ID A3PBG7_PROM0 Unreviewed; 541 AA.
AC A3PBG7;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 103.
DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061};
DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU363061};
GN Name=cyoB {ECO:0000313|EMBL:ABO17092.1};
GN OrderedLocusNames=P9301_04691 {ECO:0000313|EMBL:ABO17092.1};
OS Prochlorococcus marinus (strain MIT 9301).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167546 {ECO:0000313|EMBL:ABO17092.1, ECO:0000313|Proteomes:UP000001430};
RN [1] {ECO:0000313|EMBL:ABO17092.1, ECO:0000313|Proteomes:UP000001430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9301 {ECO:0000313|EMBL:ABO17092.1,
RC ECO:0000313|Proteomes:UP000001430};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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 {ECO:0000256|RuleBase:RU363061}.
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:0000256|ARBA:ARBA00029368,
CC ECO:0000256|RuleBase:RU363061};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU363061}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU363061};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU363061}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000256|RuleBase:RU000370}.
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DR EMBL; CP000576; ABO17092.1; -; Genomic_DNA.
DR RefSeq; WP_011862467.1; NC_009091.1.
DR AlphaFoldDB; A3PBG7; -.
DR STRING; 167546.P9301_04691; -.
DR KEGG; pmg:P9301_04691; -.
DR eggNOG; COG0843; Bacteria.
DR HOGENOM; CLU_011899_7_3_3; -.
DR OMA; WAMMSIG; -.
DR OrthoDB; 9759913at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000001430; Chromosome.
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; Cytochrome c oxidase-like, subunit I domain; 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 NCBIfam; TIGR02891; CtaD_CoxA; 1.
DR PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR PANTHER; PTHR10422:SF18; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|RuleBase:RU363061};
KW Copper {ECO:0000256|RuleBase:RU363061};
KW Electron transport {ECO:0000256|RuleBase:RU000370};
KW Heme {ECO:0000256|RuleBase:RU000370}; Iron {ECO:0000256|RuleBase:RU363061};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363061};
KW Metal-binding {ECO:0000256|RuleBase:RU363061};
KW Oxidoreductase {ECO:0000313|EMBL:ABO17092.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001430};
KW Respiratory chain {ECO:0000256|RuleBase:RU000370};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000370};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363061}; Transport {ECO:0000256|RuleBase:RU000370}.
FT TRANSMEM 32..55
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 75..96
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 117..140
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 160..185
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 197..230
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 282..306
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 318..340
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 352..374
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 394..412
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 424..448
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 468..489
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT DOMAIN 14..528
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
SQ SEQUENCE 541 AA; 60118 MW; B463DBF0E7A36E8E CRC64;
MTISIDPQKT NNESLQPKGW LRYFSFSLDH KVIGIQYLVC GFLFYLIGGS LASAIRIELA
SPMSDFMPRD VYNQVLTLHG TIMIFLWIVP VVNGAFGNYL IPFYVGARDM AFPRLNAVAF
WLIPPSGLML VASYFVEGAA QAGWTAYPPL SITTPQSGQI IWILSVLLLG GSSIFGGINF
IATIIKLRRP GLKLMQLPMY CWAMLGTSLL VVLSTPVLAG TLILLSFDII ANTGFFNPVL
GGNVVVYQHL FWFYSHPAVY IMVLPAFGLV SEILPVHARK PLFGYTTMVF SIMGIVVLGL
VVWAHHMFTS GTPPWMRLFF TIATAFIAVP TGIKFFNWVA TLWGGKISIN SAMLFSCGFI
INFVFGGITG VALAQVPFDI HVHDTYFVVA HFHYIVYGGT VFIIFSSIYH WFPKVTGKML
NEKLGILHFI ITFIGFNLCF APQHWLGLNG MPRRVAEYDP QFQFVNQISS LGALLMAIST
IPFLINVFLS VRNGKDAGDN PWNALTPEWL TSSPPPVENW EGEAPLVEEP YGYGKEISEL
K
//