ID COX1_DICDI Reviewed; 764 AA.
AC O21042; P92625; Q23893; Q7GET3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 01-MAY-2013, entry version 93.
DE RecName: Full=Cytochrome c oxidase subunit 1+2;
DE EC=1.9.3.1;
DE AltName: Full=Cytochrome c oxidase polypeptide I+II;
GN Name=cox1/2; Synonyms=cox1, coxI, Ddmco; ORFNames=DDB_G0294088;
OS Dictyostelium discoideum (Slime mold).
OG Mitochondrion.
OC Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX3;
RX PubMed=9000384; DOI=10.1007/s002940050179;
RA Ogawa S., Matsuo K., Angata K., Yanagisawa K., Tanaka Y.;
RT "Group-I introns in the cytochrome c oxidase genes of Dictyostelium
RT discoideum: two related ORFs in one loop of a group-I intron, a cox1/2
RT hybrid gene and an unusually large cox3 gene.";
RL Curr. Genet. 31:80-88(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX3;
RX PubMed=10821186; DOI=10.1007/s004380051196;
RA Ogawa S., Yoshino R., Angata K., Iwamoto M., Pi M., Kuroe K.,
RA Matsuo K., Morio T., Urushihara H., Yanagisawa K., Tanaka Y.;
RT "The mitochondrial DNA of Dictyostelium discoideum: complete sequence,
RT gene content and genome organization.";
RL Mol. Gen. Genet. 263:514-519(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 83-205.
RC STRAIN=AX3;
RA Mueller-Taubenberger A.;
RT "Dictyostelium discoideum Ddmco gene sequence.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 259-764.
RC STRAIN=AX3;
RX PubMed=9186775; DOI=10.1016/S0005-2728(97)00010-8;
RA Pellizzari R., Anjard C., Bisson R.;
RT "Subunits I and II of Dictyostelium cytochrome c oxidase are specified
RT by a single open reading frame transcribed into a large polycistronic
RT RNA.";
RL Biochim. Biophys. Acta 1320:1-7(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 259-341.
RC STRAIN=AX2;
RA Anjard C., Reymond C.D.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC chain that catalyzes the reduction of oxygen to water. Subunits 1-
CC 3 form the functional core of the enzyme complex. CO I is the
CC catalytic subunit of the enzyme. Electrons originating in
CC cytochrome c are transferred via the copper A center of subunit 2
CC and heme A of subunit 1 to the bimetallic center formed by heme A3
CC and copper B (By similarity).
CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4
CC ferricytochrome c + 2 H(2)O.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC membrane protein.
CC -!- SIMILARITY: In the N-terminal section; belongs to the heme-copper
CC respiratory oxidase family.
CC -!- SIMILARITY: In the C-terminal section; belongs to the cytochrome c
CC oxidase subunit 2 family.
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DR EMBL; D50297; BAA21123.1; -; Genomic_DNA.
DR EMBL; AB000109; BAA78055.1; -; Genomic_DNA.
DR EMBL; U87391; AAB42021.1; -; mRNA.
DR EMBL; X81884; CAA57467.1; -; Genomic_DNA.
DR EMBL; X95896; CAA65139.1; -; Genomic_DNA.
DR PIR; T43751; T43751.
DR RefSeq; NP_050073.1; NC_000895.1.
DR ProteinModelPortal; O21042; -.
DR SMR; O21042; 20-494.
DR STRING; 44689.DidioMp06; -.
DR GeneID; 2193894; -.
DR KEGG; ddi:DidioMp06; -.
DR dictyBase; DDB_G0294088; cox1/2.
DR eggNOG; COG1622; -.
DR KO; K02256; -.
DR KO; K02261; -.
DR OMA; MISAMSA; -.
DR UniPathway; UPA00705; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner 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: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:0009060; P:aerobic respiration; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 1.20.210.10; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR000883; Cyt_c_Oxase_su1.
DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR023616; Cyt_c_Oxase_su1_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 PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF02790; COX2_TM; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; COX1; 1.
DR SUPFAM; SSF49503; Cupredoxin; 1.
DR SUPFAM; SSF81464; Cyt_c_oxidase_II-like_TM; 1.
DR TIGRFAMs; TIGR02866; CoxB; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS50999; COX2_TM; 1.
