Cytochrome c oxidase subunit 1+2 - Dictyostelium discoideum (Slime mold)

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Reviewed, UniProtKB/Swiss-Prot O21042 (COX1_DICDI)

Last modified October 13, 2009. Version 68. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Cytochrome c oxidase subunit 1+2
    EC=1.9.3.1
Alternative name(s):
    Cytochrome c oxidase polypeptide I+II

Gene names

Name:	cox1/2
Synonyms:	cox1, coxI, Ddmco
ORF Names:	DDB_G0294088

Encoded on

Mitochondrion

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

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Protein attributes

Sequence length	764 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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General annotation (Comments)

Function	Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B By similarity.
Catalytic activity	4 ferrocytochrome c + O₂ + 4 H⁺ = 4 ferricytochrome c + 2 H₂O.
Pathway	Energy metabolism; oxidative phosphorylation.
Subcellular location	Mitochondrion inner membrane; Multi-pass membrane protein.
Sequence similarities	In the N-terminal section; belongs to the heme-copper respiratory oxidase family. In the C-terminal section; belongs to the cytochrome c oxidase subunit 2 family.

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Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transmembrane
Ligand	Copper Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	aerobic respiration Inferred from electronic annotation. Source: InterPro respiratory electron transport chain Inferred from electronic annotation. Source: InterPro transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-KW respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW cytochrome-c oxidase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 764

764

Cytochrome c oxidase subunit 1+2

PRO_0000312383

Regions

Transmembrane

36 – 56

Potential

Transmembrane

82 – 102

Potential

Transmembrane

121 – 141

Potential

Transmembrane

164 – 184

Potential

Transmembrane

202 – 222

Potential

Transmembrane

253 – 273

Potential

Transmembrane

285 – 305

Potential

Transmembrane

329 – 349

Potential

Transmembrane

356 – 376

Potential

Transmembrane

390 – 410

Potential

Transmembrane

438 – 458

Potential

Transmembrane

477 – 497

Potential

Transmembrane

545 – 565

Potential

Transmembrane

594 – 614

Potential

Region

1 – 485

485

COX1

Region

486 – 764

279

COX2

Sites

Metal binding

Iron (heme A axial ligand) By similarity

Metal binding

259

Copper B By similarity

Metal binding

263

Copper B By similarity

Metal binding

308

Copper B By similarity

Metal binding

309

Copper B By similarity

Metal binding

394

Iron (heme A3 axial ligand) By similarity

Metal binding

396

Iron (heme A axial ligand) By similarity

Metal binding

699

Copper A By similarity

Metal binding

734

Copper A By similarity

Metal binding

738

Copper A By similarity

Metal binding

742

Copper A By similarity

Amino acid modifications

Cross-link

259 ↔ 263

1'-histidyl-3'-tyrosine (His-Tyr) By similarity

Experimental info

Sequence conflict

83 – 89

IMIFFVV → MKVFMNC in AAB42021. Ref.3

Sequence conflict

104

I → II in AAB42021. Ref.3

Sequence conflict

198

S → P in AAB42021. Ref.3

Sequence conflict

259

H → D in CAA65139. Ref.5

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Sequences

Sequence

Length

Mass (Da)

Tools

O21042-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: BF363A039A0BA912
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FASTA

764

85,501

        10         20         30         40         50         60 
MKILEIYDKQ IAEKEGNIFI FISKWIISVD HKNIGTMYTN FSILAGIVGT LLSLVIRMEL 

        70         80         90        100        110        120 
STGNMLDGDG QQYNVIVTAH GLIMIFFVVM PAMLGGFANW FIPIMVGSPD VAFPRLNNIS 

       130        140        150        160        170        180 
LWLIIVSFFL LLTSSCVGIG VGTGWTVYPP LSTMEYHPGH AVDVGILSLH IAGASSLLGA 

       190        200        210        220        230        240 
INFLTTVFNM KIAGLSWSKV SLFVWSILIT AVLLVLSLPV LAGGLTMLIT DRNFETTFFD 

       250        260        270        280        290        300 
PIGGGDPILY QHLFWFFGHP EVYILILPGF GLVSIILSKY SNKGIFGVKG MISAMSAIGF 

       310        320        330        340        350        360 
LGFLVWAHHM YTVGLDVDTR AYFTAATMII AIPTGIKIFS WLATLWGGVI KITTPMLFVI 

       370        380        390        400        410        420 
GFLVLFTIGG LTGVVLANGG LDISLHDTYY VVAHFHYVLS MGAIFAIFAG YYYYYSIMNS 

       430        440        450        460        470        480 
TRLFGVVRYN EQLGRIHFWT MFIGVNVTFF PMHFLGLAGM PRRIGDYPDA YIGWNLIASY 

       490        500        510        520        530        540 
GSLITAFGLL FFVVNIFTPY IRRSVNIKNG AIILMGLDFA RDWQIGFQDP ATPIMEGIID 

       550        560        570        580        590        600 
LHNYIFFYLI VVAVFIGWVM GRILWRFSYK WSYPTIGDIE IFKNFTAYNQ IIHGTVIEIV 

       610        620        630        640        650        660 
WTLIPTVILY LIAIPSFTLL YAMDEIINPT VTIKIIGHQW YWSYEYGDNA SNLIEFDSYM 

       670        680        690        700        710        720 
VYERDLAEGQ LRLLEVDNAM VVPVKTHIRL IITSGDVLHS WAIPSFGIKV DAVPGRLNQI 

       730        740        750        760 
GLYVKREGTF YGQCSELCGV DHGFMPIKVQ AVKLGEYFSK LNEK

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References

[1]	"Group-I introns in the cytochrome c oxidase genes of Dictyostelium discoideum: two related ORFs in one loop of a group-I intron, a cox1/2 hybrid gene and an unusually large cox3 gene." Ogawa S., Matsuo K., Angata K., Yanagisawa K., Tanaka Y. Curr. Genet. 31:80-88(1997) [PubMed: 9000384] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: AX3.
[2]	"The mitochondrial DNA of Dictyostelium discoideum: complete sequence, gene content and genome organization." Ogawa S., Yoshino R., Angata K., Iwamoto M., Pi M., Kuroe K., Matsuo K., Morio T., Urushihara H., Yanagisawa K., Tanaka Y. Mol. Gen. Genet. 263:514-519(2000) [PubMed: 10821186] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: AX3.
[3]	"Dictyostelium discoideum Ddmco gene sequence." Mueller-Taubenberger A. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 83-205. Strain: AX3.
[4]	"Subunits I and II of Dictyostelium cytochrome c oxidase are specified by a single open reading frame transcribed into a large polycistronic RNA." Pellizzari R., Anjard C., Bisson R. Biochim. Biophys. Acta 1320:1-7(1997) [PubMed: 9186775] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 259-764. Strain: AX3.
[5]	Anjard C., Reymond C.D. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 259-341. Strain: AX2.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	D50297 Genomic DNA. Translation: BAA21123.1. AB000109 Genomic DNA. Translation: BAA78055.1. U87391 mRNA. Translation: AAB42021.1. X81884 Genomic DNA. Translation: CAA57467.1. X95896 Genomic DNA. Translation: CAA65139.1.
PIR	T43751.
RefSeq	NP_050073.1.
3D structure databases
HSSP	HSSP built from PDB template 1AR1 based on UniProtKB P98002.
ModBase	Search...
Protein-protein interaction databases
STRING	O21042.
Genome annotation databases
GeneID	2193894.
GenomeReviews	Gene locus cox1/2 in contig AB000109_GR.
Organism-specific databases
dictyBase	DDB_G0294088. cox1/2.
Enzyme and pathway databases
BRENDA	1.9.3.1. 424.
Family and domain databases
InterPro	IPR001505. Copper_CuA. IPR008972. Cupredoxin. IPR011759. Cyt_c_oxidase_II_TM. IPR000883. Cyt_c_oxidase_su1. IPR014222. Cyt_c_oxidase_su2. IPR002429. Cyt_c_oxidase_su2_C. [Graphical view]
Gene3D	G3DSA:1.20.210.10. COX1. 1 hit. G3DSA:1.10.287.90. COX2_TM. 1 hit. G3DSA:2.60.40.420. Cupredoxin. 1 hit.
PANTHER	PTHR10422. COX1. 1 hit.
Pfam	PF00115. COX1. 1 hit. PF00116. COX2. 1 hit. PF02790. COX2_TM. 1 hit. [Graphical view]
PRINTS	PR01165. CYCOXIDASEI.
ProDom	PD000131. Copper_CuA. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR02866. CoxB. 1 hit.
PROSITE	PS50855. COX1. 1 hit. PS00077. COX1_CUB. 1 hit. PS00078. COX2. 1 hit. PS50857. COX2_CUA. 1 hit. PS50999. COX2_TM. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

COX1_DICDI

Accession

Primary (citable) accession number: O21042
Secondary accession number(s): P92625, Q23893, Q7GET3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 4, 2007
Last sequence update:	January 1, 1998
Last modified:	October 13, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

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Relevant documents

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents