(data stored in ACNUC7421 zone)

SWISSPROT: A8FPN7_SHESH

ID   A8FPN7_SHESH            Unreviewed;       534 AA.
AC   A8FPN7;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   05-JUL-2017, entry version 77.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061};
DE            EC=1.9.3.1 {ECO:0000256|RuleBase:RU363061};
GN   OrderedLocusNames=Ssed_0197 {ECO:0000313|EMBL:ABV34810.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34810.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34810.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34810.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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; CP000821; ABV34810.1; -; Genomic_DNA.
DR   RefSeq; WP_012004336.1; NC_009831.1.
DR   ProteinModelPortal; A8FPN7; -.
DR   STRING; 425104.Ssed_0197; -.
DR   EnsemblBacteria; ABV34810; ABV34810; Ssed_0197.
DR   KEGG; sse:Ssed_0197; -.
DR   eggNOG; ENOG4105BZ9; Bacteria.
DR   eggNOG; COG0843; LUCA.
DR   HOGENOM; HOG000085274; -.
DR   KO; K02274; -.
DR   OMA; SFAMVIR; -.
DR   OrthoDB; POG091H042R; -.
DR   BioCyc; SSED425104:GH7Q-200-MONOMER; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000002015; 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; A8FPN7.
DR   SWISS-2DPAGE; A8FPN7.
KW   Cell membrane {ECO:0000256|RuleBase:RU363061};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
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:ABV34810.1};
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     42     63       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM     83    105       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    125    145       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    165    191       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    203    225       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    265    283       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    295    313       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    325    346       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    358    381       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    393    418       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    430    454       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   TRANSMEM    474    494       Helical. {ECO:0000256|RuleBase:RU363061}.
FT   DOMAIN       30    534       COX1. {ECO:0000259|PROSITE:PS50855}.
SQ   SEQUENCE   534 AA;  59685 MW;  894B75AB5121FBC6 CRC64;
     MSTITQDSPA AQDDHHDDHH HGAPKGIMRW LLTTNHKDIG TLYLWFSFIM FLTGGAMAMV
     IRAELFQPGL QLVEPNFFNQ MTTVHGLIMV FGAVMPAFTG LANWLIPMMI GAPDMALPRM
     NNWSFWILPF AFAILLSSLF MEGGGPNFGW TFYAPLSTTY SPDSTALFVF SVHIMGMSSI
     MGAINVIVTI VNMRAPGMRW MKLPLFVWTW LITAFLLIAV MPVLAGTVTM VLTDKYFGTS
     FFDAAGGGDP VMFQHIFWFF GHPEVYIMIL PSFGIISAIV PAFSRKRLFG YSSMVYATAS
     IAILSFLVWA HHMFTTGMPV FAELFFMYCT MLIAVPTGVK VFNWVATMWR GSISFETPML
     FAVAFIILFT IGGFSGLMLA ITPVDFQYHD TYFVVAHFHY VLVTGAIFSI MAGAYYWLPK
     WTGNMYDEKL GRLHFWCSVI SVNVLFFPMH FLGLAGMPRR IPDYAVQFAD VNQIVSIGGF
     AFGLSQLIFL AVVIKCIRGG EKAPAKPWDG AEGLEWTLPS PAPYHTFSTP PEIK
//

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