位置:首页 > 蛋白库 > AOX_BLUGR
AOX_BLUGR
ID   AOX_BLUGR               Reviewed;         358 AA.
AC   Q8X1N9;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Alternative oxidase, mitochondrial;
DE            EC=1.-.-.-;
DE   Flags: Precursor;
OS   Blumeria graminis (Powdery mildew) (Oidium monilioides).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Blumeria.
OX   NCBI_TaxID=34373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Zhang Z., Gurr S.J.;
RT   "Isolation and characterization of an alternative oxidase gene from
RT   Blumeria graminis.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes cyanide-resistant oxygen consumption. May increase
CC       respiration when the cytochrome respiratory pathway is restricted, or
CC       in response to low temperatures (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000250|UniProtKB:Q26710};
CC       Note=Binds 2 iron ions per subunit. {ECO:0000250|UniProtKB:Q26710};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF327336; AAL56983.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8X1N9; -.
DR   SMR; Q8X1N9; -.
DR   PRIDE; Q8X1N9; -.
DR   EnsemblFungi; BLGH_03428-mRNA-1; BLGH_03428-mRNA-1; BLGH_03428.
DR   VEuPathDB; FungiDB:BGT96224V316_LOCUS5787; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009916; F:alternative oxidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01053; AOX; 1.
DR   Gene3D; 1.20.1260.140; -; 1.
DR   InterPro; IPR002680; AOX.
DR   InterPro; IPR038659; AOX_sf.
DR   PANTHER; PTHR31803; PTHR31803; 1.
DR   Pfam; PF01786; AOX; 1.
DR   PIRSF; PIRSF005229; AOX; 1.
PE   3: Inferred from homology;
KW   Electron transport; Iron; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Respiratory chain;
KW   Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..358
FT                   /note="Alternative oxidase, mitochondrial"
FT                   /id="PRO_0000001715"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         159
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         159
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255"
FT   BINDING         198
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         198
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         198
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255"
FT   BINDING         201
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         201
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255"
FT   BINDING         249
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         250
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255"
FT   BINDING         306
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         306
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         306
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255"
FT   BINDING         309
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q26710"
FT   BINDING         309
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   358 AA;  41848 MW;  40242E3D0A36A4BF CRC64;
     MYLSRLPPRS IPCRSINQIS RVVARSSKSR LEFVGSYQNS LTTNQTRCLR PFSSTSRSQL
     RDYFPEADHE HIKKTEAAWP HPNYPKEQML TNISYAHRTP KDFSDRIALY LVRFLRFSTD
     LATGYKHDPV TITENGEKVL KKPYRMSERK WLIRMVFLES VAGVPGMVAG MLRHLHSLRR
     LKRDNGWIET LLEEAYNERM HLLTFLKMAK PGWFMKFMII GAQGVFFNSM FLSYLISPRT
     CHRFVAYLEE EAVLTYSTAI QDIEAGLLPK WTSPEFRIPD LAVQYWKIPE GNRTMRDLLL
     YIRADEAKHR EVNHTLGNLD QNEDPNPFVS EYRDKAAPHP SKGIEHIRPT GWERNEII
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024