COX1_BACP3
ID COX1_BACP3 Reviewed; 616 AA.
AC P16262; Q56248;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cytochrome c oxidase subunit 1;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome aa3 subunit 1;
DE AltName: Full=Cytochrome c oxidase polypeptide I;
GN Name=ctaD; Synonyms=caaB, coi;
OS Bacillus sp. (strain PS3).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-31.
RX PubMed=1964459; DOI=10.1093/oxfordjournals.jbchem.a123294;
RA Ishizuka M., Machida K., Shimada S., Mogi A., Tsuchiya T., Ohmori T.,
RA Souma Y., Gonda M., Sone N.;
RT "Nucleotide sequence of the gene coding for four subunits of cytochrome c
RT oxidase from the thermophilic bacterium PS3.";
RL J. Biochem. 108:866-873(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-552, AND PROTEIN SEQUENCE OF 2-15.
RX PubMed=2844737; DOI=10.1093/oxfordjournals.jbchem.a122314;
RA Sone N., Yokoi F., Fu T., Ohta S., Metso T., Raitio M., Saraste M.;
RT "Nucleotide sequence of the gene coding for cytochrome oxidase subunit I
RT from the thermophilic bacterium PS3.";
RL J. Biochem. 103:606-610(1988).
RN [3]
RP CHARACTERIZATION.
RX PubMed=1652469; DOI=10.1016/0014-5793(91)81024-3;
RA Sone N., Fujiwara Y.;
RT "Haem O2 can replace haem A in the active site of cytochrome c oxidase from
RT thermophilic bacterium PS3.";
RL FEBS Lett. 288:154-158(1991).
CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC chain that catalyzes the reduction of oxygen to water. Subunits 1-3
CC form the functional core of the enzyme complex. Co I is the catalytic
CC subunit of the enzyme. Electrons originating in cytochrome c are
CC transferred via the copper A center of subunit 2 and heme a of subunit
CC 1 to the bimetallic center formed by heme a3 and copper B. This
CC cytochrome c oxidase shows proton pump activity across the membrane in
CC addition to the electron transfer.
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 -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Note=Binds 1 copper B ion per subunit.;
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 2 heme groups per subunit.;
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: Under slightly air-limited conditions, the cytochrome a3
CC center of the enzyme is replaced by cytochrome o.
CC -!- MISCELLANEOUS: This cytochrome c oxidase shows clear proton pump
CC activity in addition to electron transfer across the membrane.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA01793.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D13955; BAA03046.1; -; Genomic_DNA.
DR EMBL; D11038; BAA01793.1; ALT_FRAME; Genomic_DNA.
DR PIR; JX0140; JX0140.
DR AlphaFoldDB; P16262; -.
DR SMR; P16262; -.
DR UniPathway; UPA00705; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
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:0015990; P:electron transport coupled proton transport; IEA:InterPro.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
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; IPR014241; Cyt_c_oxidase_su1_bac.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR TIGRFAMs; TIGR02891; CtaD_CoxA; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Copper; Direct protein sequencing; Electron transport; Heme;
KW Iron; Membrane; Metal-binding; Respiratory chain; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1964459,
FT ECO:0000269|PubMed:2844737"
FT CHAIN 2..616
FT /note="Cytochrome c oxidase subunit 1"
FT /id="PRO_0000183435"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 72
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 249
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 253
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 298
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 299
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 384
FT /ligand="Fe(II)-heme o"
FT /ligand_id="ChEBI:CHEBI:60530"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 384
FT /ligand="heme a3"
FT /ligand_id="ChEBI:CHEBI:83282"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 386
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT CROSSLNK 249..253
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250"
FT CONFLICT 448
FT /note="V -> W (in Ref. 2; BAA01793)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="F -> I (in Ref. 2; BAA01793)"
FT /evidence="ECO:0000305"
FT CONFLICT 506..508
FT /note="AIA -> RS (in Ref. 2; BAA01793)"
FT /evidence="ECO:0000305"
FT CONFLICT 525..526
FT /note="LD -> WT (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 616 AA; 68294 MW; 17DF1E3325014B96 CRC64;
MSTIARKKGV GAVLWDYLTT VDHKKIAHLY LISGGFFFLL GGLEALFIRI QLAKPNNDFL
VGGLYNEVLT MHGTTMIFLA AMPLVFAFMN AVVPLQIGAR DVAFPFLNAL GFWMFFFGGL
FLNCSWFLGG APDAGWTSYA SLSLDSKAHH GIDFYTLGLQ ISGFGTIMGA INFLVTIINM
RAPGMTFMRM PMFTWATFVT SALILFAFPP LTVGLIFMMM DRLFGGNFFN PAAGGNTIIW
EHLFWVFGHP EVYILVLPAF GIFSEIFATF SRKRLFGYSS MVFATVLIAF LGFMVWAHHM
FTVGMGPIAN AIFAVATMTI AVPTGVKIFN WLFTMWGGSI KFTTPMHYAV AFIPSFVMGG
VTGVMLASAA ADYQYHDSYF VVAHFHYVIV GGVVFALLAG THYWWPKMFG RMLNETLGKI
TFWLFFIGFH LTFFIQHFLG LTGMPRRVFT YLPHQGWETG NLISTIGAFF IAAATVILLI
NIVVTTAKGE KVPGDAWGDG RTLEWAIASP PPVYNFAQTP LVRGLDAFWL EKMEGKKELT
PAEPLGDIHM PNSSFLPFVI AFGLFVAAFG FTYHNDAGWG LPVAILGLLI TLGSMFLRSV
IDDHGFHIHK EEVLEL
