ID Q0HDL3_SHESM Unreviewed; 513 AA.
AC Q0HDL3;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 01-MAY-2013, entry version 62.
DE RecName: Full=Cytochrome c oxidase subunit 2;
DE EC=1.9.3.1;
GN OrderedLocusNames=Shewmr4_3791;
OS Shewanella sp. (strain MR-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60480;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J.,
RA Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella sp. MR-4.";
RL Submitted (AUG-2006) 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) (By similarity).
CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4
CC ferricytochrome c + 2 H(2)O.
CC -!- COFACTOR: Copper A (By similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC similarity).
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
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DR EMBL; CP000446; ABI40854.1; -; Genomic_DNA.
DR RefSeq; YP_735911.1; NC_008321.1.
DR ProteinModelPortal; Q0HDL3; -.
DR STRING; 60480.Shewmr4_3791; -.
DR EnsemblBacteria; ABI40854; ABI40854; Shewmr4_3791.
DR GeneID; 4254354; -.
DR KEGG; she:Shewmr4_3791; -.
DR PATRIC; 23584467; VBISheSp133532_3930.
DR eggNOG; COG2010; -.
DR HOGENOM; HOG000264987; -.
DR KO; K02275; -.
DR OMA; WGNNTGD; -.
DR ProtClustDB; CLSK907729; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
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:EC.
DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR009056; Cyt_c_dom.
DR InterPro; IPR014222; Cyt_c_oxidase_su2.
DR InterPro; IPR002429; Cyt_c_oxidase_su2_C.
DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF02790; COX2_TM; 1.
DR SUPFAM; SSF49503; Cupredoxin; 1.
DR SUPFAM; SSF81464; Cyt_c_oxidase_II-like_TM; 1.
DR SUPFAM; SSF46626; Cytochrome_c; 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;
KW Complete proteome; Copper; Electron transport; Metal-binding;
KW Oxidoreductase; Respiratory chain; Transmembrane; Transport.
SQ SEQUENCE 513 AA; 55262 MW; 9EDF016A69620682 CRC64;
MKQWLYCLLV VLFAPPLPAA DMRFNMTPGV TEISGKVYHL HMTILYICCA IGLVVFGVMI
YAMINHRKSK GAVASHFHES TKVEIAWTII PFVILILMAI PATKTLIAME DPSNADLTVK
VTGSQWKWHY SYFDQDIDFY SILATPRPQI EGSEAKGEHY LLEVDKPLVL PINRKIRFLM
TSEDVIHSWW MPAFAVKKDA NPGFINEAWT RIDKPGIYRG QCAELCGKDH GFMPIVVQAL
PEAEFDAWVE EQKQAANAAA QAAQAALSQT LTKEELMAQG EQVYLGHCAA CHQPNGEGLQ
GVFPHLKGSP IATGPLSGHL EIVLNGKAGT AMQAFGKQLT AQEIAAVVTY ERNAWGNNTG
DAVQAKDVDA HKSGGTNSEP VATTPPPATT DAPKPATEPA ASVDPASLPT LSHDELMAEG
EKTYATICAA CHQLTGAGMP PAFPALAGSA IATGPVANHI DIVMHGKPGT AMQAFGTQLT
PQQLAAIITY ERNAWGNNTG DTVQPADIAR HGQ
//
