Cytochrome c oxidase subunit 1 - Allomyces macrogynus

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Reviewed, UniProtKB/Swiss-Prot P80440 (COX1_ALLMA)

Last modified October 13, 2009. Version 63. History...

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

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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

Encoded on

Mitochondrion

Organism

Allomyces macrogynus

Taxonomic identifier

28583 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Blastocladiomycota › Blastocladiomycetes › Blastocladiales › Blastocladiaceae › Allomyces

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Protein attributes

Sequence length	536 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-SubCell mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-KW 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 – 536

536

Cytochrome c oxidase subunit 1

PRO_0000183279

Regions

Transmembrane

21 – 41

Potential

Transmembrane

62 – 82

Potential

Transmembrane

105 – 125

Potential

Transmembrane

151 – 171

Potential

Transmembrane

189 – 209

Potential

Transmembrane

240 – 260

Potential

Transmembrane

272 – 292

Potential

Transmembrane

310 – 330

Potential

Transmembrane

343 – 363

Potential

Transmembrane

382 – 402

Potential

Transmembrane

417 – 437

Potential

Transmembrane

461 – 481

Potential

Sites

Metal binding

Iron (heme A axial ligand) Probable

Metal binding

246

Copper B Probable

Metal binding

250

Copper B Probable

Metal binding

295

Copper B Probable

Metal binding

296

Copper B Probable

Metal binding

381

Iron (heme A3 axial ligand) Probable

Metal binding

383

Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link

246 ↔ 250

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

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Sequences

Sequence

Length

Mass (Da)

Tools

P80440-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 7DE8DF291EAE4091
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FASTA

536

59,445

        10         20         30         40         50         60 
MFQRNTVYRW LFSTNAKDIG TLYLVFSIFA GMIGTAFSVL IRFELAGPGV QYLYGDHQLY 

        70         80         90        100        110        120 
NVIITAHAFI MIFFLVMPAM LGGFGNYFVP IMIGAPDMAF PRLNNISFWL LPPSLILLVG 

       130        140        150        160        170        180 
SAFVEQGAGT GWTVYPPLSS IGFHSGGSVD LAIFSLHLAG ISSMLGSINF ITTILNMRAP 

       190        200        210        220        230        240 
GMTMHKLPLF VWSILITAIL LLLSLPVLAG AITMLLTDRN LNTTFYDPAG GGDPVLYQHL 

       250        260        270        280        290        300 
FWFFGHPEVY IIIIPGFGII SQVISTFSRK PIFGYLGMVY AMASIGILGF IVWSHHMYTV 

       310        320        330        340        350        360 
GLDVDTRAYF TAATMIIAVP TGIKIFSWLA TLYGGNILYR TPAYFALGFL FLFTIGGVTG 

       370        380        390        400        410        420 
VMLANASLDV ALHDTYYVVA HFHYVLSMGA VFALFAGFYY WIGKITGKQY NEFWGQVHFW 

       430        440        450        460        470        480 
TMFIGVNVTF FPMHFLGLNG MPRRIPDYPD AFTQWNVISS FGSIISIVST IVFLYGLYLT 

       490        500        510        520        530 
LSQPAVSLAN NYWHVPSFFS STHSLYGDTT QTSSSLEWVL PSPPAFHAFN HLPVQS

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References

[1]	"Molecular phylogeny of Allomyces macrogynus: congruency between nuclear ribosomal RNA- and mitochondrial protein-based trees." Paquin B., Forget L., Roewer I., Lang B.F. J. Mol. Evol. 41:657-665(1995) [PubMed: 7490780] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 46923 / Burma 3-35 (35OC).
[2]	"The mitochondrial DNA of Allomyces macrogynus: the complete genomic sequence from an ancestral fungus." Paquin B., Lang B.F. J. Mol. Biol. 255:688-701(1996) [PubMed: 8636971] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 46923 / Burma 3-35 (35OC).

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Cross-references

Sequence databases
	U41288 Genomic DNA. Translation: AAC49234.1.
PIR	S63651.
RefSeq	NP_043733.1.
3D structure databases
HSSP	HSSP built from PDB template 2OCC based on UniProtKB P00396.
ModBase	Search...
Genome annotation databases
GeneID	801856.
Enzyme and pathway databases
BRENDA	1.9.3.1. 299157.
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_ALLMA

Accession

Primary (citable) accession number: P80440

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	October 13, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal 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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents