Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q2LCQ6 (COX1_DICCI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Encoded onMitochondrion
OrganismDictyostelium citrinum (Slime mold)
Taxonomic identifier361072 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length773 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 773773Cytochrome c oxidase subunit 1+2
PRO_0000312386

Regions

Transmembrane41 – 6121Helical; Potential
Transmembrane87 – 11125Helical; Potential
Transmembrane130 – 15021Helical; Potential
Transmembrane173 – 19321Helical; Potential
Transmembrane211 – 23121Helical; Potential
Transmembrane262 – 27817Helical; Potential
Transmembrane290 – 31021Helical; Potential
Transmembrane335 – 35521Helical; Potential
Transmembrane362 – 38221Helical; Potential
Transmembrane396 – 41621Helical; Potential
Transmembrane444 – 46421Helical; Potential
Transmembrane483 – 50321Helical; Potential
Transmembrane555 – 57521Helical; Potential
Transmembrane604 – 62421Helical; Potential
Region1 – 491491COX1
Region492 – 773282COX2

Sites

Metal binding851Iron (heme A axial ligand) By similarity
Metal binding2641Copper B By similarity
Metal binding2681Copper B By similarity
Metal binding3141Copper B By similarity
Metal binding3151Copper B By similarity
Metal binding4001Iron (heme A3 axial ligand) By similarity
Metal binding4021Iron (heme A axial ligand) By similarity
Metal binding7091Copper A By similarity
Metal binding7441Copper A By similarity
Metal binding7481Copper A By similarity
Metal binding7521Copper A By similarity

Amino acid modifications

Cross-link264 ↔ 2681'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2LCQ6 [UniParc].

Last modified February 21, 2006. Version 1.
Checksum: DBAB29E1527D1BD4

FASTA77386,778
        10         20         30         40         50         60 
MKLLEIYDKQ LVEQEEGGFR AILTRYLNKW IFTVDHKLIG TMYITFSIFA GIIGTLLSLV 

        70         80         90        100        110        120 
IPMELSTGNM LEGDSQQYNV IVTAHGLIMI FFVVMYCSMP AMLGGFANWF LPIMVGAPDV 

       130        140        150        160        170        180 
AFPRLNNISL WLIVVSFGLL LTSSCVGIGA GTGWTVYPPL SMMEYHPGHA VDVGILSLHI 

       190        200        210        220        230        240 
AGASSLVGAI NFLTTVFNMK IAGLSWPKVS LFVWSVVITA VLLVLSLPVL AGGLTMLITD 

       250        260        270        280        290        300 
RNFETTFFDP IGGGDPILYQ HLFHPEVYIL ILPGFGIISI IISRYSNKGI FGVKGMISAM 

       310        320        330        340        350        360 
SAIGFLGFLV WAYHHMYTVG LDVDTRAYFT AATMIIAIPT GIKIFSWLAT LWGGVIKITT 

       370        380        390        400        410        420 
PMLFVIGFLV LFTIGGLTGV VLANGGLDIS LHDTYYVVAH FHYVLSMGAI FAIFAGYYYY 

       430        440        450        460        470        480 
YAIMNSNRIL GIVRYNEQLG RIHFWTMFIG VNVTFFPMHF LGLAGMPRRI GDYPDAYIGW 

       490        500        510        520        530        540 
NLIASYGSLI TAFGLLFFFV NIFTPYFKKK ALISKKFQRG AMILMGLDFS RDWQIGFQDP 

       550        560        570        580        590        600 
ATPIMEGIID LHNYIFFYLI VVAVFIGWVM GRILWRFAYK WSYPTIGDIE IFKNFTAYNQ 

       610        620        630        640        650        660 
IIHGTVIEIV WTLIPTVILY LIAIPSFTLL YAMDEIINPT VTIKIIGHQW YWSYEYGDNS 

       670        680        690        700        710        720 
SNLVEFDSYM VYERDLNEGQ LRLLEVDNSM IVPVKTHIRL IITSGDVLHS WAVPSFGIKV 

       730        740        750        760        770 
DAVPGRLNQI GLYVKREGTF YGQCSELCGV DHGFMPIKVE AVKVQEYLGR LYK 

« Hide

References

[1]"Mitochondrial genome evolution in the social amoebae."
Heidel A.J., Gloeckner G.
Mol. Biol. Evol. 25:1440-1450(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ336395 Genomic DNA. Translation: ABC60387.1.
RefSeqYP_492636.2. NC_007787.2.

3D structure databases

ProteinModelPortalQ2LCQ6.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3912629.

Enzyme and pathway databases

UniPathwayUPA00705.

Family and domain databases

Gene3D1.10.287.90. 1 hit.
1.20.210.10. 1 hit.
2.60.40.420. 1 hit.
InterProIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR000883. Cyt_c_Oxase_su1.
IPR023616. Cyt_c_Oxase_su1_dom.
IPR014222. Cyt_c_oxidase_su2.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]
PANTHERPTHR10422. PTHR10422. 1 hit.
PfamPF00115. COX1. 1 hit.
PF00116. COX2. 1 hit.
PF02790. COX2_TM. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF49503. SSF49503. 1 hit.
SSF81442. SSF81442. 1 hit.
SSF81464. SSF81464. 1 hit.
TIGRFAMsTIGR02866. CoxB. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_DICCI
AccessionPrimary (citable) accession number: Q2LCQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: February 21, 2006
Last modified: May 14, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways