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Cytochrome bd-I ubiquinol oxidase subunit 1 (EC 1.10.3.14) (Cytochrome bd-I oxidase subunit I) (Cytochrome d ubiquinol oxidase subunit I)

 CYDA_ECOLI              Reviewed;         522 AA.
P0ABJ9; P11026; P75754; P76823;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
25-OCT-2005, sequence version 1.
12-SEP-2018, entry version 111.
RecName: Full=Cytochrome bd-I ubiquinol oxidase subunit 1;
EC=1.10.3.14 {ECO:0000269|PubMed:1850294};
AltName: Full=Cytochrome bd-I oxidase subunit I;
AltName: Full=Cytochrome d ubiquinol oxidase subunit I;
Name=cydA; Synonyms=cyd-1; OrderedLocusNames=b0733, JW0722;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=2843510;
Green G.N., Fang H., Lin R.-J., Newton G., Mather M., Georgiou C.D.,
Gennis R.B.;
"The nucleotide sequence of the cyd locus encoding the two subunits of
the cytochrome d terminal oxidase complex of Escherichia coli.";
J. Biol. Chem. 263:13138-13143(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 1-6, FORMYLATION AT MET-1, AND SUBUNIT.
STRAIN=MR43L/F152;
PubMed=3281937;
Miller M.J., Hermodson M., Gennis R.B.;
"The active form of the cytochrome d terminal oxidase complex of
Escherichia coli is a heterodimer containing one copy of each of the
two subunits.";
J. Biol. Chem. 263:5235-5240(1988).
[6]
FUNCTION AS AN OXIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
REGULATION, COFACTOR, SUBUNIT, AND INDUCTION.
STRAIN=MR43L/F152;
PubMed=6307994;
Miller M.J., Gennis R.B.;
"The purification and characterization of the cytochrome d terminal
oxidase complex of the Escherichia coli aerobic respiratory chain.";
J. Biol. Chem. 258:9159-9165(1983).
[7]
COFACTOR.
PubMed=3013298; DOI=10.1021/bi00357a002;
Green G.N., Lorence R.M., Gennis R.B.;
"Specific overproduction and purification of the cytochrome b558
component of the cytochrome d complex from Escherichia coli.";
Biochemistry 25:2309-2314(1986).
[8]
COFACTOR.
STRAIN=MR43L/F152;
PubMed=3013299; DOI=10.1021/bi00357a003;
Lorence R.M., Koland J.G., Gennis R.B.;
"Coulometric and spectroscopic analysis of the purified cytochrome d
complex of Escherichia coli: evidence for the identification of
'cytochrome a1' as cytochrome b595.";
Biochemistry 25:2314-2321(1986).
[9]
TOPOLOGY.
PubMed=3138232;
Georgiou C.D., Dueweke T.J., Gennis R.B.;
"Beta-galactosidase gene fusions as probes for the cytoplasmic regions
of subunits I and II of the membrane-bound cytochrome d terminal
oxidase from Escherichia coli.";
J. Biol. Chem. 263:13130-13137(1988).
[10]
FUNCTION, COFACTOR, AND MUTAGENESIS OF HIS-19; HIS-86; HIS-126;
HIS-186; HIS-314 AND HIS-510.
PubMed=2656671;
Fang H., Lin R.J., Gennis R.B.;
"Location of heme axial ligands in the cytochrome d terminal oxidase
complex of Escherichia coli determined by site-directed mutagenesis.";
J. Biol. Chem. 264:8026-8032(1989).
[11]
DOMAINS.
PubMed=1689724;
Dueweke T.J., Gennis R.B.;
"Epitopes of monoclonal antibodies which inhibit ubiquinol oxidase
activity of Escherichia coli cytochrome d complex localize functional
domain.";
J. Biol. Chem. 265:4273-4277(1990).
[12]
CATALYTIC ACTIVITY.
PubMed=1850294;
Puustinen A., Finel M., Haltia T., Gennis R.B., Wikstroem M.;
"Properties of the two terminal oxidases of Escherichia coli.";
Biochemistry 30:3936-3942(1991).
[13]
TOPOLOGY.
PubMed=1724280; DOI=10.1111/j.1365-2958.1991.tb02097.x;
Newton G., Yun C.H., Gennis R.B.;
"Analysis of the topology of the cytochrome d terminal oxidase complex
of Escherichia coli by alkaline phosphatase fusions.";
Mol. Microbiol. 5:2511-2518(1991).
[14]
FUNCTION, COFACTOR, AND MUTAGENESIS OF MET-393.
PubMed=7577938; DOI=10.1021/bi00041a029;
Kaysser T.M., Ghaim J.B., Georgiou C., Gennis R.B.;
"Methionine-393 is an axial ligand of the heme b558 component of the
cytochrome bd ubiquinol oxidase from Escherichia coli.";
Biochemistry 34:13491-13501(1995).
[15]
SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=15013751; DOI=10.1016/S0014-5793(04)00125-5;
Zhang J., Barquera B., Gennis R.B.;
"Gene fusions with beta-lactamase show that subunit I of the
cytochrome bd quinol oxidase from E. coli has nine transmembrane
helices with the O2 reactive site near the periplasmic surface.";
FEBS Lett. 561:58-62(2004).
[16]
SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BL21-DE3;
PubMed=16079137; DOI=10.1074/jbc.M506479200;
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
von Heijne G., Daley D.O.;
"Protein complexes of the Escherichia coli cell envelope.";
J. Biol. Chem. 280:34409-34419(2005).
[17]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
[18]
FUNCTION IN PROTON TRANSLOCATION, AND DISRUPTION PHENOTYPE.
STRAIN=K12;
PubMed=19542282; DOI=10.1128/JB.00562-09;
Bekker M., de Vries S., Ter Beek A., Hellingwerf K.J., de Mattos M.J.;
"Respiration of Escherichia coli can be fully uncoupled via the
nonelectrogenic terminal cytochrome bd-II oxidase.";
J. Bacteriol. 191:5510-5517(2009).
[19]
FUNCTION IN PROTON TRANSLOCATION, AND DISRUPTION PHENOTYPE.
STRAIN=K12;
PubMed=21987791; DOI=10.1073/pnas.1108217108;
Borisov V.B., Murali R., Verkhovskaya M.L., Bloch D.A., Han H.,
Gennis R.B., Verkhovsky M.I.;
"Aerobic respiratory chain of Escherichia coli is not allowed to work
in fully uncoupled mode.";
Proc. Natl. Acad. Sci. U.S.A. 108:17320-17324(2011).
[20]
PROBABLE INTERACTION WITH CYDX, POSSIBLE INTERACTION WITH APPX,
SUBUNIT, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=23749980; DOI=10.1128/JB.00324-13;
Vanorsdel C.E., Bhatt S., Allen R.J., Brenner E.P., Hobson J.J.,
Jamil A., Haynes B.M., Genson A.M., Hemm M.R.;
"The Escherichia coli CydX protein is a member of the CydAB cytochrome
bd oxidase complex and is required for cytochrome bd oxidase
activity.";
J. Bacteriol. 195:3640-3650(2013).
[21]
REVIEW.
PubMed=21756872; DOI=10.1016/j.bbabio.2011.06.016;
Borisov V.B., Gennis R.B., Hemp J., Verkhovsky M.I.;
"The cytochrome bd respiratory oxygen reductases.";
Biochim. Biophys. Acta 1807:1398-1413(2011).
-!- FUNCTION: A terminal oxidase that produces a proton motive force
by the vectorial transfer of protons across the inner membrane. It
is the component of the aerobic respiratory chain of E.coli that
predominates when cells are grown at low aeration. Generates a
proton motive force using protons and electrons from opposite
sides of the membrane to generate H(2)O, transferring 1
proton/electron. {ECO:0000269|PubMed:19542282,
ECO:0000269|PubMed:21987791, ECO:0000269|PubMed:2656671,
ECO:0000269|PubMed:6307994, ECO:0000269|PubMed:7577938}.
-!- CATALYTIC ACTIVITY: 2 ubiquinol + O(2)(Side 2) + 4 H(+)(Side 2) =
2 ubiquinone + 2 H(2)O(Side 2) + 4 H(+)(Side 1).
{ECO:0000269|PubMed:1850294, ECO:0000269|PubMed:6307994}.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000269|PubMed:2656671,
ECO:0000269|PubMed:3013298, ECO:0000269|PubMed:3013299,
ECO:0000269|PubMed:6307994, ECO:0000269|PubMed:7577938};
Note=Binds 1 protoheme IX center (heme b558) per subunit.
{ECO:0000269|PubMed:2656671, ECO:0000269|PubMed:3013298,
ECO:0000269|PubMed:3013299, ECO:0000269|PubMed:6307994,
ECO:0000269|PubMed:7577938};
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000269|PubMed:2656671,
ECO:0000269|PubMed:3013298, ECO:0000269|PubMed:3013299,
ECO:0000269|PubMed:6307994, ECO:0000269|PubMed:7577938};
Note=Binds 1 protoheme IX center (heme b595, originally called
cytochrome a1) per heterodimer, in conjunction with CydB.
