(data stored in ACNUC7421 zone)

SWISSPROT: Q146B0_PARXL

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}.
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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
//

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