Back to PBIL home page
ID Q146B0_PARXL Unreviewed; 538 AA.
AC Q146B0;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 08-MAY-2019, entry version 106.
DE RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU004024};
DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU004024};
GN ORFNames=Bxe_A4171 {ECO:0000313|EMBL:ABE28829.1};
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28829.1, ECO:0000313|Proteomes:UP000001817};
RN [1] {ECO:0000313|EMBL:ABE28829.1, ECO:0000313|Proteomes:UP000001817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400 {ECO:0000313|EMBL:ABE28829.1,
RC ECO:0000313|Proteomes:UP000001817};
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT genome shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC -!- FUNCTION: Subunits I and II form the functional core of the enzyme
CC complex. Electrons originating in cytochrome c are transferred via
CC heme a and Cu(A) to the binuclear center formed by heme a3 and
CC Cu(B). {ECO:0000256|RuleBase:RU004024}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4
CC [Fe(III)cytochrome c] + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-
CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=1.9.3.1;
CC Evidence={ECO:0000256|RuleBase:RU004024};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|RuleBase:RU004024};
CC Note=Binds a copper A center. {ECO:0000256|RuleBase:RU004024};
CC -!- SUBCELLULAR LOCATION: Cell membrane
CC {ECO:0000256|RuleBase:RU000456}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU000456}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000256|RuleBase:RU000456}.
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; CP000270; ABE28829.1; -; Genomic_DNA.
DR RefSeq; WP_011486666.1; NZ_CP008760.1.
DR STRING; 266265.Bxe_A4171; -.
DR EnsemblBacteria; ABE28829; ABE28829; Bxe_A4171.
DR GeneID; 4001867; -.
DR KEGG; bxe:Bxe_A4171; -.
DR PATRIC; fig|266265.5.peg.308; -.
DR eggNOG; ENOG4105CV4; Bacteria.
DR eggNOG; COG1622; LUCA.
DR eggNOG; COG2010; LUCA.
DR HOGENOM; HOG000264987; -.
DR KO; K02275; -.
DR OMA; HAFMPIA; -.
DR OrthoDB; 1654242at2; -.
DR BioCyc; BXEN266265:BXE_RS01445-MONOMER; -.
DR Proteomes; UP000001817; Chromosome 1.
DR GO; GO:0009279; C:cell outer membrane; IEA:InterPro.
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:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR CDD; cd07185; OmpA_C-like; 1.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 1.10.760.10; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR Gene3D; 3.30.1330.60; -; 1.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR014222; Cyt_c_oxidase_su2.
DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR InterPro; IPR006664; OMP_bac.
DR InterPro; IPR006665; OmpA-like.
DR InterPro; IPR036737; OmpA-like_sf.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF02790; COX2_TM; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR Pfam; PF00691; OmpA; 1.
DR PRINTS; PR01021; OMPADOMAIN.
DR SUPFAM; SSF103088; SSF103088; 1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81464; SSF81464; 1.
DR TIGRFAMs; TIGR02866; CoxB; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS50999; COX2_TM; 1.
DR PROSITE; PS51007; CYTC; 1.
DR PROSITE; PS51123; OMPA_2; 1.
PE 3: Inferred from homology;
DR PRODOM; Q146B0.
DR SWISS-2DPAGE; Q146B0.
KW Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW Copper {ECO:0000256|RuleBase:RU004024};
KW Electron transport {ECO:0000256|RuleBase:RU000456};
KW Heme {ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|PROSITE-ProRule:PRU00433};
KW Membrane {ECO:0000256|PROSITE-ProRule:PRU00473,
KW ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00433,
KW ECO:0000256|RuleBase:RU004024};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000456,
KW ECO:0000313|EMBL:ABE28829.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW Respiratory chain {ECO:0000256|RuleBase:RU000456};
KW Transmembrane {ECO:0000256|RuleBase:RU000456,
KW ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|RuleBase:RU000456}.
FT TRANSMEM 59 86 Helical. {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 107 125 Helical. {ECO:0000256|SAM:Phobius}.
FT DOMAIN 40 135 COX2_TM. {ECO:0000259|PROSITE:PS50999}.
FT DOMAIN 136 276 COX2_CUA. {ECO:0000259|PROSITE:PS50857}.
FT DOMAIN 296 373 Cytochrome c. {ECO:0000259|PROSITE:
FT PS51007}.
FT DOMAIN 429 538 OmpA-like. {ECO:0000259|PROSITE:PS51123}.
SQ SEQUENCE 538 AA; 56825 MW; 5BF6D83505C769CC CRC64;
MEILGKEAMK TIKRALMGVL AMSGLLFAGA ALAVGDVPGG PAVNEINLQP PATKIAEELF
SLHMFMLVLC TVIFVGVFAV MFYSIFAHRK SKGHKASNFH ESTTVEIIWT IVPFIIVVLM
ALPATKTVVA MKDTTNADLT IKVTGYQWKW GYDYVKGPGE GISFLSTLAT PRAETDGRQP
ISTTYLQEVD NPLVVPVDKK IRIITTANDV VHSWYVPAFG VKQDAIPGFV RDTWFKAEKV
GTFRGFCTEL CGKEHAFMPV VVEVLSADDY AKWVDAQKKK MAAGQDDPNK TYTMAELMER
GGKVYAANCA VCHQPTGKGA GAFPALDGSK IANGPIAEHV SLVLKGKNAM PSWAPTLNDV
EIASVITYER NSWGNHTGDI LQPKQVADAR NGKLPEGGNH LADAGAAASG AEAASGASGA
ETAAAGSDSA AAQATLPASI YFDTGKSTLP AEAKAAVEAA AAYAKSHPDA KFTLSGFTDA
TGSADLNAKL AKSRAEAVRD ALKAAGIAED HIILKKPETI TGGSDAKEAR RVQISPAA
//
Back to PBIL home page