COX1_DICDI
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 03-AUG-2022, entry version 138.
DE RecName: Full=Cytochrome c oxidase subunit 1+2;
DE EC=7.1.1.9;
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; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; 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/pl00008685;
RA Ogawa S., Yoshino R., Angata K., Iwamoto M., Pi M., Kuroe K., Matsuo K.,
RA Morio T., Urushihara H., Yanagisawa K., Tanaka Y.;
RT "The mitochondrial DNA of Dictyostelium discoideum: complete sequence, gene
RT 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 by a
RT single open reading frame transcribed into a large polycistronic 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: Component of the cytochrome c oxidase, the last enzyme in the
CC mitochondrial electron transport chain which drives oxidative
CC phosphorylation. The respiratory chain contains 3 multisubunit
CC complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC transfer electrons derived from NADH and succinate to molecular oxygen,
CC creating an electrochemical gradient over the inner membrane that
CC drives transmembrane transport and the ATP synthase. Cytochrome c
CC oxidase is the component of the respiratory chain that catalyzes the
CC reduction of oxygen to water. Electrons originating from reduced
CC cytochrome c in the intermembrane space (IMS) are transferred via the
CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC to the active site in subunit 1, a binuclear center (BNC) formed by
CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC water molecules using 4 electrons from cytochrome c in the IMS and 4
CC protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P00401}.
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 Evidence={ECO:0000250|UniProtKB:P00401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC Evidence={ECO:0000250|UniProtKB:P00401};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P00401};
CC Note=Binds 2 heme A groups non-covalently per subunit.
CC {ECO:0000250|UniProtKB:P00401};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P00401};
CC Note=Binds a copper B center. {ECO:0000250|UniProtKB:P00401};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P00401}.
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of a catalytic core of 3 subunits and
CC several supernumerary subunits. The complex exists as a monomer or a
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1
CC complex, complex III, CIII). {ECO:0000250|UniProtKB:P00401}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00401}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00401}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the heme-copper
CC respiratory oxidase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the cytochrome c
CC oxidase subunit 2 family. {ECO:0000305}.
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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 AlphaFoldDB; O21042; -.
DR SMR; O21042; -.
DR GeneID; 2193894; -.
DR KEGG; ddi:DidioMp06; -.
DR dictyBase; DDB_G0294088; cox1/2.
DR InParanoid; O21042; -.
DR PhylomeDB; O21042; -.
DR UniPathway; UPA00705; -.
DR PRO; PR:O21042; -.
DR Proteomes; UP000002195; Mitochondrion.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR CDD; cd13912; CcO_II_C; 1.
DR CDD; cd01663; Cyt_c_Oxidase_I; 1.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 1.20.210.10; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR034210; CcO_II_C.
DR InterPro; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR InterPro; IPR000883; Cyt_C_Oxase_1.
DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR033944; Cyt_c_oxase_su1_dom.
DR InterPro; IPR014222; Cyt_c_oxidase_su2.
DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
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; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81442; SSF81442; 1.
DR SUPFAM; SSF81464; SSF81464; 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 Calcium; Copper; Electron transport; Heme; Iron; Magnesium; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..764
FT /note="Cytochrome c oxidase subunit 1+2"
FT /id="PRO_0000312383"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 594..614
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..485
FT /note="COX1"
FT REGION 486..764
FT /note="COX2"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 80
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_note="low-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 259
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 263
FT /ligand="O2"
FT /ligand_id="ChEBI:CHEBI:15379"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 308
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 309
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 386
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with subunit 2"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 387
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with subunit 2"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 394
FT /ligand="heme a3"
FT /ligand_id="ChEBI:CHEBI:83282"
FT /ligand_note="high-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 396
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_note="low-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 699
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 734
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 738
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 742
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT CROSSLNK 259..263
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT CONFLICT 83..89
FT /note="IMIFFVV -> MKVFMNC (in Ref. 3; AAB42021)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="I -> II (in Ref. 3; AAB42021)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="S -> P (in Ref. 3; AAB42021)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="H -> D (in Ref. 5; CAA65139)"
FT /evidence="ECO:0000305"
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