{ECO:0000269|PubMed:2656671, ECO:0000269|PubMed:3013298,
ECO:0000269|PubMed:3013299, ECO:0000269|PubMed:6307994,
ECO:0000269|PubMed:7577938};
-!- COFACTOR:
Name=heme d cis-diol; Xref=ChEBI:CHEBI:62814;
Evidence={ECO:0000269|PubMed:2656671,
ECO:0000269|PubMed:3013298, ECO:0000269|PubMed:3013299,
ECO:0000269|PubMed:6307994, ECO:0000269|PubMed:7577938};
Note=Binds 1 iron-chlorin (heme d or cytochrome d) per
heterodimer, in conjunction with CydB.
{ECO:0000269|PubMed:2656671, ECO:0000269|PubMed:3013298,
ECO:0000269|PubMed:3013299, ECO:0000269|PubMed:6307994,
ECO:0000269|PubMed:7577938};
-!- ACTIVITY REGULATION: 90% inhibited by cyanide and 2-heptyl-4-
hydroxyquinoline N-oxide, at 1 mM and 40 uM respectively.
{ECO:0000269|PubMed:6307994}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.1 mM for ubiquinol-1 {ECO:0000269|PubMed:6307994};
KM=0.28 mM for 2,3,5,6-tetramethyl-p-phenylenediamine
{ECO:0000269|PubMed:6307994};
KM=0.68 mM for N,N,N',N'-tetramethyl-p-phenylenediamine
{ECO:0000269|PubMed:6307994};
Vmax=383 umol/min/mg enzyme for ubiquinol-1
{ECO:0000269|PubMed:6307994};
Vmax=270 umol/min/mg enzyme for 2,3,5,6-tetramethyl-p-
phenylenediamine {ECO:0000269|PubMed:6307994};
Vmax=126 umol/min/mg enzyme for N,N,N',N'-tetramethyl-p-
phenylenediamine {ECO:0000269|PubMed:6307994};
Note=pH 7.0, 37 degrees Celsius.;
-!- PATHWAY: Energy metabolism; oxidative phosphorylation.
-!- SUBUNIT: Heterodimer of subunits I and II. Probably interacts with
CydX, and overexpressed AppX. {ECO:0000269|PubMed:16079137,
ECO:0000269|PubMed:23749980, ECO:0000269|PubMed:3281937,
ECO:0000269|PubMed:6307994}.
-!- INTERACTION:
P0ABK2:cydB; NbExp=5; IntAct=EBI-906928, EBI-1213195;
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:15013751, ECO:0000269|PubMed:16079137}; Multi-
pass membrane protein {ECO:0000269|PubMed:15013751,
ECO:0000269|PubMed:16079137}.
-!- INDUCTION: Under conditions of low aeration, in stationary phase
(at protein level). {ECO:0000269|PubMed:6307994}.
-!- PTM: The N-terminus is blocked.
-!- DISRUPTION PHENOTYPE: A double cydA/cydB deletion shows increased
sensitivity to reductant (beta-mercapoethanol).
{ECO:0000269|PubMed:19542282, ECO:0000269|PubMed:21987791,
ECO:0000269|PubMed:23749980}.
-!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 1
family. {ECO:0000305}.
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EMBL; J03939; AAA18804.1; -; Unassigned_DNA.
EMBL; U00096; AAC73827.2; -; Genomic_DNA.
EMBL; AP009048; BAA35399.1; -; Genomic_DNA.
RefSeq; NP_415261.2; NC_000913.3.
RefSeq; WP_000884361.1; NZ_LN832404.1.
ProteinModelPortal; P0ABJ9; -.
BioGrid; 4263539; 372.
ComplexPortal; CPX-268; Cytochrome bd-I ubiquinol oxidase complex.
DIP; DIP-36181N; -.
IntAct; P0ABJ9; 4.
MINT; P0ABJ9; -.
STRING; 316385.ECDH10B_0799; -.
TCDB; 3.D.4.3.2; the proton-translocating cytochrome oxidase (cox) superfamily.
EPD; P0ABJ9; -.
PaxDb; P0ABJ9; -.
PRIDE; P0ABJ9; -.
EnsemblBacteria; AAC73827; AAC73827; b0733.
EnsemblBacteria; BAA35399; BAA35399; BAA35399.
