Cytochrome c oxidase subunit 1 - Beta vulgaris (Sugar beet)

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Reviewed, UniProtKB/Swiss-Prot P24794 (COX1_BETVU)

Last modified June 16, 2009. Version 67. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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

Beta vulgaris (Sugar beet)

Taxonomic identifier

161934 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Beta

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Protein attributes

Sequence length	524 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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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.

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Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transmembrane
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 transport Inferred from electronic annotation. Source: UniProtKB-KW
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: UniProtKB-KW 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
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 524

524

Cytochrome c oxidase subunit 1

PRO_0000183293

Regions

Transmembrane

18 – 38

Potential

Transmembrane

66 – 86

Potential

Transmembrane

103 – 123

Potential

Transmembrane

148 – 168

Potential

Transmembrane

186 – 206

Potential

Transmembrane

237 – 257

Potential

Transmembrane

269 – 289

Potential

Transmembrane

312 – 332

Potential

Transmembrane

340 – 360

Potential

Transmembrane

379 – 399

Potential

Transmembrane

414 – 434

Potential

Transmembrane

458 – 478

Potential

Sites

Metal binding

Iron (heme A axial ligand) Probable

Metal binding

243

Copper B Probable

Metal binding

247

Copper B Probable

Metal binding

292

Copper B Probable

Metal binding

293

Copper B Probable

Metal binding

378

Iron (heme A3 axial ligand) Probable

Metal binding

380

Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link

243 ↔ 247

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

Experimental info

Sequence conflict

1 – 9

MTNLVRWLF → MAV in AAA87330. Ref.2

Sequence conflict

220 – 227

TTFFDPAG → RPFLIRW in AAA87330. Ref.2

Sequence conflict

501 – 503

EWM → ND in AAA87330. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P24794-1 [UniParc].

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

524

57,581

        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

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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: 1651175] [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].

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Cross-references

Sequence databases
	X57693 Genomic DNA. Translation: CAA40874.1. M57645 Genomic DNA. Translation: AAA87330.1.
PIR	S14138.
3D structure databases
HSSP	HSSP built from PDB template 2OCC based on UniProtKB P00396.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.9.3.1. 124.
Family and domain databases
InterPro	IPR000883. Cyt_c_oxidase_su1. IPR014241. Cyt_c_oxidase_su1_bac. [Graphical view]
Gene3D	G3DSA:1.20.210.10. COX1. 1 hit.
PANTHER	PTHR10422. COX1. 1 hit.
Pfam	PF00115. COX1. 1 hit. [Graphical view]
PRINTS	PR01165. CYCOXIDASEI.
TIGRFAMs	TIGR02891. CtaD_CoxA. 1 hit.
PROSITE	PS50855. COX1. 1 hit. PS00077. COX1_CUB. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

COX1_BETVU

Accession

Primary (citable) accession number: P24794

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents