(data stored in SCRATCH zone)

SWISSPROT: A8FPN8_SHESH

ID   A8FPN8_SHESH            Unreviewed;       524 AA.
AC   A8FPN8;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 79.
DE   RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU004024};
DE            EC=1.9.3.1 {ECO:0000256|RuleBase:RU004024};
GN   OrderedLocusNames=Ssed_0198 {ECO:0000313|EMBL:ABV34811.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34811.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34811.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34811.1,
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: 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; CP000821; ABV34811.1; -; Genomic_DNA.
DR   RefSeq; WP_012004337.1; NC_009831.1.
DR   ProteinModelPortal; A8FPN8; -.
DR   STRING; 425104.Ssed_0198; -.
DR   EnsemblBacteria; ABV34811; ABV34811; Ssed_0198.
DR   KEGG; sse:Ssed_0198; -.
DR   eggNOG; ENOG4105CV4; Bacteria.
DR   eggNOG; COG1622; LUCA.
DR   eggNOG; COG2010; LUCA.
DR   HOGENOM; HOG000264987; -.
DR   KO; K02275; -.
DR   OMA; HAFMPIA; -.
DR   OrthoDB; POG091H05L4; -.
DR   BioCyc; SSED425104:GH7Q-201-MONOMER; -.
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: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:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   CDD; cd13912; CcO_II_C; 1.
DR   Gene3D; 1.10.760.10; -; 2.
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; IPR009056; Cyt_c-like_dom.
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   Pfam; PF13442; Cytochrome_CBB3; 2.
DR   SUPFAM; SSF46626; SSF46626; 2.
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.
DR   PROSITE; PS51007; CYTC; 2.
PE   3: Inferred from homology;
DR   PRODOM; A8FPN8.
DR   SWISS-2DPAGE; A8FPN8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Copper {ECO:0000256|RuleBase:RU004024};
KW   Electron transport {ECO:0000256|RuleBase:RU000456};
KW   Heme {ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00433,
KW   ECO:0000256|RuleBase:RU004024};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000456,
KW   ECO:0000313|EMBL:ABV34811.1};
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     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    524       Cytochrome c oxidase subunit 2.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002719907.
FT   TRANSMEM     43     64       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     85    103       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       18    113       COX2_TM. {ECO:0000259|PROSITE:PS50999}.
FT   DOMAIN      114    251       COX2_CUA. {ECO:0000259|PROSITE:PS50857}.
FT   DOMAIN      275    355       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51007}.
FT   DOMAIN      426    506       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51007}.
SQ   SEQUENCE   524 AA;  56132 MW;  107FF970DC826D56 CRC64;
     MKQKLYGLPA LLFSPSILAA DMPLNMTQGV TEISGRVYNL HMIILYICCA IGILVFGVMI
     YSMINHRKSR GAVAANFHES TKVEIAWTLV PFIILVLMAI PATKTLIAME DPSDADLTIK
     ITGSQWKWHY SYFDHDLEFY SLLSTPREQI EGTEVKGENY LLEVDKPLVL PVNKKVRFLM
     TSDDVIHSWW VPAFAVKKDA NPGFINEAWT RIDKPGVYRG QCAELCGKDH GFMPIVVEAL
     SEVDFDKWVI AQKQQANNAE AEAKAALSKT LSMEELMAKG EQIYLARCAA CHQPNGAGLP
     GVFPSLIGSP ITIGPVAAHV DIVVNGKPGT AMQAFAKQLN ATEIAAVVTF ERNAWGNDSG
     DTVQAADVSS GGSSSAASND SSTAIPATLP ASQPETEQVK TAVAETASKV VEEVEAVVLD
     DLTMDELMAV GEKVYMTHCV ACHQAAGTGL PGAFPSLVGS PVITGPISGH LDVVINGKPG
     TAMQSFSSLL TPQQLAAVVT YERNAWGNNS GDTVQASDVV GHGN
//

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