GeneID; 945341; -.
KEGG; ecj:JW0722; -.
KEGG; eco:b0733; -.
PATRIC; fig|1411691.4.peg.1540; -.
EchoBASE; EB0170; -.
EcoGene; EG10173; cydA.
eggNOG; ENOG4105C4M; Bacteria.
eggNOG; COG1271; LUCA.
HOGENOM; HOG000084938; -.
InParanoid; P0ABJ9; -.
KO; K00425; -.
OMA; RDMTKFW; -.
PhylomeDB; P0ABJ9; -.
BioCyc; EcoCyc:CYDA-MONOMER; -.
BioCyc; MetaCyc:CYDA-MONOMER; -.
BRENDA; 1.10.3.14; 2026.
UniPathway; UPA00705; -.
PRO; PR:P0ABJ9; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0070069; C:cytochrome complex; IDA:EcoCyc.
GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
GO; GO:0016020; C:membrane; IDA:EcoCyc.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
GO; GO:0020037; F:heme binding; IDA:EcoCyc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016679; F:oxidoreductase activity, acting on diphenols and related substances as donors; IDA:EcoCyc.
GO; GO:0019646; P:aerobic electron transport chain; IDA:EcoCyc.
GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
InterPro; IPR002585; Cyt-d_ubiquinol_oxidase_su_1.
PANTHER; PTHR30365; PTHR30365; 1.
Pfam; PF01654; Cyt_bd_oxida_I; 1.
PIRSF; PIRSF006446; Cyt_quinol_oxidase_1; 1.
1: Evidence at protein level;
Cell inner membrane; Cell membrane; Complete proteome;
Direct protein sequencing; Electron transport; Formylation; Heme;
Iron; Membrane; Metal-binding; Oxidoreductase; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 522 Cytochrome bd-I ubiquinol oxidase subunit
1.
/FTId=PRO_0000183919.
TOPO_DOM 1 15 Periplasmic. {ECO:0000305}.
TRANSMEM 16 35 Helical. {ECO:0000305}.
TOPO_DOM 36 54 Cytoplasmic. {ECO:0000305}.
TRANSMEM 55 69 Helical. {ECO:0000305}.
TOPO_DOM 70 96 Periplasmic. {ECO:0000305}.
TRANSMEM 97 114 Helical. {ECO:0000305}.
TOPO_DOM 115 128 Cytoplasmic. {ECO:0000305}.
TRANSMEM 129 146 Helical. {ECO:0000305}.
TOPO_DOM 147 186 Periplasmic. {ECO:0000305}.
TRANSMEM 187 203 Helical. {ECO:0000305}.
TOPO_DOM 204 219 Cytoplasmic. {ECO:0000305}.
TRANSMEM 220 235 Helical. {ECO:0000305}.
TOPO_DOM 236 390 Periplasmic. {ECO:0000305}.
TRANSMEM 391 407 Helical. {ECO:0000305}.
TOPO_DOM 408 423 Cytoplasmic. {ECO:0000305}.
TRANSMEM 424 441 Helical. {ECO:0000305}.
TOPO_DOM 442 472 Periplasmic. {ECO:0000305}.
TRANSMEM 473 487 Helical. {ECO:0000305}.
TOPO_DOM 488 522 Cytoplasmic. {ECO:0000305}.
METAL 19 19 Iron (heme b595 axial ligand).
{ECO:0000255}.
METAL 186 186 Iron (heme b558 axial ligand).
METAL 393 393 Iron (heme b558 axial ligand).
MOD_RES 1 1 N-formylmethionine.
{ECO:0000269|PubMed:3281937}.
MUTAGEN 19 19 H->L,R: Loss of cytochrome b595 and heme
d, no aerobic growth, complex assembles.
{ECO:0000269|PubMed:2656671}.
MUTAGEN 86 86 H->R: No effect.
{ECO:0000269|PubMed:2656671}.
MUTAGEN 126 126 H->P: Loss of all cofactors, no aerobic
growth, complex assembles.
{ECO:0000269|PubMed:2656671}.
MUTAGEN 126 126 H->R: No effect.
{ECO:0000269|PubMed:2656671}.
MUTAGEN 186 186 H->L: Loss of cytochrome b558, no aerobic
growth, complex assembles, this subunit
is more susceptible to proteolysis.
{ECO:0000269|PubMed:2656671}.
MUTAGEN 314 314 H->L: Grows aerobically, has altered
cytochrome b/d ratio, complex assembles.
{ECO:0000269|PubMed:2656671}.