PE 2: Evidence at transcript level;
KW Complete proteome; Copper; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Oxidoreductase; Reference proteome; Respiratory chain; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1 764 Cytochrome c oxidase subunit 1+2.
FT /FTId=PRO_0000312383.
FT TRANSMEM 36 56 Helical; (Potential).
FT TRANSMEM 82 102 Helical; (Potential).
FT TRANSMEM 121 141 Helical; (Potential).
FT TRANSMEM 164 184 Helical; (Potential).
FT TRANSMEM 202 222 Helical; (Potential).
FT TRANSMEM 253 273 Helical; (Potential).
FT TRANSMEM 285 305 Helical; (Potential).
FT TRANSMEM 329 349 Helical; (Potential).
FT TRANSMEM 356 376 Helical; (Potential).
FT TRANSMEM 390 410 Helical; (Potential).
FT TRANSMEM 438 458 Helical; (Potential).
FT TRANSMEM 477 497 Helical; (Potential).
FT TRANSMEM 545 565 Helical; (Potential).
FT TRANSMEM 594 614 Helical; (Potential).
FT REGION 1 485 COX1.
FT REGION 486 764 COX2.
FT METAL 80 80 Iron (heme A axial ligand) (By
FT similarity).
FT METAL 259 259 Copper B (By similarity).
FT METAL 263 263 Copper B (By similarity).
FT METAL 308 308 Copper B (By similarity).
FT METAL 309 309 Copper B (By similarity).
FT METAL 394 394 Iron (heme A3 axial ligand) (By
FT similarity).
FT METAL 396 396 Iron (heme A axial ligand) (By
FT similarity).
FT METAL 699 699 Copper A (By similarity).
FT METAL 734 734 Copper A (By similarity).
FT METAL 738 738 Copper A (By similarity).
FT METAL 742 742 Copper A (By similarity).
FT CROSSLNK 259 263 1'-histidyl-3'-tyrosine (His-Tyr) (By
FT similarity).
FT CONFLICT 83 89 IMIFFVV -> MKVFMNC (in Ref. 3; AAB42021).
FT CONFLICT 104 104 I -> II (in Ref. 3; AAB42021).
FT CONFLICT 198 198 S -> P (in Ref. 3; AAB42021).
FT CONFLICT 259 259 H -> D (in Ref. 5; CAA65139).
SQ SEQUENCE 764 AA; 85501 MW; BF363A039A0BA912 CRC64;
MKILEIYDKQ IAEKEGNIFI FISKWIISVD HKNIGTMYTN FSILAGIVGT LLSLVIRMEL
STGNMLDGDG QQYNVIVTAH GLIMIFFVVM PAMLGGFANW FIPIMVGSPD VAFPRLNNIS
LWLIIVSFFL LLTSSCVGIG VGTGWTVYPP LSTMEYHPGH AVDVGILSLH IAGASSLLGA
INFLTTVFNM KIAGLSWSKV SLFVWSILIT AVLLVLSLPV LAGGLTMLIT DRNFETTFFD
PIGGGDPILY QHLFWFFGHP EVYILILPGF GLVSIILSKY SNKGIFGVKG MISAMSAIGF
LGFLVWAHHM YTVGLDVDTR AYFTAATMII AIPTGIKIFS WLATLWGGVI KITTPMLFVI
GFLVLFTIGG LTGVVLANGG LDISLHDTYY VVAHFHYVLS MGAIFAIFAG YYYYYSIMNS
TRLFGVVRYN EQLGRIHFWT MFIGVNVTFF PMHFLGLAGM PRRIGDYPDA YIGWNLIASY
GSLITAFGLL FFVVNIFTPY IRRSVNIKNG AIILMGLDFA RDWQIGFQDP ATPIMEGIID
LHNYIFFYLI VVAVFIGWVM GRILWRFSYK WSYPTIGDIE IFKNFTAYNQ IIHGTVIEIV
WTLIPTVILY LIAIPSFTLL YAMDEIINPT VTIKIIGHQW YWSYEYGDNA SNLIEFDSYM
VYERDLAEGQ LRLLEVDNAM VVPVKTHIRL IITSGDVLHS WAIPSFGIKV DAVPGRLNQI
GLYVKREGTF YGQCSELCGV DHGFMPIKVQ AVKLGEYFSK LNEK
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