(data stored in ACNUC7421 zone)

SWISSPROT: D4YYS2_SPHJU

ID   D4YYS2_SPHJU            Unreviewed;       555 AA.
AC   D4YYS2;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   05-JUL-2017, entry version 53.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061};
DE            EC=1.9.3.1 {ECO:0000256|RuleBase:RU363061};
GN   Name=coxA {ECO:0000313|EMBL:BAI95504.1};
GN   OrderedLocusNames=SJA_C1-06700 {ECO:0000313|EMBL:BAI95504.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95504.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95504.1, 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: 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; AP010803; BAI95504.1; -; Genomic_DNA.
DR   RefSeq; WP_013039197.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-06700; -.
DR   EnsemblBacteria; BAI95504; BAI95504; SJA_C1-06700.
DR   GeneID; 29272343; -.
DR   KEGG; sjp:SJA_C1-06700; -.
DR   eggNOG; ENOG4105BZ9; Bacteria.
DR   eggNOG; COG0843; LUCA.
DR   HOGENOM; HOG000085275; -.
DR   KO; K02274; -.
DR   OMA; SFAMVIR; -.
DR   OrthoDB; POG091H042R; -.
DR   UniPathway; UPA00705; -.
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: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; D4YYS2.
DR   SWISS-2DPAGE; D4YYS2.
KW   Cell membrane {ECO:0000256|RuleBase:RU363061};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
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:BAI95504.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
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     38     60       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    102    127       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    139    157       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    188    213       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    225    252       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    272    296       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    308    332       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    344    367       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    379    400       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    420    438       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    450    474       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    494    515       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   DOMAIN       29    555       COX1. {ECO:0000259|PROSITE:PS50855}.
SQ   SEQUENCE   555 AA;  61047 MW;  F1AC88A65FECA28B CRC64;
     MTTITADHHG DHAHDHHDAD HKPAFFQRWF MSTNHKDIGT LYLIFAIVAG IIGGAISGLM
     RAELAQPGIQ YLQTWAQFSD GPEATLDQAY HLWNVLITAH GLIMVFFMVM PAMIGGFGNW
     FVPIMIGAPD MAFPRMNNIS FWLLIPAFVL LLGSTFVPGG TGNGAGTGWT VYAPLSTSGS
     AGPAVDMAIL SLHVAGVSSI LGAINFITTI LNMRAPGMTL HKMPLFVWSV LVTAFLLLLA
     LPVLAAAITM LLTDRNFGTT FYDAAGGGDP ELYQHLFWFF GHPEVYIMIL PGFGIISQIV
     STFSRKPVFG YLGMAYAMVA IGVVGFVVWA HHMFTTGMSV NVKMYFTAAT MVIAVPTGIK
     IFSWIATIWG GSISYKTPMV WALGFIFLFT VGGVTGVVLA NGGVDDVLHD TYYVVAHFHY
     VLSLGAVFGL FAGFYYWFPK MSGRMYNEFL GHLHFWVFFV GVNMLFFPMH FLGLSGMPRR
     YPDYPEAFAY WNKFASHGYE IMAAGMLIFF VNLIWSLAAG KKAEGNPWGE GATTLEWTLS
     SPPPFHQFET LPVID
//

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