ID Q72H23_THET2 Unreviewed; 337 AA.
AC Q72H23;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 29-MAY-2013, entry version 75.
DE RecName: Full=Cytochrome c oxidase subunit 2;
DE EC=1.9.3.1;
GN OrderedLocusNames=TT_C1672;
OS Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HB27 / ATCC BAA-163 / DSM 7039;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T.,
RA Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R.,
RA Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R.,
RA Klenk H.-P., Overbeek R., Kramer W., Merkl R., Gottschalk G.,
RA Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus
RT thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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; AE017221; AAS82014.1; -; Genomic_DNA.
DR RefSeq; YP_005641.1; NC_005835.1.
DR ProteinModelPortal; Q72H23; -.
DR EnsemblBacteria; AAS82014; AAS82014; TT_C1672.
DR GeneID; 2776061; -.
DR KEGG; tth:TTC1672; -.
DR PATRIC; 23953797; VBITheThe54392_1669.
DR eggNOG; COG2857; -.
DR KO; K02275; -.
DR OMA; FYGKCAE; -.
DR ProtClustDB; CLSK738613; -.
DR BioCyc; TTHE262724:GCAT-1705-MONOMER; -.
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:0005506; F:iron ion 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; IPR003088; Cyt_c_I.
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 Pfam; PF00034; Cytochrom_C; 1.
DR SUPFAM; SSF49503; Cupredoxin; 1.
DR SUPFAM; SSF81464; Cyt_c_oxidase_II-like_TM; 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; 1.
PE 3: Inferred from homology;
KW Complete proteome; Copper; Electron transport; Membrane;
KW Metal-binding; Oxidoreductase; Respiratory chain; Transmembrane;
KW Transport.
SQ SEQUENCE 337 AA; 37271 MW; E527F9588FF8BF60 CRC64;
MQRSFAALGL WGLSLAQEAH RVAITHPGGS FNQEVAFLFP WVYFFSFLIF LVVAGSLAYV
TWKFRARPED QEEPPQIHGN DRLEVVWTLI PLAIVLVLFG LTAKALIQVN RPIPGALKVE
VTGYQFWWDF HYPELGLRNS NELVLPAGVP VELEITSKDV IHSFWVPGLS GKRDAIPGQT
TRISFEPKEP GLYYGFCAEL CGASHARMLF RVVVLPKEEF DRFVEQAKAS PAPVADERGQ
QVFQQNCAAC HGVARSMPPA VIGPELGLLG NRTSLGAGIV ENTPENLKAW IRDPAGMKPG
VKMPGFPQLS EEDLDALARY LEGLKVEGFD FGALPKF
//
