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COX2_THETH
ID   COX2_THETH              Reviewed;         135 AA.
AC   P98052;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 2.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Cytochrome c oxidase subunit 2;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome c ba(3) subunit II;
DE   AltName: Full=Cytochrome c oxidase polypeptide II;
DE   AltName: Full=Cytochrome cba3 subunit 2;
DE   Flags: Fragment;
GN   Name=cbaB; Synonyms=ctaC;
OS   Thermus thermophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX   PubMed=10360350; DOI=10.1038/9274;
RA   Williams P.A., Blackburn N.J., Sanders D., Bellamy H., Stura E.A.,
RA   Fee J.A., McRee D.E.;
RT   "The CuA domain of Thermus thermophilus ba3-type cytochrome c oxidase at
RT   1.6-A resolution.";
RL   Nat. Struct. Biol. 6:509-516(1999).
CC   -!- FUNCTION: Subunits I and II form the functional core of the enzyme
CC       complex. Electrons originating in cytochrome c are transferred via heme
CC       a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC         [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC         Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034; EC=7.1.1.9;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: The sequence shown here has been extracted from PDB entry
CC       2CUA. {ECO:0000305}.
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DR   PDB; 1XME; X-ray; 2.30 A; B=1-135.
DR   PDB; 2CUA; X-ray; 1.60 A; A/B=1-135.
DR   PDB; 2FWL; NMR; -; B=1-135.
DR   PDB; 2LLN; NMR; -; A=11-135.
DR   PDB; 5U7N; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-135.
DR   PDBsum; 1XME; -.
DR   PDBsum; 2CUA; -.
DR   PDBsum; 2FWL; -.
DR   PDBsum; 2LLN; -.
DR   PDBsum; 5U7N; -.
DR   AlphaFoldDB; P98052; -.
DR   BMRB; P98052; -.
DR   SMR; P98052; -.
DR   IntAct; P98052; 1.
DR   DrugBank; DB02451; B-nonylglucoside.
DR   EvolutionaryTrace; P98052; -.
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:respirasome; 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   CDD; cd13913; ba3_CcO_II_C; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR034214; Ba3_CcO_II_C.
DR   InterPro; IPR002429; CcO_II-like_C.
DR   InterPro; IPR001505; Copper_CuA.
DR   InterPro; IPR008972; Cupredoxin.
DR   Pfam; PF00116; COX2; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   PROSITE; PS00078; COX2; 1.
DR   PROSITE; PS50857; COX2_CUA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Copper; Electron transport; Membrane;
KW   Metal-binding; Respiratory chain; Translocase; Transmembrane; Transport.
FT   CHAIN           <1..135
FT                   /note="Cytochrome c oxidase subunit 2"
FT                   /id="PRO_0000183721"
FT   BINDING         81
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT   BINDING         116
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT   BINDING         120
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT   BINDING         124
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT   NON_TER         1
FT   HELIX           3..5
FT                   /evidence="ECO:0007829|PDB:2FWL"
FT   HELIX           7..11
FT                   /evidence="ECO:0007829|PDB:2FWL"
FT   STRAND          15..19
FT                   /evidence="ECO:0007829|PDB:2LLN"
FT   TURN            22..27
FT                   /evidence="ECO:0007829|PDB:2CUA"
FT   TURN            30..32
FT                   /evidence="ECO:0007829|PDB:2CUA"
FT   HELIX           34..36
FT                   /evidence="ECO:0007829|PDB:2CUA"
FT   STRAND          38..42
FT                   /evidence="ECO:0007829|PDB:2CUA"
FT   STRAND          45..53
FT                   /evidence="ECO:0007829|PDB:2CUA"
FT   STRAND          56..65
FT                   /evidence="ECO:0007829|PDB:2CUA"
FT   STRAND          68..79
FT                   /evidence="ECO:0007829|PDB:2CUA"
FT   STRAND          81..85
FT                   /evidence="ECO:0007829|PDB:2CUA"
FT   TURN            86..89
FT                   /evidence="ECO:0007829|PDB:2LLN"
FT   STRAND          91..94
FT                   /evidence="ECO:0007829|PDB:2CUA"
FT   STRAND          96..99
FT                   /evidence="ECO:0007829|PDB:2LLN"
FT   STRAND          100..105
FT                   /evidence="ECO:0007829|PDB:2CUA"
FT   STRAND          110..115
FT                   /evidence="ECO:0007829|PDB:2CUA"
FT   HELIX           124..126
FT                   /evidence="ECO:0007829|PDB:2FWL"
FT   STRAND          128..134
FT                   /evidence="ECO:0007829|PDB:2CUA"
SQ   SEQUENCE   135 AA;  14804 MW;  786895A803A52FAB CRC64;
     AYTLATHTAG VIPAGKLERV DPTTVRQEGP WADPAQAVVQ TGPNQYTVYV LAFAFGYQPN
     PIEVPQGAEI VFKITSPDVI HGFHVEGTNI NVEVLPGEVS TVRYTFKRPG EYRIICNQYC
     GLGHQNMFGT IVVKE
 
 
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