ID A0A0S0IGF3_ACAPO Unreviewed; 329 AA.
AC A0A0S0IGF3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 22-APR-2020, entry version 11.
DE RecName: Full=Cytochrome c oxidase subunit 3 {ECO:0000256|RuleBase:RU003375};
GN Name=cox3 {ECO:0000313|EMBL:ALG41015.1};
OS Acanthamoeba polyphaga (Amoeba).
OG Mitochondrion {ECO:0000313|EMBL:ALG41015.1}.
OC Eukaryota; Amoebozoa; Discosea; Longamoebia; Centramoebida;
OC Acanthamoebidae; Acanthamoeba.
OX NCBI_TaxID=5757 {ECO:0000313|EMBL:ALG41015.1};
RN [1] {ECO:0000313|EMBL:ALG41015.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Linc Ap-1 {ECO:0000313|EMBL:ALG41015.1};
RX PubMed=31221647;
RA Karlyshev A.V.;
RT "Remarkable Features of Mitochondrial DNA of Acanthamoeba polyphaga Linc
RT Ap-1, Revealed by Whole-Genome Sequencing.";
RL Microbiol Resour Announc 8:e00430-19(2019).
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:RU003375}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c]
CC + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-
CC COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034;
CC Evidence={ECO:0000256|SAAS:SAAS01246601};
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC {ECO:0000256|RuleBase:RU003375, ECO:0000256|SAAS:SAAS00709834}.
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DR EMBL; KP054475; ALG41015.1; -; Genomic_DNA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro.
DR CDD; cd01665; Cyt_c_Oxidase_III; 1.
DR Gene3D; 1.20.120.80; -; 1.
DR InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3.
DR InterPro; IPR033945; Cyt_c_oxase_su3_dom.
DR InterPro; IPR000298; Cyt_c_oxidase-like_su3.
DR InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf.
DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx.
DR PANTHER; PTHR11403; PTHR11403; 1.
DR Pfam; PF00510; COX3; 2.
DR SUPFAM; SSF81452; SSF81452; 1.
DR PROSITE; PS50253; COX3; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAAS:SAAS00709742, ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|RuleBase:RU003375, ECO:0000313|EMBL:ALG41015.1};
KW Oxidoreductase {ECO:0000256|SAAS:SAAS01246713};
KW Transmembrane {ECO:0000256|RuleBase:RU003375,
KW ECO:0000256|SAAS:SAAS00709762, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAAS:SAAS00709799,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 54..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..322
FT /note="COX3"
FT /evidence="ECO:0000259|PROSITE:PS50253"
SQ SEQUENCE 329 AA; 38843 MW; 2384486A69C20628 CRC64;
MKLNYDFFLN KFSNVYNNDI RLVDLSNKWW YHNCRVHFAG NQKHSFHIVT RSPWPLYSSI
AALMFTFGMV MHMHNYSYGN LLSLAGFLLI LLMMFVWWRD VIRESTFSGY HTKKVQQGLR
LGVILFIISE VMFFFSFFWA FFHASLSPSV VLGSVWPPLG INVLNPLKIP LLNTLILLLS
GLTVTWSHHV IRDKSWQKFF FSSTDNEEFK TPLLDNYVIC AFALFLTIFL GLEFTVWQGY
EYYKASFYIY DGVYGSTFYM TTGLHGLHVI IGTLFLIVCF FRLIDLHFIY NHHFGYEAAI
WYWHFVDVVW IFLFLSIYCW GSGVDSFFK
//