COX1_BOVIN
ID COX1_BOVIN Reviewed; 514 AA.
AC P00396;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Cytochrome c oxidase subunit 1;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide I;
GN Name=MT-CO1; Synonyms=COI, COXI, MTCO1;
OS Bos taurus (Bovine).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000312|Proteomes:UP000009136}; TISSUE=Heart;
RX PubMed=7120390; DOI=10.1016/0022-2836(82)90137-1;
RA Anderson S., de Bruijn M.H.L., Coulson A.R., Eperon I.C., Sanger F.,
RA Young I.G.;
RT "Complete sequence of bovine mitochondrial DNA. Conserved features of the
RT mammalian mitochondrial genome.";
RL J. Mol. Biol. 156:683-717(1982).
RN [2]
RP PROTEIN SEQUENCE, AND FORMYLATION AT MET-1.
RC TISSUE=Heart;
RX PubMed=2165784; DOI=10.1515/bchm3.1990.371.1.411;
RA Hensel S., Buse G.;
RT "Studies on cytochrome-c oxidase, XIV. The amino-acid sequence of subunit I
RT -- proteinchemical methods for the analysis of a large hydrophobic membrane
RT protein.";
RL Biol. Chem. Hoppe-Seyler 371:411-422(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=65, 66, D, and F;
RA Wettstein P.J.;
RT "Bos taurus mitochondrial protein coding regions.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP COVALENT BOND.
RX PubMed=10338009; DOI=10.1110/ps.8.5.985;
RA Buse G., Soulimane T., Dewor M., Meyer H.E., Blueggel M.;
RT "Evidence for a copper-coordinated histidine-tyrosine cross-link in the
RT active site of cytochrome oxidase.";
RL Protein Sci. 8:985-990(1999).
RN [5]
RP SUBUNIT.
RX PubMed=26698328; DOI=10.1074/jbc.m115.680553;
RA Shinzawa-Itoh K., Shimomura H., Yanagisawa S., Shimada S., Takahashi R.,
RA Oosaki M., Ogura T., Tsukihara T.;
RT "Purification of active respiratory supercomplex from bovine heart
RT mitochondria enables functional studies.";
RL J. Biol. Chem. 291:4178-4184(2016).
RN [6]
RP METAL BINDING.
RX PubMed=23537388; DOI=10.1021/ja4005706;
RA Marechal A., Iwaki M., Rich P.R.;
RT "Structural changes in cytochrome c oxidase induced by binding of sodium
RT and calcium ions: an ATR-FTIR study.";
RL J. Am. Chem. Soc. 135:5802-5807(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=8638158; DOI=10.1126/science.272.5265.1136;
RA Tsukihara T., Aoyama H., Yamashita E., Tomizaki T., Yamaguchi H.,
RA Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.;
RT "The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8
RT A.";
RL Science 272:1136-1144(1996).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RC TISSUE=Heart;
RX PubMed=10089392; DOI=10.1107/s0907444998006362;
RA Tomizaki T., Yamashita E., Yamaguchi H., Aoyama H., Tsukihara T.,
RA Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.;
RT "Structure analysis of bovine heart cytochrome c oxidase at 2.8 A
RT resolution.";
RL Acta Crystallogr. D 55:31-45(1999).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RC TISSUE=Heart;
RX PubMed=10771420; DOI=10.1107/s0907444900002213;
RA Fei M.J., Yamashita E., Inoue N., Yao M., Yamaguchi H., Tsukihara T.,
RA Shinzawa-Itoh K., Nakashima R., Yoshikawa S.;
RT "X-ray structure of azide-bound fully oxidized cytochrome c oxidase from
RT bovine heart at 2.9 A resolution.";
RL Acta Crystallogr. D 56:529-535(2000).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
RX PubMed=20385840; DOI=10.1073/pnas.0910410107;
RA Muramoto K., Ohta K., Shinzawa-Itoh K., Kanda K., Taniguchi M.,
RA Nabekura H., Yamashita E., Tsukihara T., Yoshikawa S.;
RT "Bovine cytochrome c oxidase structures enable O2 reduction with
RT minimization of reactive oxygens and provide a proton-pumping gate.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:7740-7745(2010).
RN [11]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.10 ANGSTROMS), AND SUBUNIT.
RX PubMed=27830641; DOI=10.7554/elife.21290;
RA Sousa J.S., Mills D.J., Vonck J., Kuehlbrandt W.;
RT "Functional asymmetry and electron flow in the bovine respirasome.";
RL Elife 5:0-0(2016).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH SODIUM.
