A1131_ARTBC
ID A1131_ARTBC Reviewed; 499 AA.
AC D4AY62;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Cytochrome P450 ARB_01131 {ECO:0000305};
DE EC=1.14.14.- {ECO:0000250|UniProtKB:P16141};
DE Flags: Precursor;
GN ORFNames=ARB_01131;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
CC -!- FUNCTION: Together with an NADPH cytochrome P450 the enzyme system
CC catalyzes the terminal hydroxylation as the first step in the
CC assimilation of alkanes and fatty acids.
CC {ECO:0000250|UniProtKB:P16141}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; ABSU01000018; EFE31878.1; -; Genomic_DNA.
DR RefSeq; XP_003012518.1; XM_003012472.1.
DR AlphaFoldDB; D4AY62; -.
DR SMR; D4AY62; -.
DR STRING; 63400.XP_003012518.1; -.
DR EnsemblFungi; EFE31878; EFE31878; ARB_01131.
DR GeneID; 9526589; -.
DR KEGG; abe:ARB_01131; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_27_0_1; -.
DR OMA; VNNCVLD; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
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:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..499
FT /note="Cytochrome P450 ARB_01131"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434501"
FT BINDING 437
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 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 499 AA; 56092 MW; 64D7D61C150E87FE CRC64;
MLSLIVACLV LPLICYKLVR SYNQSREDEQ FAASKGCQPP RKWSAKWPLG LDMLVKAVRY
EKRQQILQLF LEEVAASGST FEQNLLFARG IDTVEPRNIE AILSTQFTGS GIFTQDGPQW
KHSRELLRPQ FMTNRFRNFE QIRHAVNNLI SSVPDSGVVD LQPLFFRLTF ETTLFLLFGH
YLPSLKSEGI TGHESQFANA FNLGQDYLAQ RGRLGDLYWL LGGREFKDAC KVCHDFIDNA
VQKALKHSSR EKKVSDEEKE TYVFIDALVQ ETREPSVLRD QCLNILLAGR DTTACCLTWT
LRLLVQHPDV LSKLRDEVRD TIGMGPDAPD PTISQVKKLS YLSLVIKEVL RLYPSVPVNS
RAAVKTTTLP TGGGPDGSAP LLVRRGEAVG YCVYAMHRRK DIYGPDADCF RPERWENDAL
KDVGYGYLPF NGGPRICLGQ EFALLEVGYT VVRLLQTFET IEEAETKVPG APLGEEKQTL
TLVVSSGEGC WVSMKKGTK