Cytochrome c oxidase subunit 1 - Allomyces macrogynus

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P80440 (COX1_ALLMA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 81. 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

Encoded on

Mitochondrion

Organism

Allomyces macrogynus

Taxonomic identifier

28583 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	536 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 – 536

536

Cytochrome c oxidase subunit 1

PRO_0000183279

Regions

Transmembrane

21 – 41

Helical; Potential

Transmembrane

62 – 82

Helical; Potential

Transmembrane

105 – 125

Helical; Potential

Transmembrane

151 – 171

Helical; Potential

Transmembrane

189 – 209

Helical; Potential

Transmembrane

240 – 260

Helical; Potential

Transmembrane

272 – 292

Helical; Potential

Transmembrane

310 – 330

Helical; Potential

Transmembrane

343 – 363

Helical; Potential

Transmembrane

382 – 402

Helical; Potential

Transmembrane

417 – 437

Helical; Potential

Transmembrane

461 – 481

Helical; 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

Sequences

Sequence

Length

Mass (Da)

Tools

P80440 [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 46923 / Burma 3-35 (35OC).

Cross-references

Sequence databases
EMBL GenBank DDBJ	U41288 Genomic DNA. Translation: AAC49234.1.
PIR	S63651.
RefSeq	NP_043733.1. NC_001715.1.
3D structure databases
ProteinModelPortal	P80440.
SMR	P80440. Positions 7-529.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	801856.
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_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:	April 3, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal 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