ID   COX5_ASPNG              Reviewed;         197 AA.
AC   O93980;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Cytochrome c oxidase polypeptide 5, mitochondrial;
DE   AltName: Full=Cytochrome c oxidase polypeptide V;
DE   Flags: Precursor;
GN   Name=cox5;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10503533; DOI=10.1007/pl00008638;
RA   Shuster J.R., Connelley M.B.;
RT   "Promoter-tagged restriction enzyme-mediated insertion (PT-REMI)
RT   mutagenesis in Aspergillus niger.";
RL   Mol. Gen. Genet. 262:27-34(1999).
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:0000250|UniProtKB:P00424}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:P00424}.
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       seevral supernumerary subunits. The complex exists as a monomer or a
CC       dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC       membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1
CC       complex, complex III, CIII). {ECO:0000250|UniProtKB:P00424}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00424}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P00424}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase IV family.
CC       {ECO:0000305}.
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DR   EMBL; AJ132229; CAA10609.1; -; Genomic_DNA.
DR   AlphaFoldDB; O93980; -.
DR   SMR; O93980; -.
DR   STRING; 5061.CADANGAP00011133; -.
DR   VEuPathDB; FungiDB:An14g04170; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1141664; -.
DR   VEuPathDB; FungiDB:ATCC64974_3600; -.
DR   VEuPathDB; FungiDB:M747DRAFT_291509; -.
DR   eggNOG; KOG4075; Eukaryota.
DR   UniPathway; UPA00705; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:InterPro.
DR   CDD; cd00922; Cyt_c_Oxidase_IV; 1.
DR   Gene3D; 1.10.442.10; -; 1.
DR   InterPro; IPR004203; Cyt_c_oxidase_su4_fam.
DR   InterPro; IPR036639; Cyt_c_oxidase_su4_sf.
DR   PANTHER; PTHR10707; PTHR10707; 1.
DR   Pfam; PF02936; COX4; 1.
DR   SUPFAM; SSF81406; SSF81406; 1.
PE   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..13
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           14..197
FT                   /note="Cytochrome c oxidase polypeptide 5, mitochondrial"
FT                   /id="PRO_0000006094"
FT   TOPO_DOM        14..129
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00424"
FT   TRANSMEM        130..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        148..197
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00424"
SQ   SEQUENCE   197 AA;  22250 MW;  ED41386462784E34 CRC64;
     MFLRSVTRAA ARSSAVPTTG LRSYRTVSGP MACLNARPQT EKKSIAPQQT RAASEHAISN
     PTLAGIEKRW EAMPPQEQAE LWMQLRDRMK VDWHQMTLQE KKAAYWISFG PHGPRSVPPK
     GENLKIFFKV AQLTLVSFGI FYVIHLFAKP QPKTMTKEWQ EASNEYAKQE KINPIYGISA
     EGYEGKGFVQ SPPAEKQ