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P24794 (COX1_BETVU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 93. 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

EC=1.9.3.1
Alternative name(s):
Cytochrome c oxidase polypeptide I
Gene names
Name:COX1
Synonyms:COXI
Encoded onMitochondrion
OrganismBeta vulgaris (Sugar beet)
Taxonomic identifier161934 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeBeta

Protein attributes

Sequence length524 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.

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

Belongs to the heme-copper respiratory oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 524524Cytochrome c oxidase subunit 1
PRO_0000183293

Regions

Transmembrane18 – 3821Helical; Potential
Transmembrane66 – 8621Helical; Potential
Transmembrane103 – 12321Helical; Potential
Transmembrane148 – 16821Helical; Potential
Transmembrane186 – 20621Helical; Potential
Transmembrane237 – 25721Helical; Potential
Transmembrane269 – 28921Helical; Potential
Transmembrane312 – 33221Helical; Potential
Transmembrane340 – 36021Helical; Potential
Transmembrane379 – 39921Helical; Potential
Transmembrane414 – 43421Helical; Potential
Transmembrane458 – 47821Helical; Potential

Sites

Metal binding641Iron (heme A axial ligand) Probable
Metal binding2431Copper B Probable
Metal binding2471Copper B Probable
Metal binding2921Copper B Probable
Metal binding2931Copper B Probable
Metal binding3781Iron (heme A3 axial ligand) Probable
Metal binding3801Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link243 ↔ 2471'-histidyl-3'-tyrosine (His-Tyr) By similarity

Experimental info

Sequence conflict1 – 99MTNLVRWLF → MAV in AAA87330. Ref.2
Sequence conflict220 – 2278TTFFDPAG → RPFLIRW in AAA87330. Ref.2
Sequence conflict501 – 5033EWM → ND in AAA87330. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P24794 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: A862089EE5C476EA

FASTA52457,581
        10         20         30         40         50         60 
MTNLVRWLFS TNHKDIGTLY FIFGAIAGVM GTCFSVLIRM ELARPGDQIL GGNHQLYNVL 

        70         80         90        100        110        120 
ITAHAFLMIF FMVMPAMIGG FGNWFVPILI GAPDMAFPRL NNISFWLLPP SLLLLLSSAL 

       130        140        150        160        170        180 
VEVGSGTGWT VYPPLSGITS HSGGAVDLAI FSLHLSGVSS ILGSINFITT IFNMRGPGMT 

       190        200        210        220        230        240 
MHRLPLFVWS VLVTAFLLLL SLPVLAGAIT MLLTDRNFNT TFFDPAGGGD PILYQHLFWF 

       250        260        270        280        290        300 
FGHPEVYILI LPGFGIISHI VSTFSGKPVF GYLGMVYAMI SIGVLGFLVW AHHMFTVGLD 

       310        320        330        340        350        360 
VDTRAYFTAA TMIIAVPTGI KIFSWIATMW GGSIQYKTPM LFAVGFIFLF TVGGLTGIVL 

       370        380        390        400        410        420 
ANSGLDIALH DTYYVVAHFH YVLSMGAVFA LFAGFYYWVG KIFGRTYPET LGQIHFWITF 

       430        440        450        460        470        480 
FGVNLTFFPM HFLGLSGMPR RIPDYPDAYA GWNALSSFGS YISVVGICCF FVVVTITLSS 

       490        500        510        520 
GKNKRCAPSP WAVEENSTTL EWMVQSPPAF HTFGELPAIK ETKS 

« Hide

References

[1]"Genomic organization and sequence analysis of the cytochrome oxidase subunit II gene from normal and male-sterile mitochondria in sugar beet."
Senda M., Harada T., Mikami T., Sugiura M., Kinoshita T.
Curr. Genet. 19:175-181(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. TK81-O.
[2]"Nucleotide sequence of cytochrome c oxidase subunit I gene of sugar beet mitochondria."
Harada T., Mikami T., Kinoshita T.
Proc. Sugar Beet Res. 29:15-21(1987)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57693 Genomic DNA. Translation: CAA40874.1.
M57645 Genomic DNA. Translation: AAA87330.1.
PIRS14138.
RefSeqNP_064063.1. NC_002511.2.

3D structure databases

ProteinModelPortalP24794.
SMRP24794. Positions 6-515.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID809579.

Enzyme and pathway databases

UniPathwayUPA00705.

Family and domain databases

Gene3D1.20.210.10. 1 hit.
InterProIPR000883. Cyt_c_Oxase_su1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. Cyt_c_Oxase_su1_dom.
IPR014241. Cyt_c_oxidase_su1_bac.
[Graphical view]
PANTHERPTHR10422. PTHR10422. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF81442. SSF81442. 1 hit.
TIGRFAMsTIGR02891. CtaD_CoxA. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_BETVU
AccessionPrimary (citable) accession number: P24794
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: February 1, 1996
Last modified: May 14, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways