COX6B_DICDI
ID COX6B_DICDI Reviewed; 78 AA.
AC Q54P95;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Probable cytochrome c oxidase subunit 6B;
GN ORFNames=DDB_G0284693;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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:Q01519}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:Q01519}.
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. 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:Q01519}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q01519}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q01519}; Intermembrane side
CC {ECO:0000250|UniProtKB:Q01519}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6B family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000070; EAL65116.1; -; Genomic_DNA.
DR RefSeq; XP_638480.1; XM_633388.1.
DR AlphaFoldDB; Q54P95; -.
DR SMR; Q54P95; -.
DR STRING; 44689.DDB0186146; -.
DR PaxDb; Q54P95; -.
DR EnsemblProtists; EAL65116; EAL65116; DDB_G0284693.
DR GeneID; 8624731; -.
DR KEGG; ddi:DDB_G0284693; -.
DR dictyBase; DDB_G0284693; -.
DR eggNOG; KOG3057; Eukaryota.
DR HOGENOM; CLU_133964_2_0_1; -.
DR InParanoid; Q54P95; -.
DR OMA; VQRWNQQ; -.
DR PhylomeDB; Q54P95; -.
DR UniPathway; UPA00705; -.
DR PRO; PR:Q54P95; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0045277; C:respiratory chain complex IV; IEA:InterPro.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR CDD; cd00926; Cyt_c_Oxidase_VIb; 1.
DR Gene3D; 1.10.10.140; -; 1.
DR InterPro; IPR003213; Cyt_c_oxidase_su6B.
DR InterPro; IPR036549; Cyt_c_oxidase_su6B_sf.
DR PANTHER; PTHR11387; PTHR11387; 1.
DR Pfam; PF02297; COX6B; 1.
DR PIRSF; PIRSF000278; Cyt_c_oxidase_6B; 1.
DR SUPFAM; SSF47694; SSF47694; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome.
FT CHAIN 1..78
FT /note="Probable cytochrome c oxidase subunit 6B"
FT /id="PRO_0000369433"
FT DOMAIN 21..64
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 24..34
FT /note="Cx9C motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 45..56
FT /note="Cx10C motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 24..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 34..45
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ SEQUENCE 78 AA; 9115 MW; CB4B3302A9FB2EA3 CRC64;
MEGEQLQTAP YNPRFPQQNQ TKHCWANYVD YYGCVKHYNG DNSKCQTFFN SMNSLCPAAW
ISEWDEQKAA DLFPSDRV