RX PubMed=27605664; DOI=10.1074/jbc.m115.711770;
RA Yano N., Muramoto K., Shimada A., Takemura S., Baba J., Fujisawa H.,
RA Mochizuki M., Shinzawa-Itoh K., Yamashita E., Tsukihara T., Yoshikawa S.;
RT "The Mg2+-containing water cluster of mammalian cytochrome c oxidase
RT collects four pumping proton equivalents in each catalytic cycle.";
RL J. Biol. Chem. 291:23882-23894(2016).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=31533957; DOI=10.1073/pnas.1907183116;
RA Shinzawa-Itoh K., Sugimura T., Misaki T., Tadehara Y., Yamamoto S.,
RA Hanada M., Yano N., Nakagawa T., Uene S., Yamada T., Aoyama H.,
RA Yamashita E., Tsukihara T., Yoshikawa S., Muramoto K.;
RT "Monomeric structure of an active form of bovine cytochrome c oxidase.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:19945-19951(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:0000250|UniProtKB:P00401}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=7.1.1.9;
CC Evidence={ECO:0000250|UniProtKB:P00401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC Evidence={ECO:0000250|UniProtKB:P00401};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:2165784,
CC ECO:0000269|PubMed:8638158};
CC Note=Binds 2 heme A groups non-covalently per subunit.
CC {ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:2165784,
CC ECO:0000269|PubMed:8638158};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:2165784,
CC ECO:0000269|PubMed:8638158};
CC Note=Binds a copper B center. {ECO:0000269|PubMed:20385840,
CC ECO:0000269|PubMed:2165784, ECO:0000269|PubMed:8638158};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P00401}.
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of 14 subunits. The complex is composed of
CC a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in
CC the mitochondrial DNA, and 11 supernumerary subunits COX4I1 (or
CC COX4I2), COX5A, COX5B, COX6A2 (or COX6A1), COX6B1 (or COX6B2), COX6C,
CC COX7A1 (or COX7A2), COX7B, COX7C, COX8B and NDUFA4, which are encoded
CC in the nuclear genome (PubMed:8638158). The complex exists as a monomer
CC or a dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex
CC III, CIII), resulting in different assemblies (supercomplex
CC SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (PubMed:26698328,
CC PubMed:27830641). As a newly synthesized protein, rapidly incorporates
CC into a multi-subunit assembly intermediate in the inner membrane,
CC called MITRAC (mitochondrial translation regulation assembly
CC intermediate of cytochrome c oxidase) complex, whose core components
CC are COA3/MITRAC12 and COX14. Within the MITRAC complex, interacts with
CC COA3 and with SMIM20/MITRAC7; the interaction with SMIM20 stabilizes
CC the newly synthesized MT-CO1 and prevents its premature turnover.
CC Interacts with TMEM177 in a COX20-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:P00395, ECO:0000269|PubMed:26698328,
CC ECO:0000269|PubMed:27830641, ECO:0000269|PubMed:8638158}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:27605664,
CC ECO:0000269|PubMed:31533957}.
CC -!- PTM: His-240 and Tyr-244 are involved in the formation of a copper-
CC coordinated covalent cross-link at the active site of the catalytic
CC subunit I.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; V00654; CAA23999.1; -; Genomic_DNA.
DR EMBL; AF490528; AAM08330.1; -; Genomic_DNA.
DR EMBL; AF490529; AAM08343.1; -; Genomic_DNA.
DR EMBL; AF493541; AAM12791.1; -; Genomic_DNA.
DR EMBL; AF493542; AAM12804.1; -; Genomic_DNA.
DR PIR; A00464; ODBO1.
DR PDB; 1OCC; X-ray; 2.80 A; A/N=1-514.
DR PDB; 1OCO; X-ray; 2.80 A; A/N=1-514.
DR PDB; 1OCR; X-ray; 2.35 A; A/N=1-514.
DR PDB; 1OCZ; X-ray; 2.90 A; A/N=1-514.
DR PDB; 1V54; X-ray; 1.80 A; A/N=1-514.
DR PDB; 1V55; X-ray; 1.90 A; A/N=1-514.
DR PDB; 2DYR; X-ray; 1.80 A; A/N=1-514.
DR PDB; 2DYS; X-ray; 2.20 A; A/N=1-514.
DR PDB; 2EIJ; X-ray; 1.90 A; A/N=1-514.
DR PDB; 2EIK; X-ray; 2.10 A; A/N=1-514.
