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Database: UniProt
Entry: M7XCZ0_RHOT1
LinkDB: M7XCZ0_RHOT1
Original site: M7XCZ0_RHOT1 
ID   M7XCZ0_RHOT1            Unreviewed;       358 AA.
AC   M7XCZ0;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Long-chain fatty alcohol oxidase, FAO1 {ECO:0000313|EMBL:EMS21654.1};
GN   ORFNames=RHTO_01714 {ECO:0000313|EMBL:EMS21654.1};
OS   Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS21654.1, ECO:0000313|Proteomes:UP000016926};
RN   [1] {ECO:0000313|EMBL:EMS21654.1, ECO:0000313|Proteomes:UP000016926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NP11 {ECO:0000313|EMBL:EMS21654.1,
RC   ECO:0000313|Proteomes:UP000016926};
RX   PubMed=23047670; DOI=10.1038/ncomms2112;
RA   Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA   Ye M., Zou H., Zou H., Zhao Z.K.;
RT   "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL   Nat. Commun. 3:1112-1112(2012).
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000256|RuleBase:RU003682}.
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DR   EMBL; KB722655; EMS21654.1; -; Genomic_DNA.
DR   RefSeq; XP_016272773.1; XM_016415395.1.
DR   AlphaFoldDB; M7XCZ0; -.
DR   GeneID; 27365727; -.
DR   eggNOG; KOG0143; Eukaryota.
DR   HOGENOM; CLU_010119_6_2_1; -.
DR   OrthoDB; 1332763at2759; -.
DR   Proteomes; UP000016926; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR   InterPro; IPR026992; DIOX_N.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR47990:SF27; FE2OG DIOXYGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|RuleBase:RU003682};
KW   Metal-binding {ECO:0000256|RuleBase:RU003682};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003682}.
FT   DOMAIN          169..289
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          74..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   358 AA;  40062 MW;  16A99D7FFA5D7474 CRC64;
     MPSIAQAPLS VPRINLRDFS ARREEIKEQL MSAASEIGFF TLVGHEISLE EVNKAFGLAE
     RFFDLPTEVK QKYPWSPRNQ GYESNQQIRP STGYPDPKES YQVGFQRTEE QEALWPTEED
     CPGFRRETEE FMRKVQGLSV KVMELFAEGL GLPANTFTEG TVAPEGTDKA DSMSTLRLLK
     YHDCEGKDFG EGYMRAGAHA DFDVMTFLFQ RKGQSGLELC PGRKISTEFG YGDTWVPVDV
     EEGAIVINVG DQLMRWSDDR LKSTFHRVRC PRPGEYQGAR YSIGFFNQAR RDTVIQGPAK
     AYPKITGGEF IAQAMKRNFE AAQAKAKAKA YEISQETIEA NKGFEVSGTG LAPVKAAA
//
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