Ubiquinol oxidase subunit 1 - Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)

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P57543 (CYOB_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. 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:
Ubiquinol oxidase subunit 1
EC=1.10.3.-

Alternative name(s):
Cytochrome o subunit 1
Cytochrome o ubiquinol oxidase subunit 1
Oxidase BO(3) subunit 1
Ubiquinol oxidase polypeptide I

Gene names

Name:	cyoB
Ordered Locus Names:	BU471

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) [Reference proteome] [HAMAP]

Taxonomic identifier

107806 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera ›

Protein attributes

Sequence length	662 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain that predominates when cells are grown at high aeration. This ubiquinol oxidase shows proton pump activity across the membrane in addition to the electron transfer By similarity.
Catalytic activity	Ubiquinol-8 + O₂ = Ubiquinone-8 + H₂O.
Cofactor	Binds 1 copper ion By similarity. Binds 2 protoheme IX (heme b55 and b562) groups.
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity.
Miscellaneous	Ubiquinol oxidase catalyzes the terminal step in the electron transport chain.
Sequence similarities	Belongs to the heme-copper respiratory oxidase family.

Ontologies

Keywords
Biological process	Electron transport Hydrogen ion transport Ion transport Respiratory chain Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Copper Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aerobic respiration Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cytochrome-c oxidase activity Inferred from electronic annotation. Source: InterPro 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 oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor 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 – 662

662

Ubiquinol oxidase subunit 1

PRO_0000183479

Regions

Topological domain

1 – 14

Extracellular Potential

Transmembrane

15 – 35

Helical; Potential

Topological domain

36 – 58

Cytoplasmic Potential

Transmembrane

59 – 79

Helical; Potential

Topological domain

80 – 106

Extracellular Potential

Transmembrane

107 – 127

Helical; Potential

Topological domain

128 – 145

Cytoplasmic Potential

Transmembrane

146 – 166

Helical; Potential

Topological domain

167 – 189

Extracellular Potential

Transmembrane

190 – 210

Helical; Potential

Topological domain

211 – 232

Cytoplasmic Potential

Transmembrane

233 – 253

Helical; Potential

Topological domain

254 – 277

Extracellular Potential

Transmembrane

278 – 298

Helical; Potential

Topological domain

299 – 309

Cytoplasmic Potential

Transmembrane

310 – 330

Helical; Potential

Topological domain

331 – 346

Extracellular Potential

Transmembrane

347 – 367

Helical; Potential

Topological domain

368 – 380

Cytoplasmic Potential

Transmembrane

381 – 401

Helical; Potential

Topological domain

402 – 413

Extracellular Potential

Transmembrane

414 – 434

Helical; Potential

Topological domain

435 – 456

Cytoplasmic Potential

Transmembrane

457 – 477

Helical; Potential

Topological domain

478 – 493

Extracellular Potential

Transmembrane

494 – 514

Helical; Potential

Topological domain

515 – 586

Cytoplasmic Potential

Transmembrane

587 – 607

Helical; Potential

Topological domain

608

Extracellular Potential

Transmembrane

609 – 629

Helical; Potential

Topological domain

630 – 662

Cytoplasmic Potential

Sites

Metal binding

106

Iron (heme B axial ligand) Probable

Metal binding

284

Copper B Probable

Metal binding

288

Copper B Probable

Metal binding

333

Copper B Probable

Metal binding

334

Copper B Probable

Metal binding

419

Iron (heme O axial ligand) Probable

Metal binding

421

Iron (heme B axial ligand) Probable

Amino acid modifications

Cross-link

284 ↔ 288

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

Sequences

Sequence

Length

Mass (Da)

Tools

P57543 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: 3F502A628133EA65
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FASTA

662

75,455

        10         20         30         40         50         60 
MFGKLTFDAI PYHEPIIMIT YIAIILIALC IASTITYYKK WKYLWYEWFT TVDHKKISIM 

        70         80         90        100        110        120 
YGILAFVMLF RGFVDAILMR TQQVVASAGF KGFLPPHHYD QIFTAHGVIM IFFVAMPLVI 

       130        140        150        160        170        180 
GLMNLVIPLQ IGARDVAFPF LNNLSFWLNV SSAVLLTLSL GIGEFAQTGW LAYPPLSGIK 

       190        200        210        220        230        240 
YSSGVGVDYW IWSLQISGVG TTLTGINFLV TILKMRAPGM SFFKMPVFTW TSLCTNILIV 

       250        260        270        280        290        300 
ISFPVLTVTL VLLTLDRYFN FHFFTNDLGG NAMMYVNLIW IWGHPEVYIL VLPVFGVFSE 

       310        320        330        340        350        360 
VVATFSKKRL FGYVSLVWAT LSITILSFIV WLHHFFTMGA GADVNTFFGI TTMIIAIPTG 

       370        380        390        400        410        420 
VKIFNWLFTI YQGRVHMHSS ILWTLGFLVT FSIGGMTGVL LSVPPADFVL HNSLFLVAHF 

       430        440        450        460        470        480 
HNVIIGGVVF GCFAGINYWF PKLFGFVLNE IWGKRAFWFW IIGFFLAFIP LYFLGLMGMT 

       490        500        510        520        530        540 
RRLSQNIDSE FHMLLCIAAI GACFIGIGII CQVIQFFISI KERRHNLDLT GDPWDGRTLE 

       550        560        570        580        590        600 
WSTSSPAPLY NFAIIPKVED RDDFWRNKEG QHYNKLINSI NYHDIHMPKN TGLGFMISIF 

       610        620        630        640        650        660 
SLFFGFSAVW HITWLCILSF LAIIISLFIN SLNEDTEYTI SAEEIKKIEH QYWKNIQKAG 


LK

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References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: APS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000003 Genomic DNA. Translation: BAB13168.1.
RefSeq	NP_240282.1. NC_002528.1.
3D structure databases
ProteinModelPortal	P57543.
SMR	P57543. Positions 52-552.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB13168; BAB13168; BAB13168.
GeneID	1109818.
KEGG	buc:BU471.
PATRIC	21244484. VBIBucAph127364_0480.
Phylogenomic databases
eggNOG	COG0843.
HOGENOM	HOG000085275.
KO	K02298.
OMA	WNIWLYI.
ProtClustDB	CLSK435874.
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. IPR014207. Cyt_c_ubiqinol_oxidase_su1. [Graphical view]
PANTHER	PTHR10422. PTHR10422. 1 hit.
Pfam	PF00115. COX1. 1 hit. [Graphical view]
PRINTS	PR01165. CYCOXIDASEI.
SUPFAM	SSF81442. COX1. 1 hit.
TIGRFAMs	TIGR02843. CyoB. 1 hit.
PROSITE	PS50855. COX1. 1 hit. PS00077. COX1_CUB. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYOB_BUCAI

Accession

Primary (citable) accession number: P57543

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Buchnera aphidicola (subsp. Acyrthosiphon pisum)

Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names

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

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents