ID B2SX27_PARPJ Unreviewed; 537 AA. AC B2SX27; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 12-AUG-2020, entry version 90. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061}; DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU363061}; GN OrderedLocusNames=Bphyt_0545 {ECO:0000313|EMBL:ACD14970.1}; OS Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN) OS (Burkholderia phytofirmans). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=398527 {ECO:0000313|EMBL:ACD14970.1, ECO:0000313|Proteomes:UP000001739}; RN [1] {ECO:0000313|EMBL:ACD14970.1, ECO:0000313|Proteomes:UP000001739} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17436 / LMG 22146 / PsJN RC {ECO:0000313|Proteomes:UP000001739}; RX PubMed=21551308; DOI=10.1128/JB.05055-11; RA Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.; RT "Complete genome sequence of the plant growth-promoting endophyte RT Burkholderia phytofirmans strain PsJN."; RL J. Bacteriol. 193:3383-3384(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 {ECO:0000256|RuleBase:RU363061}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c] CC + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA- CC COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=7.1.1.9; CC Evidence={ECO:0000256|ARBA:ARBA00000342, 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:RU363061}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001052; ACD14970.1; -; Genomic_DNA. DR RefSeq; WP_012431609.1; NC_010681.1. DR STRING; 398527.Bphyt_0545; -. DR EnsemblBacteria; ACD14970; ACD14970; Bphyt_0545. DR KEGG; bpy:Bphyt_0545; -. DR eggNOG; COG0843; Bacteria. DR HOGENOM; CLU_011899_7_3_4; -. DR KO; K02274; -. DR OMA; PVDFQYH; -. DR OrthoDB; 316745at2; -. DR BioCyc; BPHY398527:GJEX-522-MONOMER; -. DR UniPathway; UPA00705; -. DR Proteomes; UP000001739; Chromosome 1. 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:0045277; C:respiratory chain complex IV; IEA:InterPro. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro. 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; IEA:InterPro. DR GO; GO:0015990; P:electron transport coupled proton transport; IEA:InterPro. DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. 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 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 3: Inferred from homology; KW Cell membrane {ECO:0000256|RuleBase:RU363061}; KW Copper {ECO:0000256|RuleBase:RU363061}; KW Electron transport {ECO:0000256|RuleBase:RU363061}; KW Heme {ECO:0000256|RuleBase:RU363061}; 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:ACD14970.1}; KW Respiratory chain {ECO:0000256|RuleBase:RU363061}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU363061}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU363061}; Transport {ECO:0000256|RuleBase:RU363061}. FT TRANSMEM 42..63 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363061" FT TRANSMEM 83..104 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363061" FT TRANSMEM 125..154 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363061" FT TRANSMEM 166..192 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363061" FT TRANSMEM 204..232 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363061" FT TRANSMEM 264..282 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363061" FT TRANSMEM 294..313 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363061" FT TRANSMEM 325..345 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363061" FT TRANSMEM 357..379 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363061" FT TRANSMEM 391..416 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363061" FT TRANSMEM 432..453 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363061" FT TRANSMEM 473..497 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363061" FT DOMAIN 21..537 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" SQ SEQUENCE 537 AA; 59677 MW; 7D899A81FBF2BE8D CRC64; MSSIGHDVVA GHEHVHGDHA HETPHGWRRW LFATNHKDIG TLYLIFSFTM FLSGGVMALM IRAELFEPGL QIMRPEFFNQ LTTMHGLIMV FGAIMPAFVG FANWMVPLQI GASDMAFARM NNFSFWLLPV AAVLLVGSFF SPGGATAAGW TLYAPLSTQM GPGMDFAIFA IHLMGASSIM GGINIVVTIL NMRAPGLTLM KMPMFVWTWL ITAYLLIAVM PVLAGAITMV LFDRHFGTSF FNAAGGGDPV MYQHIFWFFG HPEVYIMILP AFGIVSQVIP AFSRKPLFGY SSMVYATSSI AILSFMVWAH HMFATGMPVT GQLFFMYATM LIAVPTGVKV FNWVATMWRG SLSFETPMLF AVGFLLVFTF GGLSGLMLAM APLDIQYHGT YFVVAHFHYV LVAGSLFALF SGWYYWAPKW TGWMYNETRG KIHFWASMFF FNLAFLPMHF VGLAGMPRRY ADYPAQFTDW NQVISIGAFG FGLAQVYFLF AVALPAYRGG GELEKAGDKP WDGATGLEWT VPSPAPFHTF ENPPTVE //