(data stored in ACNUC7421 zone)

HOGENOM: ACIAC_1_PE3832

ID   ACIAC_1_PE3832                       STANDARD;      PRT;   390 AA.
AC   ACIAC_1_PE3832; A1TU12;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Cytochrome c oxidase subunit 2; EC=1.9.3 1;Flags:
DE   Precursor; (ACIAC_1.PE3832).
GN   OrderedLocusNames=Aave_3907;
OS   ACIDOVORAX CITRULLI AAC00-1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=397945;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIAC_1.PE3832.
CC       Acidovorax avenae subsp. citrulli AAC00-1, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:A1TU12_ACIAC
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.
CC   -!- GENE_FAMILY: HOG000264987 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A1TU12; -.
DR   EMBL; CP000512; ABM34450.1; -; Genomic_DNA.
DR   RefSeq; YP_972224.1; NC_008752.1.
DR   ProteinModelPortal; A1TU12; -.
DR   STRING; A1TU12; -.
DR   GeneID; 4668296; -.
DR   GenomeReviews; CP000512_GR; Aave_3907.
DR   KEGG; aav:Aave_3907; -.
DR   NMPDR; fig|397945.5.peg.3338; -.
DR   eggNOG; COG1622; -.
DR   OMA; WGNNTGD; -.
DR   PhylomeDB; A1TU12; -.
DR   ProtClustDB; CLSK951273; -.
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:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
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; IPR015964; Cyt_c_oxidase_su2-like_TM_dom.
DR   InterPro; IPR002429; Cyt_c_oxidase_su2_C.
DR   InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR   Gene3D; G3DSA:1.10.287.90; COX2_TM; 1.
DR   Gene3D; G3DSA:2.60.40.420; Cupredoxin; 2.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   Pfam; PF00116; COX2; 1.
DR   Pfam; PF02790; COX2_TM; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR01166; CYCOXIDASEII.
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.
DR   HOGENOMDNA; ACIAC_1.PE3832; -.
KW   cytochrome c oxidase, subunit II;
KW   Complete proteome; Copper; Electron transport; Metal-binding;
KW   Oxidoreductase; Respiratory chain; Signal; Transmembrane; Transport.
SQ   SEQUENCE   390 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKKSISNPLP SLLLLCGAWV GGAAQAVQDL PGGPAVRQLN LAPPVTRIAE EQHFLHWMML
     VICTLIFVGV FSVMFYSIWK HRKSQGAKPA NFHESVTVEV IWTIVPFIIV ILMALPATKV
     LVAQKDTTNA DLTVKVTGYQ WKWGYDYING EGQGLAYIST LDNSHRRLSD SGRVADAPPD
     YLLKVDNPLV VPVGKKVRVI TTANDVIHSF MVPAFGIKQD AIPGFVRDTW FRADKVGDYY
     GQCAELCGKE HAYMPIHVKV LSAADYTQWV AAEKKKAAAK ADDPNKVWTL TDIVARGEKV
     YAANCAACHQ PNGKGAGPIK PLDGSAIVKD EDHTRQIQIV LKGAAGGAMP SWAQLSDTDL
     AAVVSYTKNA WSNKTGQIVQ PAEIVAQRGK
//

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