(data stored in ACNUC7421 zone)

SWISSPROT: B8I9Q1_METNO

ID   B8I9Q1_METNO            Unreviewed;       288 AA.
AC   B8I9Q1;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 60.
DE   RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU004024};
DE            EC=1.9.3.1 {ECO:0000256|RuleBase:RU004024};
GN   OrderedLocusNames=Mnod_0260 {ECO:0000313|EMBL:ACL55304.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55304.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55304.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001349; ACL55304.1; -; Genomic_DNA.
DR   RefSeq; WP_015927017.1; NC_011894.1.
DR   ProteinModelPortal; B8I9Q1; -.
DR   STRING; 460265.Mnod_0260; -.
DR   EnsemblBacteria; ACL55304; ACL55304; Mnod_0260.
DR   KEGG; mno:Mnod_0260; -.
DR   eggNOG; ENOG4105CV4; Bacteria.
DR   eggNOG; COG1622; LUCA.
DR   HOGENOM; HOG000264988; -.
DR   KO; K02275; -.
DR   OMA; HAFMPIA; -.
DR   OrthoDB; POG091H05L4; -.
DR   Proteomes; UP000008207; 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; B8I9Q1.
DR   SWISS-2DPAGE; B8I9Q1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
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:ACL55304.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207};
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     33       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        34    288       Cytochrome c oxidase subunit 2.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002873870.
FT   TRANSMEM     57     84       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    105    123       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       38    133       COX2_TM. {ECO:0000259|PROSITE:PS50999}.
FT   DOMAIN      134    269       COX2_CUA. {ECO:0000259|PROSITE:PS50857}.
SQ   SEQUENCE   288 AA;  32029 MW;  FE42F348D02F4DE9 CRC64;
     MGMARAQHRR FGRSFVGGAA IAAALLTGTA AFAAGTGQPE PWQMDLQKPV TEVATEIYNF
     HHLLNVIMVG IVLLVLVLLL LVIFRFNERS QPNPSRTTHN TILEVAWTVV PVLILVAIAI
     PSFRVLRTQL SDPKADLMVK VIGHAWYWSY EYPQEVGGFK FDANLLEGED QEKSGQPKLL
     ATDNEMVVPV NKIVKIQVTA ADVMHSWAMP SFGFKIDAIP GRLNQFWFKA EREGTYHGQC
     SELCGQRHAY MPITVRVVSD EAFQAWTAEA KTKFARIDTS GAKFASAR
//

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