COX1_ALKPO
ID COX1_ALKPO Reviewed; 625 AA.
AC Q04440; D3FU49;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 3.
DT 03-AUG-2022, entry version 137.
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; OrderedLocusNames=BpOF4_00910;
OS Alkalihalophilus pseudofirmus (strain ATCC BAA-2126 / JCM 17055 / OF4)
OS (Bacillus pseudofirmus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalophilus.
OX NCBI_TaxID=398511;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-13.
RX PubMed=7678007; DOI=10.1016/s0021-9258(18)54205-8;
RA Quirk P.G., Hicks D.B., Krulwich T.A.;
RT "Cloning of the cta operon from alkaliphilic Bacillus firmus OF4 and
RT characterization of the pH-regulated cytochrome caa3 oxidase it encodes.";
RL J. Biol. Chem. 268:678-685(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2126 / JCM 17055 / OF4;
RX PubMed=21951522; DOI=10.1111/j.1462-2920.2011.02591.x;
RA Janto B., Ahmed A., Ito M., Liu J., Hicks D.B., Pagni S., Fackelmayer O.J.,
RA Smith T.A., Earl J., Elbourne L.D., Hassan K., Paulsen I.T., Kolsto A.B.,
RA Tourasse N.J., Ehrlich G.D., Boissy R., Ivey D.M., Li G., Xue Y., Ma Y.,
RA Hu F.Z., Krulwich T.A.;
RT "Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that
RT support the ability to grow in an external pH range from 7.5 to 11.4.";
RL Environ. Microbiol. 13:3289-3309(2011).
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.
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 -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Elevated expression at high pH.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; M94110; AAA22365.1; -; Genomic_DNA.
DR EMBL; CP001878; ADC48251.1; -; Genomic_DNA.
DR RefSeq; WP_012959533.1; NC_013791.2.
DR AlphaFoldDB; Q04440; -.
DR SMR; Q04440; -.
DR STRING; 398511.BpOF4_00910; -.
DR EnsemblBacteria; ADC48251; ADC48251; BpOF4_00910.
DR KEGG; bpf:BpOF4_00910; -.
DR eggNOG; COG0843; Bacteria.
DR HOGENOM; CLU_011899_7_1_9; -.
DR OMA; PVDFQYH; -.
DR OrthoDB; 316745at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000001544; Chromosome.
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; Reference proteome; Respiratory chain;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7678007"
FT CHAIN 2..625
FT /note="Cytochrome c oxidase subunit 1"
FT /id="PRO_0000183434"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 551..571
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 69
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 246
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 250
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 295
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 296
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 381
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 383
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 246..250
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250"
FT CONFLICT 575
FT /note="N -> K (in Ref. 1; AAA22365)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 625 AA; 69871 MW; 6D8058522B7C54A4 CRC64;
MATQKQEKSV IWDWLTTVDH KKIAIMYLIA GTLFFVKAGV MALFMRIQLM YPEMNFLSGQ
TFNEFITMHG TIMLFLAATP LLFAFMNYVI PLQIGARDVA FPFVNALGFW IFFFGGLLLS
LSWFFGGGPD AGWTAYVPLS SRDYGGLGID FYVLGLQVSG IGTLISAINF LVTIVNMRAP
GMTMMRLPLF VWTSFISSTL ILFAFTPLAA GLALLMLDRL FEAQYFIPSM GGNVVLWQHI
FWIFGHPEVY ILVLPAFGII SEVIPAFSRK RLFGYTAMVF ATMIIAFLGF MVWAHHMFTV
GMGPVANSIF AVATMTIAVP TGIKIFNWLF TMWGGKITFN TAMLFASSFV PTFVLGGVTG
VMLAMAPVDY LYHDTYFVVA HFHYIIVGGI VLSLFAGLFY WYPKMFGHML NETLGKLFFW
VFYIGFHLTF FVQHLLGLMG MPRRVYTYLG DQGLDAFNFI STIGTFFMSA GVILLVINVI
YSAFKGERVT VADPWDARTL EWATPTPVPE YNFAQTPQVR SLDPLFYEKI HGDGTMKPAE
PVTDIHMPNG SILPFIMSIG LFFAGFGLIM LNMDNPIINP WIVAIGGLAL TFGCMFVRSI
KEDHGYHIPA EQVKADLAEL KKGGN
