Cytochrome c oxidase subunit 1 - Marchantia polymorpha (Liverwort)

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P26856 (COX1_MARPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 83. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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 on

Mitochondrion

Organism

Marchantia polymorpha (Liverwort) (Marchantia aquatica)

Taxonomic identifier

3197 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Marchantiophyta › Marchantiopsida › Marchantiidae › Marchantiales › Marchantiaceae › Marchantia

Protein attributes

Sequence length	522 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transmembrane Transmembrane helix
Ligand	Copper Heme Iron Metal-binding
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological_process	aerobic respiration Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW oxidative phosphorylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: InterPro respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	copper ion binding Inferred from electronic annotation. Source: InterPro 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 iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 522

522

Cytochrome c oxidase subunit 1

PRO_0000183360

Regions

Transmembrane

19 – 39

Helical; Potential

Transmembrane

67 – 87

Helical; Potential

Transmembrane

104 – 124

Helical; Potential

Transmembrane

149 – 169

Helical; Potential

Transmembrane

187 – 207

Helical; Potential

Transmembrane

238 – 258

Helical; Potential

Transmembrane

270 – 290

Helical; Potential

Transmembrane

313 – 333

Helical; Potential

Transmembrane

341 – 361

Helical; Potential

Transmembrane

380 – 400

Helical; Potential

Transmembrane

417 – 437

Helical; Potential

Transmembrane

459 – 479

Helical; Potential

Sites

Metal binding

Iron (heme A axial ligand) Probable

Metal binding

244

Copper B Probable

Metal binding

248

Copper B Probable

Metal binding

293

Copper B Probable

Metal binding

294

Copper B Probable

Metal binding

379

Iron (heme A3 axial ligand) Probable

Metal binding

381

Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link

244 ↔ 248

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

Sequences

Sequence

Length

Mass (Da)

Tools

P26856 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: 4B88E16F03A11D01
Show »

FASTA

522

57,552

        10         20         30         40         50         60 
MNNFAQRWLF STNHKDIGTL YLIFGAIAGV MGTCFSVLIR MELAQPGNQI LGGNHQLYNV 

        70         80         90        100        110        120 
LITAHAFLMI FFMVMPAMIG GFGNWFVPIL IGSPDMAFPR LNNISFWLLP PSLLLLLSSA 

       130        140        150        160        170        180 
LVEVGCGSGW TVYPPLSGIT SHSGGSVDLA IFSLHLSGVS SILGSINFIT TIFNMRAPGL 

       190        200        210        220        230        240 
TMHRLPLFVW SVLVTAFLLL LSLPVLAGAI TMLLTDRNFN TTFFDPAGGG DPILYQHLFW 

       250        260        270        280        290        300 
FFGHPEVYIL ILPGFGIISH IVSTFSRKPV FGYLGMVYAM ISIGVLGFIV WAHHMFTVGL 

       310        320        330        340        350        360 
DVDTRAYFTA ATMIIAVPTG IKIFSWIATM WGGSIQYKTP MLFAVGFIFL FTVGGLTGIV 

       370        380        390        400        410        420 
LANSGVDIAL HDTYYVVAHF HYVLSMGAVF ALFAGFYYWI GKITGLQYPE TLGQIHFWIT 

       430        440        450        460        470        480 
FFGVNLTFFP MHFLGLAGMP RRIPDYPDAY AGWNAFSSFG SYVSVVGIFC FFVVVFLTLT 

       490        500        510        520 
SENKCAPSPW AVEQNSTTLE WMVPSPPAFH TFEELPAIKE SI

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References

[1]

"Gene organization deduced from the complete sequence of liverwort Marchantia polymorpha mitochondrial DNA. A primitive form of plant mitochondrial genome."
Oda K., Yamato K., Ohta E., Nakamura Y., Takemura M., Nozato N., Akashi K., Kanegae T., Ogura Y., Kohchi T., Ohyama K.
J. Mol. Biol. 223:1-7(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	M68929 Genomic DNA. Translation: AAC09451.1.
PIR	S25956.
RefSeq	NP_054454.1. NC_001660.1.
3D structure databases
ProteinModelPortal	P26856.
SMR	P26856. Positions 4-514.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2702483.
Enzyme and pathway databases
UniPathway	UPA00705.
Family and domain databases
Gene3D	1.20.210.10. 1 hit.
InterPro	IPR000883. Cyt_c_Oxase_su1. IPR023615. Cyt_c_Oxase_su1_BS. IPR023616. Cyt_c_Oxase_su1_dom. IPR014241. Cyt_c_oxidase_su1_bac. [Graphical view]
PANTHER	PTHR10422. PTHR10422. 1 hit.
Pfam	PF00115. COX1. 1 hit. [Graphical view]
PRINTS	PR01165. CYCOXIDASEI.
SUPFAM	SSF81442. COX1. 1 hit.
TIGRFAMs	TIGR02891. CtaD_CoxA. 1 hit.
PROSITE	PS50855. COX1. 1 hit. PS00077. COX1_CUB. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

COX1_MARPO

Accession

Primary (citable) accession number: P26856

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	February 1, 1994
Last modified:	April 3, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents