AOX_CRYNH
ID AOX_CRYNH Reviewed; 401 AA.
AC Q8NKE2; J9VI64;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Alternative oxidase, mitochondrial;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=AOX1; ORFNames=CNAG_00162;
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=14500501; DOI=10.1128/iai.71.10.5794-5802.2003;
RA Akhter S., McDade H.C., Gorlach J.M., Heinrich G., Cox G.M., Perfect J.R.;
RT "Role of alternative oxidase gene in pathogenesis of Cryptococcus
RT neoformans.";
RL Infect. Immun. 71:5794-5802(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
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}.
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DR EMBL; AF502293; AAM22475.1; -; Genomic_DNA.
DR EMBL; CP003820; AFR92299.1; -; Genomic_DNA.
DR RefSeq; XP_012046575.1; XM_012191185.1.
DR AlphaFoldDB; Q8NKE2; -.
DR SMR; Q8NKE2; -.
DR EnsemblFungi; AFR92299; AFR92299; CNAG_00162.
DR GeneID; 23884025; -.
DR VEuPathDB; FungiDB:CNAG_00162; -.
DR HOGENOM; CLU_041974_1_0_1; -.
DR PHI-base; PHI:275; -.
DR Proteomes; UP000010091; Chromosome 1.
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 ?..401
FT /note="Alternative oxidase, mitochondrial"
FT /id="PRO_0000001719"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 53..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 191
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 191
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 230
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 230
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 230
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 233
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 233
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 281
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 282
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 335
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 335
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 335
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 338
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 338
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT CONFLICT 80
FT /note="G -> E (in Ref. 1; AAM22475)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="F -> L (in Ref. 1; AAM22475)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 44440 MW; 40CA3CF5A0468032 CRC64;
MSAIMLRSGN VARSTILAGG PLIGGPMTFR SAVSSTRTFS LFTKARIQSD DMKRASLSLQ
PSVREAEKSQ GPVVGSEGRG VEGPHYQDQV SHNVLSDAST TGAWTMFNPI YTEKELNTVQ
VVGRAPVTFG DKAAHRTVKF LRKCFDLLTG YTPYEVPASV LAQKPIPIAE LRSKGKLLSD
QKWLFRIILL ESIAGVPGMV GGTLRHLRSM RLLKRDGGWI HSLLEEAENE RMHLLTFMTI
AQPGIFTRAL VLAAQGVFYN AFFLTYLISP RIAHRFVGAL EEEAVRTYTH CISDMEAGLI
PEWKDMPAPA IAIDYWRLPA SSSLLDVIRA VRADEATHRF VNHSLANLDQ KRDFNPFALS
EASPEERGSK WGYTREESAK FALEQQRKLM AASEKSSGLV E
