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Database: UniProt
Entry: A8PW15_MALGO
LinkDB: A8PW15_MALGO
Original site: A8PW15_MALGO 
ID   A8PW15_MALGO            Unreviewed;       106 AA.
AC   A8PW15;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   03-MAY-2023, entry version 66.
DE   RecName: Full=Cytochrome c oxidase subunit 6, mitochondrial {ECO:0000256|RuleBase:RU368103};
DE   AltName: Full=Cytochrome c oxidase polypeptide VI {ECO:0000256|RuleBase:RU368103};
GN   ORFNames=MGL_1005 {ECO:0000313|EMBL:EDP44523.1};
OS   Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP44523.1, ECO:0000313|Proteomes:UP000008837};
RN   [1] {ECO:0000313|EMBL:EDP44523.1, ECO:0000313|Proteomes:UP000008837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX   PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA   Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA   Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA   Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA   Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT   "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT   virulence traits shared with plant and human fungal pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
CC   -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC       mitochondrial electron transport chain which drives oxidative
CC       phosphorylation. The respiratory chain contains 3 multisubunit
CC       complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC       cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC       CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC       transfer electrons derived from NADH and succinate to molecular oxygen,
CC       creating an electrochemical gradient over the inner membrane that
CC       drives transmembrane transport and the ATP synthase. Cytochrome c
CC       oxidase is the component of the respiratory chain that catalyzes the
CC       reduction of oxygen to water. Electrons originating from reduced
CC       cytochrome c in the intermembrane space (IMS) are transferred via the
CC       dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC       to the active site in subunit 1, a binuclear center (BNC) formed by
CC       heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC       water molecules using 4 electrons from cytochrome c in the IMS and 4
CC       protons from the mitochondrial matrix. {ECO:0000256|RuleBase:RU368103}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU368103}.
CC   -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC       multisubunit enzyme composed of a catalytic core of 3 subunits and
CC       several supernumerary subunits. {ECO:0000256|RuleBase:RU368103}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004443, ECO:0000256|RuleBase:RU368103};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004443,
CC       ECO:0000256|RuleBase:RU368103}; Matrix side
CC       {ECO:0000256|ARBA:ARBA00004443, ECO:0000256|RuleBase:RU368103}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 5A family.
CC       {ECO:0000256|ARBA:ARBA00007972, ECO:0000256|RuleBase:RU368103}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDP44523.1}.
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DR   EMBL; AAYY01000003; EDP44523.1; -; Genomic_DNA.
DR   RefSeq; XP_001731737.1; XM_001731685.1.
DR   AlphaFoldDB; A8PW15; -.
DR   STRING; 425265.A8PW15; -.
DR   GeneID; 5856042; -.
DR   KEGG; mgl:MGL_1005; -.
DR   VEuPathDB; FungiDB:MGL_1005; -.
DR   InParanoid; A8PW15; -.
DR   OMA; ENKNQYQ; -.
DR   OrthoDB; 2876967at2759; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000008837; Unassembled WGS sequence.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:UniProtKB-UniRule.
DR   CDD; cd00923; Cyt_c_Oxidase_Va; 1.
DR   Gene3D; 1.25.40.40; Cytochrome c oxidase, subunit Va/VI; 1.
DR   InterPro; IPR003204; Cyt_c_oxidase_su5A/6.
DR   InterPro; IPR036545; Cyt_c_oxidase_su5A/6_sf.
DR   PANTHER; PTHR14200; CYTOCHROME C OXIDASE POLYPEPTIDE; 1.
DR   PANTHER; PTHR14200:SF11; CYTOCHROME C OXIDASE POLYPEPTIDE VA; 1.
DR   Pfam; PF02284; COX5A; 1.
DR   SUPFAM; SSF48479; Cytochrome c oxidase subunit E; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU368103};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU368103};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368103};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU368103};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|RuleBase:RU368103};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW   ECO:0000256|RuleBase:RU368103};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008837};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW   ECO:0000256|RuleBase:RU368103}.
SQ   SEQUENCE   106 AA;  12380 MW;  529D3C7C9B7E0F32 CRC64;
     MYSAHNETFE EFNDRFVKFF EGVEDQFEAQ RGLNNAFAHD LVPSPEVIES ALKAARRVND
     FSLAVRIFEG LKFKTENDNQ YKQYLEVLKP LREELGVPLK EEIYSS
//
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