MUTAGEN 314 314 H->P: Loss of cytochrome b595 and heme d,
no aerobic growth, loss of complex.
{ECO:0000269|PubMed:2656671}.
MUTAGEN 393 393 M->L: Cytochrome b558 shifts to a high
spin configuration, complex assembles.
Retains about 1% quinol oxidoreductase
activity after purification.
MUTAGEN 510 510 H->L: No effect.
{ECO:0000269|PubMed:2656671}.
CONFLICT 213 213 F -> L (in Ref. 1; AAA18804).
{ECO:0000305}.
SEQUENCE 522 AA; 58205 MW; E757442068BCFCFE CRC64;
MLDIVELSRL QFALTAMYHF LFVPLTLGMA FLLAIMETVY VLSGKQIYKD MTKFWGKLFG
INFALGVATG LTMEFQFGTN WSYYSHYVGD IFGAPLAIEG LMAFFLESTF VGLFFFGWDR
LGKVQHMCVT WLVALGSNLS ALWILVANGW MQNPIASDFN FETMRMEMVS FSELVLNPVA
QVKFVHTVAS GYVTGAMFIL GISAWYMLKG RDFAFAKRSF AIAASFGMAA VLSVIVLGDE
SGYEMGDVQK TKLAAIEAEW ETQPAPAAFT LFGIPDQEEE TNKFAIQIPY ALGIIATRSV
DTPVIGLKEL MVQHEERIRN GMKAYSLLEQ LRSGSTDQAV RDQFNSMKKD LGYGLLLKRY
TPNVADATEA QIQQATKDSI PRVAPLYFAF RIMVACGFLL LAIIALSFWS VIRNRIGEKK
WLLRAALYGI PLPWIAVEAG WFVAEYGRQP WAIGEVLPTA VANSSLTAGD LIFSMVLICG
LYTLFLVAEL FLMFKFARLG PSSLKTGRYH FEQSSTTTQP AR


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EIAAB08786 Canis familiaris,Canis lupus familiaris,COX8B,COX8H,Cytochrome c oxidase polypeptide VIII-heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase sub
EIAAB10104 Cox7a2,Cox7a3,Cox7al,Cytochrome c oxidase subunit 7A2, mitochondrial,Cytochrome c oxidase subunit VIIa-L,Cytochrome c oxidase subunit VIIa-liver_heart,Rat,Rattus norvegicus
EIAAB10106 Cox7a2,Cox7a3,Cox7al,Cytochrome c oxidase subunit 7A2, mitochondrial,Cytochrome c oxidase subunit VIIa-L,Cytochrome c oxidase subunit VIIa-liver_heart,Mouse,Mus musculus
EIAAB10080 Bos taurus,Bovine,COX6A1,Cytochrome c oxidase polypeptide VIa-liver,Cytochrome c oxidase subunit 6A1, mitochondrial,Cytochrome c oxidase subunit SSG
EIAAB10103 Bos taurus,Bovine,COX7A2,COX7AL,Cytochrome c oxidase subunit 7A2, mitochondrial,Cytochrome c oxidase subunit VIIa-L,Cytochrome c oxidase subunit VIIa-liver_heart
EIAAB08759 Cox5b,Cytochrome c oxidase polypeptide Vb,Cytochrome c oxidase subunit 5B, mitochondrial,Cytochrome c oxidase subunit VIA*,Rat,Rattus norvegicus
EIAAB08746 COX IV-1,COX4,COX4I1,COXIV,Cytochrome c oxidase polypeptide IV,Cytochrome c oxidase subunit 4 isoform 1, mitochondrial,Cytochrome c oxidase subunit IV isoform 1,Oryctolagus cuniculus,Rabbit
EIAAB10095 Bos taurus,Bovine,COX VIb-2,COX6B2,Cytochrome c oxidase subunit 6B2,Cytochrome c oxidase subunit VIb isoform 2,Cytochrome c oxidase subunit VIb, testis-specific isoform
EIAAB10094 COX VIb-2,Cox6b2,Cytochrome c oxidase subunit 6B2,Cytochrome c oxidase subunit VIb isoform 2,Cytochrome c oxidase subunit VIb, testis-specific isoform,Rat,Rattus norvegicus
EIAAB10092 COX VIb-2,Cox6b2,Cytochrome c oxidase subunit 6B2,Cytochrome c oxidase subunit VIb isoform 2,Cytochrome c oxidase subunit VIb, testis-specific isoform,Mouse,Mus musculus


 

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