(data stored in ACNUC7421 zone)

SWISSPROT: D4YYS1_SPHJU

ID   D4YYS1_SPHJU            Unreviewed;       337 AA.
AC   D4YYS1;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 48.
DE   RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU004024};
DE            EC=1.9.3.1 {ECO:0000256|RuleBase:RU004024};
GN   Name=coxB {ECO:0000313|EMBL:BAI95503.1};
GN   OrderedLocusNames=SJA_C1-06690 {ECO:0000313|EMBL:BAI95503.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95503.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95503.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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: 4 ferrocytochrome c + O(2) + 4 H(+) = 4
CC       ferricytochrome c + 2 H(2)O. {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; AP010803; BAI95503.1; -; Genomic_DNA.
DR   RefSeq; WP_007688548.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-06690; -.
DR   EnsemblBacteria; BAI95503; BAI95503; SJA_C1-06690.
DR   GeneID; 29272342; -.
DR   KEGG; sjp:SJA_C1-06690; -.
DR   eggNOG; ENOG4105CV4; Bacteria.
DR   eggNOG; COG1622; LUCA.
DR   HOGENOM; HOG000264988; -.
DR   KO; K02275; -.
DR   OMA; WSYEYTD; -.
DR   OrthoDB; POG091H05L4; -.
DR   Proteomes; UP000007753; 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:0070469; C:respiratory chain; 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:0022900; P:electron transport chain; IEA:InterPro.
DR   CDD; cd13912; CcO_II_C; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR002429; CcO_II-like_C.
DR   InterPro; IPR034210; CcO_II_C.
DR   InterPro; IPR001505; Copper_CuA.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR014222; Cyt_c_oxidase_su2.
DR   InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR   Pfam; PF00116; COX2; 1.
DR   Pfam; PF02790; COX2_TM; 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.
PE   3: Inferred from homology;
DR   PRODOM; D4YYS1.
DR   SWISS-2DPAGE; D4YYS1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Copper {ECO:0000256|RuleBase:RU004024};
KW   Electron transport {ECO:0000256|RuleBase:RU000456};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU004024};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000456,
KW   ECO:0000313|EMBL:BAI95503.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Respiratory chain {ECO:0000256|RuleBase:RU000456};
KW   Signal {ECO:0000256|SAM:SignalP};
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   SIGNAL        1     27       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        28    337       Cytochrome c oxidase subunit 2.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003068304.
FT   TRANSMEM    104    125       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    146    168       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       78    174       COX2_TM. {ECO:0000259|PROSITE:PS50999}.
FT   DOMAIN      176    310       COX2_CUA. {ECO:0000259|PROSITE:PS50857}.
SQ   SEQUENCE   337 AA;  35526 MW;  172631BD137645CD CRC64;
     MNKVKSLVLA GLLAFAPTLA MNGPALAQDN AAVAAPAAGN EAVAADSAGN AAAPAAEAAP
     AAKVAAPPRM KPTPGIGMPM PGEITLQKQF SPTGHTARWL HDVMLLPIIT IISIFVLILM
     LYVMVRFRRS ANPTPSKTSH NTVIEVIWTV VPVVILLAIA VPSIGLLADQ YKPAPKDALT
     VKVTGYQWYW GYEYPDNGIP EFVSNMLPKD KAEANGEPYL LAPDNRLVLP VGRPIKLIIT
     GADVIHSFAV PSLWVKMDAV PGRLNEKSFT IEKPGVYYGQ CSELCGARHG FMPIAIEALE
     PAQFDQWLLS QGGTLKGAAA ATTAEAAAPA AAPAAKL
//

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