(data stored in SCRATCH zone)

SWISSPROT: B8I9Q2_METNO

ID   B8I9Q2_METNO            Unreviewed;       542 AA.
AC   B8I9Q2;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   05-JUL-2017, entry version 63.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061};
DE            EC=1.9.3.1 {ECO:0000256|RuleBase:RU363061};
GN   OrderedLocusNames=Mnod_0261 {ECO:0000313|EMBL:ACL55305.1};
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:ACL55305.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55305.1, 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: Cytochrome c oxidase is the component of the respiratory
CC       chain that catalyzes the reduction of oxygen to water. Subunits 1-
CC       3 form the functional core of the enzyme complex. CO I is the
CC       catalytic subunit of the enzyme. Electrons originating in
CC       cytochrome c are transferred via the copper A center of subunit 2
CC       and heme A of subunit 1 to the bimetallic center formed by heme A3
CC       and copper B. {ECO:0000256|RuleBase:RU363061}.
CC   -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4
CC       ferricytochrome c + 2 H(2)O. {ECO:0000256|RuleBase:RU363061}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000256|RuleBase:RU363061}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000256|RuleBase:RU363061}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU363061}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000256|RuleBase:RU363061}.
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DR   EMBL; CP001349; ACL55305.1; -; Genomic_DNA.
DR   RefSeq; WP_015927018.1; NC_011894.1.
DR   ProteinModelPortal; B8I9Q2; -.
DR   STRING; 460265.Mnod_0261; -.
DR   EnsemblBacteria; ACL55305; ACL55305; Mnod_0261.
DR   KEGG; mno:Mnod_0261; -.
DR   eggNOG; ENOG4105BZ9; Bacteria.
DR   eggNOG; COG0843; LUCA.
DR   HOGENOM; HOG000085274; -.
DR   KO; K02274; -.
DR   OMA; FTVGMGP; -.
DR   OrthoDB; POG091H042R; -.
DR   UniPathway; UPA00705; -.
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:0045277; C:respiratory chain complex IV; IEA:InterPro.
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   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0009060; P:aerobic respiration; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd01663; Cyt_c_Oxidase_I; 1.
DR   Gene3D; 1.20.210.10; -; 1.
DR   InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR   InterPro; IPR000883; Cyt_C_Oxase_1.
DR   InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR   InterPro; IPR033944; Cyt_c_oxase_su1_dom.
DR   InterPro; IPR014241; Cyt_c_oxidase_su1_bac.
DR   PANTHER; PTHR10422; PTHR10422; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; SSF81442; 1.
DR   TIGRFAMs; TIGR02891; CtaD_CoxA; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
PE   3: Inferred from homology;
DR   PRODOM; B8I9Q2.
DR   SWISS-2DPAGE; B8I9Q2.
KW   Cell membrane {ECO:0000256|RuleBase:RU363061};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
KW   Copper {ECO:0000256|RuleBase:RU363061};
KW   Electron transport {ECO:0000256|RuleBase:RU363061};
KW   Heme {ECO:0000256|RuleBase:RU363061};
KW   Iron {ECO:0000256|RuleBase:RU363061};
KW   Membrane {ECO:0000256|RuleBase:RU363061};
KW   Metal-binding {ECO:0000256|RuleBase:RU363061};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU363061,
KW   ECO:0000313|EMBL:ACL55305.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207};
KW   Respiratory chain {ECO:0000256|RuleBase:RU363061};
KW   Transmembrane {ECO:0000256|RuleBase:RU363061};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU363061};
KW   Transport {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM     35     54       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM     74     97       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    118    136       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    167    193       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    205    232       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    252    276       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    288    312       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    324    346       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    358    380       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    400    418       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    430    451       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    471    497       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   DOMAIN       23    535       COX1. {ECO:0000259|PROSITE:PS50855}.
SQ   SEQUENCE   542 AA;  59515 MW;  4E91289AC135E9B7 CRC64;
     MATAASAGHA EAHDHTPPFF QRWFNSTNHK DIGTLYLLFA FSAGIVGAFL SFGIRMEMEQ
     PGLQYFSNPQ TYNVFVTGHG LIMVFFMVMP ALIGGFGNWF VPLMIGAPDM AFPRMNNISF
     WLTVAGFLSL VCSLFVEGAP GATGPGTGWT VYPPLSTDGH PGPAVDFGIF ALHLSGAGSI
     LGAINFITTI LNMRAPGMTL HKMPLFAWSM LVTAFLLLLS LPVLAGAITM LLTDRNFGTT
     FFSPSGGGDP ILYQHLFWFF GHPEVYIMIL PAFGIVSHII STFSRKPIFG YLAMAYAMVA
     IGVVGFVVWA HHMYTVGLTL QTQSYFVFAT MVIAVPTGVK IFSWIATMWG GSIRFTAAMH
     WAVGFVFLFT VGGVTGVILA NAAVDRYLHD TYYVVAHFHY VLSLGAVFII FAGVYYWFPK
     MTGRMIPEWA GKLHFWLAFI GANVLFFPMH FLGLAGMPRR YADYPDAFAG WHYVATMGGH
     VFALGMVVFV IGVVLAFRSK ERAADNPWGE GATTLEWTLS SPPPFHQYET LPVIVDEPSH
     AH
//

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