(data stored in ACNUC7421 zone)

SWISSPROT: C3MHJ1_SINFN

ID   C3MHJ1_SINFN            Unreviewed;       294 AA.
AC   C3MHJ1;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 58.
DE   RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU004024};
DE            EC=1.9.3.1 {ECO:0000256|RuleBase:RU004024};
GN   Name=ctaC {ECO:0000313|EMBL:ACP24319.1};
GN   OrderedLocusNames=NGR_c05230 {ECO:0000313|EMBL:ACP24319.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24319.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24319.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP24319.1; -; Genomic_DNA.
DR   RefSeq; WP_012707104.1; NC_012587.1.
DR   RefSeq; YP_002825072.1; NC_012587.1.
DR   STRING; 394.NGR_c05230; -.
DR   EnsemblBacteria; ACP24319; ACP24319; NGR_c05230.
DR   GeneID; 7791749; -.
DR   KEGG; rhi:NGR_c05230; -.
DR   PATRIC; fig|394.7.peg.3336; -.
DR   eggNOG; ENOG4105CV4; Bacteria.
DR   eggNOG; COG1622; LUCA.
DR   HOGENOM; HOG000264988; -.
DR   KO; K02275; -.
DR   OMA; HAFMPIA; -.
DR   OrthoDB; POG091H05L4; -.
DR   Proteomes; UP000001054; Chromosome.
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; C3MHJ1.
DR   SWISS-2DPAGE; C3MHJ1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
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:ACP24319.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
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     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    294       Cytochrome c oxidase subunit 2.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002927883.
FT   TRANSMEM     50     71       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     92    113       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       25    120       COX2_TM. {ECO:0000259|PROSITE:PS50999}.
FT   DOMAIN      122    263       COX2_CUA. {ECO:0000259|PROSITE:PS50857}.
SQ   SEQUENCE   294 AA;  32163 MW;  DE303785946E7898 CRC64;
     MKNKAYAVLA ALACLLFASS AFADKPVDWQ TRFQAAATGI MEEITWFEQY TLWFIIPITL
     LVLLLLIIVV VKFREGANPV PSRTSHNTAI EVIWTVGPVI ILLFLAIPSF KLLNAQLTPP
     QNPDLTVKAT GNQWYWSYEY EVGENPLSFD SLLLKDEDRA SAGKEDKAAY PRLLAVDNEV
     VVPVGKTVRL LVTAADVIHA FAMPAFGVKI DAVPGRLNET WFKAAREGLY YGQCSELCGK
     DHAYMPIAVR VVSQEKYDAW LAAAATNLGE ANKALMASID GAAKTVDVAA NAAQ
//

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