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P14544 (COX1_LEITA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:COI
Encoded onMitochondrion
OrganismLeishmania tarentolae (Sauroleishmania tarentolae)
Taxonomic identifier5689 [NCBI]
Taxonomic lineageEukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Leishmaniinae › Leishmania › lizard Leishmania

Protein attributes

Sequence length549 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 – 549549Cytochrome c oxidase subunit 1
PRO_0000183350

Regions

Transmembrane18 – 3821Helical; Potential
Transmembrane42 – 6221Helical; Potential
Transmembrane66 – 8621Helical; Potential
Transmembrane100 – 12021Helical; Potential
Transmembrane148 – 16821Helical; Potential
Transmembrane186 – 20621Helical; Potential
Transmembrane222 – 24221Helical; Potential
Transmembrane246 – 26621Helical; Potential
Transmembrane269 – 28921Helical; Potential
Transmembrane306 – 32621Helical; Potential
Transmembrane340 – 36021Helical; Potential
Transmembrane379 – 39921Helical; Potential
Transmembrane402 – 42221Helical; Potential
Transmembrane460 – 48021Helical; Potential
Transmembrane484 – 50421Helical; Potential
Transmembrane520 – 54021Helical; 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

Sequences

Sequence LengthMass (Da)Tools
P14544 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: F6DD04815A4917C2

FASTA54963,272
        10         20         30         40         50         60 
MFWLCLVCLS VSHKMIGLCY LLVAILSGFV GYVYSLFIRL ELSLIGCGIL FGDYQFYNVL 

        70         80         90        100        110        120 
ITSHGLIMVF AFIMPVMMGG LVNYFIPVMA GFPDMVFPRL NNMSFWMYLA GFGCVVNGFL 

       130        140        150        160        170        180 
TEEGMGVGWT LYPTLICIDF HSSLACDFVM FAVHLLGISS ILNSINLLGT LFCCRRKFFS 

       190        200        210        220        230        240 
FLSWSLFIWA ALITAILLII TLPVLAGGVT LILCDRNFNT SFYDVVGGGD LILFQHIFWF 

       250        260        270        280        290        300 
FGHPEVYIIL LPVFGLISTI VEVIGFRCVF STVAMIYSMI LIAILGMFVW AHHMFVVGMD 

       310        320        330        340        350        360 
VDSRAYFGGV SILIGLPTCV KLFNWIYSFL YTDMIITFEV YFVIMFIFMF LIGAVTGLFL 

       370        380        390        400        410        420 
SNVGIDIMLH DTYFVVGHFH YVLSLGAVVG FFTGFIHFLA KWLPIELYLF WMFYFISTLF 

       430        440        450        460        470        480 
IGSNMLFFPM HSLGMYAFPR RISDYPVSFL FWSSFMLYGM LLLASLILFL CALFCVFLFW 

       490        500        510        520        530        540 
DYCLFFVSLF VFSLYCFFYF STWLPCVMVL YLLLVDFAHI VLDYLFLILC FCFVFFIFFW 


QSLFLFFYI

« Hide

References

[1]"Sequences of six genes and several open reading frames in the kinetoplast maxicircle DNA of Leishmania tarentolae."
de la Cruz V.F., Neckelmann N., Simpson L.
J. Biol. Chem. 259:15136-15147(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

PIRD30010.

3D structure databases

ProteinModelPortalP14544.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
[Graphical view]
PANTHERPTHR10422. PTHR10422. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF81442. COX1. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_LEITA
AccessionPrimary (citable) accession number: P14544
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 3, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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