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Q37370 (COX1_ACACA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. 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
OrganismAcanthamoeba castellanii (Amoeba)
Taxonomic identifier5755 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaCentramoebidaAcanthamoebidaeAcanthamoeba

Protein attributes

Sequence length873 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 – 873873Cytochrome c oxidase subunit 1+2
PRO_0000183275

Regions

Transmembrane29 – 4921Helical; Potential
Transmembrane70 – 9021Helical; Potential
Transmembrane91 – 11121Helical; Potential
Transmembrane114 – 13421Helical; Potential
Transmembrane159 – 17921Helical; Potential
Transmembrane197 – 21721Helical; Potential
Transmembrane248 – 26821Helical; Potential
Transmembrane280 – 30021Helical; Potential
Transmembrane323 – 34321Helical; Potential
Transmembrane351 – 37121Helical; Potential
Transmembrane390 – 41021Helical; Potential
Transmembrane427 – 44721Helical; Potential
Transmembrane469 – 48921Helical; Potential
Transmembrane536 – 55621Helical; Potential
Transmembrane585 – 60521Helical; Potential
Transmembrane656 – 67621Helical; Potential
Transmembrane845 – 86521Helical; Potential
Region1 – 474474COX1
Region475 – 843369COX2

Sites

Metal binding751Iron (heme A axial ligand) Probable
Metal binding2541Copper B Probable
Metal binding2581Copper B Probable
Metal binding3031Copper B Probable
Metal binding3041Copper B Probable
Metal binding3891Iron (heme A3 axial ligand) Probable
Metal binding3911Iron (heme A axial ligand) Probable
Metal binding8011Copper A Probable
Metal binding8361Copper A Probable
Metal binding8401Copper A Probable
Metal binding8441Copper A Probable

Amino acid modifications

Cross-link254 ↔ 2581'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q37370 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 0BC820F0162B8EB3

FASTA87399,214
        10         20         30         40         50         60 
MINRLLNNLT SFFTDNRWLF STNHKDIGTL YLIFGGFSGI IGTIFSMIIR LELAAPGSQI 

        70         80         90        100        110        120 
LSGNSQLYNV IITAHAFVMI FFFVMPVMIG GFGNWFVPLM IGAPDMAFPR LNNISFWLLP 

       130        140        150        160        170        180 
PSLFLLLCSS LVEFGAGTGW TVYPPLSSIV AHSGGSVDLA IFSLHLAGIS SLLGAINFIT 

       190        200        210        220        230        240 
TIFNMRVPGL SMHKLPLFVW SVLITAFLLL FSLPVLAGAI TMLLTDRNFN TSFFDPSGGG 

       250        260        270        280        290        300 
DPILYQHLFW FFGHPEVYIL ILPAFGIVSQ IIGTFSNKSI FGYIGMVYAM LSIAVLGFIV 

       310        320        330        340        350        360 
WAHHMYTVGL DVDTRAYFTA ATMMIAVPTG IKIFSWIATL WGGQIVRKTP LLFVIGFLIL 

       370        380        390        400        410        420 
FTLGGLTGIV LSNAGLDIML HDTYYVVAHF HYVLSMGAVF AFFAGFYYWF WKISGYTYNE 

       430        440        450        460        470        480 
MYGNVHFWLM FIGVNLTFFP MHFVGLAGMP RRIPDYPDNY YYWNILSSFG SIISSVSVIV 

       490        500        510        520        530        540 
FFYLIYLAFN NNNTPKLIKL VHSIFAPYIN TLSKNLLTFA SIKSTSDSSF FKFSKFFIFF 

       550        560        570        580        590        600 
MVSLSVLFIF YDSLLCLNDH TNSWKIGFQD PTTPIAYGII KLHDHILFFL AVILFVVGYL 

       610        620        630        640        650        660 
LLSTYKKFYY GSLNNDLPES KRISLFDTLI NTYKENLSFN VTNRTYNINH GTTIEIIWTI 

       670        680        690        700        710        720 
LPAFILLFIA VPSFALLYAM DEIIDPVLTV KVIGHQWYWS YEYSDYSVVY SNRMLDYDSI 

       730        740        750        760        770        780 
DRFAAMEMMY KGMGYLKDRS LLSYLYIPMV IPETTIKFDS YMIHEAELNL GDLRLLKTDM 

       790        800        810        820        830        840 
PLFLPKNTHI RLLITSSDVL HSWAVPSFGV KVDAVPGRLN QTSLYLKNTG TFYGQCSELC 

       850        860        870 
GVNHAFMPIE VYVVNPVYFY NYVYIYFKNF NLI 

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References

[1]"The mitochondrial DNA of the amoeboid protozoon, Acanthamoeba castellanii: complete sequence, gene content and genome organization."
Burger G., Plante I., Lonergan K.M., Gray M.W.
J. Mol. Biol. 245:522-537(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 30010 / Neff.
[2]"Expression of a continuous open reading frame encoding subunits 1 and 2 of cytochrome c oxidase in the mitochondrial DNA of Acanthamoeba castellanii."
Lonergan K.M., Gray M.W.
J. Mol. Biol. 257:1019-1030(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U12386 Genomic DNA. Translation: AAD11820.1.
PIRS53828.
RefSeqNP_042527.1. NC_001637.1.

3D structure databases

ProteinModelPortalQ37370.
SMRQ37370. Positions 16-489.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ37370.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1734020.

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.
IPR023615. Cyt_c_Oxase_su1_BS.
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. 2 hits.
PF02790. COX2_TM. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF49503. SSF49503. 2 hits.
SSF81442. SSF81442. 1 hit.
SSF81464. SSF81464. 2 hits.
TIGRFAMsTIGR02866. CoxB. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
PS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_ACACA
AccessionPrimary (citable) accession number: Q37370
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 95 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