DR PDB; 2EIL; X-ray; 2.10 A; A/N=1-514.
DR PDB; 2EIM; X-ray; 2.60 A; A/N=1-514.
DR PDB; 2EIN; X-ray; 2.70 A; A/N=1-514.
DR PDB; 2OCC; X-ray; 2.30 A; A/N=1-514.
DR PDB; 2Y69; X-ray; 1.95 A; A/N=1-514.
DR PDB; 2YBB; EM; 19.00 A; L=1-514.
DR PDB; 2ZXW; X-ray; 2.50 A; A/N=1-514.
DR PDB; 3ABK; X-ray; 2.00 A; A/N=1-514.
DR PDB; 3ABL; X-ray; 2.10 A; A/N=1-514.
DR PDB; 3ABM; X-ray; 1.95 A; A/N=1-514.
DR PDB; 3AG1; X-ray; 2.20 A; A/N=1-514.
DR PDB; 3AG2; X-ray; 1.80 A; A/N=1-514.
DR PDB; 3AG3; X-ray; 1.80 A; A/N=1-514.
DR PDB; 3AG4; X-ray; 2.05 A; A/N=1-514.
DR PDB; 3ASN; X-ray; 3.00 A; A/N=1-514.
DR PDB; 3ASO; X-ray; 2.30 A; A/N=1-514.
DR PDB; 3WG7; X-ray; 1.90 A; A/N=1-514.
DR PDB; 3X2Q; X-ray; 2.00 A; A/N=1-514.
DR PDB; 5B1A; X-ray; 1.50 A; A/N=1-514.
DR PDB; 5B1B; X-ray; 1.60 A; A/N=1-514.
DR PDB; 5B3S; X-ray; 1.68 A; A/N=2-514.
DR PDB; 5GPN; EM; 5.40 A; y=1-514.
DR PDB; 5IY5; X-ray; 2.00 A; A/N=1-514.
DR PDB; 5LUF; EM; 9.10 A; x=1-514.
DR PDB; 5W97; X-ray; 2.30 A; A/a=1-514.
DR PDB; 5WAU; X-ray; 1.95 A; A/a=1-514.
DR PDB; 5X19; X-ray; 2.20 A; A/N=1-514.
DR PDB; 5X1B; X-ray; 2.40 A; A/N=1-514.
DR PDB; 5X1F; X-ray; 2.20 A; A/N=1-514.
DR PDB; 5XDQ; X-ray; 1.77 A; A/N=1-514.
DR PDB; 5XDX; X-ray; 1.99 A; A/N=1-514.
DR PDB; 5XTH; EM; 3.90 A; x=1-514.
DR PDB; 5XTI; EM; 17.40 A; Bx/x=1-514.
DR PDB; 5Z84; X-ray; 1.85 A; A/N=1-514.
DR PDB; 5Z85; X-ray; 1.85 A; A/N=1-514.
DR PDB; 5Z86; X-ray; 1.85 A; A/N=1-514.
DR PDB; 5ZCO; X-ray; 1.90 A; A/N=1-514.
DR PDB; 5ZCP; X-ray; 1.65 A; A/N=1-514.
DR PDB; 5ZCQ; X-ray; 1.65 A; A/N=1-514.
DR PDB; 6J8M; X-ray; 1.90 A; A/N=1-514.
DR PDB; 6JUW; X-ray; 1.80 A; A/N=1-514.
DR PDB; 6JY3; X-ray; 1.85 A; A=1-514.
DR PDB; 6JY4; X-ray; 1.95 A; A=1-514.
DR PDB; 6NKN; X-ray; 2.50 A; A/N=1-514.
DR PDB; 6NMF; X-ray; 2.80 A; A/N=1-514.
DR PDB; 6NMP; X-ray; 2.90 A; A/N=1-514.
DR PDB; 7COH; X-ray; 1.30 A; A/N=1-514.
DR PDB; 7CP5; X-ray; 1.76 A; A/N=1-514.
DR PDB; 7D5W; X-ray; 1.84 A; A/N=1-514.
DR PDB; 7D5X; X-ray; 1.74 A; A/N=1-514.
DR PDB; 7EV7; X-ray; 1.70 A; A/N=1-514.
DR PDB; 7THU; X-ray; 1.93 A; AAA/NNN=1-514.
DR PDB; 7TIE; X-ray; 1.90 A; AAA/NNN=1-514.
DR PDB; 7TIH; X-ray; 2.35 A; AAA/NNN=1-514.
DR PDB; 7TII; X-ray; 2.45 A; AAA/NNN=1-514.
DR PDBsum; 1OCC; -.
DR PDBsum; 1OCO; -.
DR PDBsum; 1OCR; -.
DR PDBsum; 1OCZ; -.
DR PDBsum; 1V54; -.
DR PDBsum; 1V55; -.
DR PDBsum; 2DYR; -.
DR PDBsum; 2DYS; -.
DR PDBsum; 2EIJ; -.
DR PDBsum; 2EIK; -.
DR PDBsum; 2EIL; -.
DR PDBsum; 2EIM; -.
DR PDBsum; 2EIN; -.
DR PDBsum; 2OCC; -.
DR PDBsum; 2Y69; -.
DR PDBsum; 2YBB; -.
DR PDBsum; 2ZXW; -.
DR PDBsum; 3ABK; -.
DR PDBsum; 3ABL; -.
DR PDBsum; 3ABM; -.
DR PDBsum; 3AG1; -.
DR PDBsum; 3AG2; -.
DR PDBsum; 3AG3; -.
DR PDBsum; 3AG4; -.
DR PDBsum; 3ASN; -.
DR PDBsum; 3ASO; -.
DR PDBsum; 3WG7; -.
DR PDBsum; 3X2Q; -.
DR PDBsum; 5B1A; -.
DR PDBsum; 5B1B; -.
DR PDBsum; 5B3S; -.
DR PDBsum; 5GPN; -.
DR PDBsum; 5IY5; -.
DR PDBsum; 5LUF; -.
DR PDBsum; 5W97; -.
DR PDBsum; 5WAU; -.
DR PDBsum; 5X19; -.
DR PDBsum; 5X1B; -.
DR PDBsum; 5X1F; -.
DR PDBsum; 5XDQ; -.
DR PDBsum; 5XDX; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR PDBsum; 5Z84; -.
DR PDBsum; 5Z85; -.
DR PDBsum; 5Z86; -.
DR PDBsum; 5ZCO; -.
DR PDBsum; 5ZCP; -.
DR PDBsum; 5ZCQ; -.
DR PDBsum; 6J8M; -.
DR PDBsum; 6JUW; -.
DR PDBsum; 6JY3; -.
DR PDBsum; 6JY4; -.
DR PDBsum; 6NKN; -.
DR PDBsum; 6NMF; -.
DR PDBsum; 6NMP; -.
DR PDBsum; 7COH; -.
DR PDBsum; 7CP5; -.
DR PDBsum; 7D5W; -.
DR PDBsum; 7D5X; -.
DR PDBsum; 7EV7; -.
DR PDBsum; 7THU; -.
DR PDBsum; 7TIE; -.
DR PDBsum; 7TIH; -.
DR PDBsum; 7TII; -.
DR AlphaFoldDB; P00396; -.
DR SMR; P00396; -.
DR CORUM; P00396; -.
DR DIP; DIP-60937N; -.
DR IntAct; P00396; 13.
DR MINT; P00396; -.
DR STRING; 9913.ENSBTAP00000053147; -.
DR TCDB; 3.D.4.7.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR iPTMnet; P00396; -.
DR PaxDb; P00396; -.
DR PRIDE; P00396; -.
DR eggNOG; KOG4769; Eukaryota.
DR InParanoid; P00396; -.
DR BRENDA; 7.1.1.9; 908.
DR SABIO-RK; P00396; -.
DR UniPathway; UPA00705; -.
DR EvolutionaryTrace; P00396; -.
DR Proteomes; UP000009136; Mitochondrion.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IBA:GO_Central.
DR GO; GO:0045277; C:respiratory chain complex IV; IDA:UniProtKB.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR CDD; cd01663; Cyt_c_Oxidase_I; 1.
DR Gene3D; 1.20.210.10; -; 1.
DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR InterPro; IPR000883; Cyt_C_Oxase_1.
DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR033944; Cyt_c_oxase_su1_dom.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Copper; Direct protein sequencing;
KW Electron transport; Formylation; Heme; Iron; Magnesium; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Sodium; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..514
FT /note="Cytochrome c oxidase subunit 1"
FT /id="PRO_0000183294"
FT TOPO_DOM 1..11
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:2165784,
FT ECO:0000269|PubMed:27605664"
FT TRANSMEM 12..40
FT /note="Helical; Name=I"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 41..50
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:27605664,
FT ECO:0000269|PubMed:8638158"
FT TRANSMEM 51..86
FT /note="Helical; Name=II"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 87..94
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:2165784,
FT ECO:0000269|PubMed:27605664"
FT TRANSMEM 95..117
FT /note="Helical; Name=III"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 118..140
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:2165784,
FT ECO:0000269|PubMed:27605664"
FT TRANSMEM 141..170
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 171..182
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:2165784,
FT ECO:0000269|PubMed:27605664"
FT TRANSMEM 183..212
FT /note="Helical; Name=V"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 213..227
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:2165784,
FT ECO:0000269|PubMed:27605664"
FT TRANSMEM 228..261
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 262..269
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:2165784,
FT ECO:0000269|PubMed:27605664"
FT TRANSMEM 270..286
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 287..298
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:2165784,
FT ECO:0000269|PubMed:27605664"
FT TRANSMEM 299..327
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 328..335
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TRANSMEM 336..357
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 358..370
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TRANSMEM 371..400
FT /note="Helical; Name=X"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 401..406
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:2165784,
FT ECO:0000269|PubMed:27605664"
FT TRANSMEM 407..433
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 434..446
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TRANSMEM 447..478
FT /note="Helical; Name=XII"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 479..514
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:2165784,
FT ECO:0000269|PubMed:27605664"
FT BINDING 40
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:27605664,
FT ECO:0000305|PubMed:23537388"
FT BINDING 45
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:27605664,
FT ECO:0000305|PubMed:23537388"
FT BINDING 61
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_note="low-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:20385840,
FT ECO:0000269|PubMed:8638158"
FT BINDING 240
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000269|PubMed:20385840,
FT ECO:0000269|PubMed:8638158"
FT BINDING 244
FT /ligand="O2"
FT /ligand_id="ChEBI:CHEBI:15379"
FT /evidence="ECO:0000305"
FT BINDING 290
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000269|PubMed:20385840,
FT ECO:0000269|PubMed:8638158"
FT BINDING 291
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000269|PubMed:20385840,
FT ECO:0000269|PubMed:8638158"
FT BINDING 368
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with MT-CO2"
FT /evidence="ECO:0000269|PubMed:20385840,
FT ECO:0000269|PubMed:8638158"
FT BINDING 369
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with MT-CO2"
FT /evidence="ECO:0000269|PubMed:20385840,
FT ECO:0000269|PubMed:8638158"
FT BINDING 376
FT /ligand="heme a3"
FT /ligand_id="ChEBI:CHEBI:83282"
FT /ligand_note="high-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:20385840,
FT ECO:0000269|PubMed:8638158"
FT BINDING 378
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_note="low-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:20385840,
FT ECO:0000269|PubMed:8638158"
FT BINDING 441
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:27605664,
FT ECO:0000305|PubMed:23537388"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:2165784"
FT CROSSLNK 240..244
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000269|PubMed:10338009"
FT HELIX 2..6
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 12..40
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:5B1B"
FT HELIX 51..67
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:7COH"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 78..86
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:7COH"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:7COH"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:7COH"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 142..170
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 183..214
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 228..261
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:2EIM"
FT HELIX 299..311
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 313..327
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 336..358
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 361..367
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 371..381
FT /evidence="ECO:0007829|PDB:7COH"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 385..401
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 407..425
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 428..433
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:5B1B"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 448..478
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 481..484
FT /evidence="ECO:0007829|PDB:3AG3"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:7COH"
SQ SEQUENCE 514 AA; 57032 MW; 0D7C807D7FA3996C CRC64;
MFINRWLFST NHKDIGTLYL LFGAWAGMVG TALSLLIRAE LGQPGTLLGD DQIYNVVVTA
HAFVMIFFMV MPIMIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSMVEA
GAGTGWTVYP PLAGNLAHAG ASVDLTIFSL HLAGVSSILG AINFITTIIN MKPPAMSQYQ
TPLFVWSVMI TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH
PEVYILILPG FGMISHIVTY YSGKKEPFGY MGMVWAMMSI GFLGFIVWAH HMFTVGMDVD
TRAYFTSATM IIAIPTGVKV FSWLATLHGG NIKWSPAMMW ALGFIFLFTV GGLTGIVLAN
SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM GGFVHWFPLF SGYTLNDTWA KIHFAIMFVG
VNMTFFPQHF LGLSGMPRRY SDYPDAYTMW NTISSMGSFI SLTAVMLMVF IIWEAFASKR
EVLTVDLTTT NLEWLNGCPP PYHTFEEPTY VNLK
