKKVEKTA KAKMILYYLA SIPLAIICYL
     AWYLHVPWDL PSLPRIPFYV SILGLWSSMG QDEIYERWLR KPLEAHGAVL IWFAGRWSIL
     VTRPDLLTDM FRNEDLYAKA GSQKKIPWSV IATLVGDNII NSHGDTWKLY TGIMKPGLQK
     KNFDTAPLLL KSRRFVDEIL AEQNSAGRGT GILVNTFVQQ WAVDVMGMSF LDLDLQSLEK
     PHGTVRLEAI QSVIKLMLFR PLFFNFPDLD QFAWLIKSRQ RAYEIMHEFG DTLMATVLGR
     IDSDREKGIK PAEEMVVHML VDAYRDGRLT EKQFKDNLKI VFLTAHENAQ QLVNSMFWEI
     GKNNEVQTRL RAEILSTNTT TPTSEVVNAL PYLTAVVYEL LRLYPPVSQL INRVTVRPAM
     LGNEIPIPAG TFVGWNAYGV HVNPAIWGPD ANEFKPERWG RTVGEMHARF RRETVRGTYI
     PFNAHSRKCL GQGFVLLQMK ILLFEVLRRI EWTVDPGYRL KMTPVSYFLE SGRKSTDA