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Entry version 124 (13 Nov 2019)
Sequence version 1 (25 Oct 2005)
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Protein

Cytochrome bo(3) ubiquinol oxidase subunit 1

Gene

cyoB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Cytochrome bo3 ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron. Protons are probably pumped via D- and K- channels found in this subunit (PubMed:11017202).4 Publications

Miscellaneous

Ubiquinol oxidase catalyzes the terminal step in the electron transport chain.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Competitively inhibited by piericidin A, non-competitively inhibited by 2-n-heptyl-4-hydroxyquinoline N-oxide, NaN3 and KCN; 50% inhibition occurs at 2 µM, 2 µM, 15 mM and 10 µM, respectively. Inhibited by Zn2+ and Cd2+.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=50 µM for ubiquinol-11 Publication
  2. KM=50 µM for ubiquinol-61 Publication
  1. Vmax=15.5 µmol/min/nmol enzyme with ubiquinol-11 Publication
  2. Vmax=12.6 µmol/min/nmol enzyme with ubiquinol-61 Publication

pH dependencei

Optimum pH is 7.4.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei71Quinone (QH)Curated1
Binding sitei75Quinone (QH)Curated1
Binding sitei98Quinone (QH)Curated1
Binding sitei101Quinone (QH)Curated1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi106Iron (heme b axial ligand)1
Metal bindingi284Copper1
Metal bindingi288CopperCurated1
Metal bindingi333Copper1
Metal bindingi334Copper1
Metal bindingi419Iron (heme o axial ligand)1
Metal bindingi421Iron (heme b axial ligand)1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTranslocase
Biological processElectron transport, Hydrogen ion transport, Ion transport, Respiratory chain, Transport
LigandCopper, Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:CYOB-MONOMER
ECOL316407:JW0421-MONOMER
MetaCyc:CYOB-MONOMER

Protein family/group databases

Transport Classification Database

More...
TCDBi
3.D.4.5.1 the proton-translocating cytochrome oxidase (cox) superfamily

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cytochrome bo(3) ubiquinol oxidase subunit 1 (EC:7.1.1.31 Publication)
Alternative name(s):
Cytochrome b562-o complex subunit I
Cytochrome o ubiquinol oxidase subunit 1
Short name:
Cytochrome o subunit 1
Oxidase bo(3) subunit 1
Ubiquinol oxidase chain A
Ubiquinol oxidase polypeptide I
Ubiquinol oxidase subunit 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:cyoB
Ordered Locus Names:b0431, JW0421
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

  • Cell inner membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 16PeriplasmicAdd BLAST16
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei17 – 35Helical; Name=IAdd BLAST19
Topological domaini36 – 52CytoplasmicAdd BLAST17
Transmembranei53 – 80Helical; Name=IIAdd BLAST28
Topological domaini81 – 95PeriplasmicAdd BLAST15
Transmembranei96 – 132Helical; Name=IIIAdd BLAST37
Topological domaini133 – 137Cytoplasmic5
Transmembranei138 – 161Helical; Name=IVAdd BLAST24
Topological domaini162 – 184PeriplasmicAdd BLAST23
Transmembranei185 – 215Helical; Name=VAdd BLAST31
Topological domaini216 – 224Cytoplasmic9
Transmembranei225 – 260Helical; Name=VIAdd BLAST36
Topological domaini261 – 270Periplasmic10
Transmembranei271 – 307Helical; Name=VIIAdd BLAST37
Topological domaini308 – 311Cytoplasmic4
Transmembranei312 – 326Helical; Name=VIIIAdd BLAST15
Topological domaini327 – 340PeriplasmicAdd BLAST14
Transmembranei341 – 369Helical; Name=IXAdd BLAST29
Topological domaini370 – 377Cytoplasmic8
Transmembranei378 – 409Helical; Name=XAdd BLAST32
Topological domaini410 – 412Periplasmic3
Transmembranei413 – 445Helical; Name=XIAdd BLAST33
Topological domaini446 – 448Cytoplasmic3
Transmembranei449 – 477Helical; Name=XIIAdd BLAST29
Topological domaini478 – 489PeriplasmicAdd BLAST12
Transmembranei490 – 521Helical; Name=XIIIAdd BLAST32
Topological domaini522 – 587CytoplasmicAdd BLAST66
Transmembranei588 – 606Helical; Name=XIVAdd BLAST19
Topological domaini607 – 613Periplasmic7
Transmembranei614 – 632Helical; Name=XVAdd BLAST19
Topological domaini633 – 663CytoplasmicAdd BLAST31

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Increased reduction of the ubiquinone pool (in aerobically grown minimal medium with glucose).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi54H → A: 50% quinol oxidase activity. 1 Publication1
Mutagenesisi55K → Q: No effect. 1 Publication1
Mutagenesisi71R → H: No quinol oxidase activity. 2 Publications1
Mutagenesisi71R → Q or L: Abolishes quinol oxidase activity. 2 Publications1
Mutagenesisi75D → E: Very similar to wild-type. 3 Publications1
Mutagenesisi75D → H: No quinol oxidase activity, altered binding of a semiquinone intermediate at the QH site. 3 Publications1
Mutagenesisi75D → N: Abolishes quinol oxidase activity. 3 Publications1
Mutagenesisi80R → Q: Abolishes quinol oxidase activity. 1 Publication1
Mutagenesisi98H → F: About 1% quinol oxidase activity. 2 Publications1
Mutagenesisi98H → N: Abolishes enzyme activity. 2 Publications1
Mutagenesisi101Q → N: Reduces quinol oxidase activity by 75%, decreased affinity for ubiquinol-1. 1 Publication1
Mutagenesisi102I → W: No quinol oxidase activity. 1 Publication1
Mutagenesisi106H → A: 2% quinol oxidase activity, loss of heme b, loss of heme o, loss of Cu(B). 1 Publication1
Mutagenesisi135D → N: Abolishes quinol oxidase activity. 1 Publication1
Mutagenesisi173Y → F: No effect. 1 Publication1
Mutagenesisi188D → N: No effect. 1 Publication1
Mutagenesisi256D → N: No effect. 1
Mutagenesisi257R → Q: Abolishes quinol oxidase activity. 1
Mutagenesisi284H → A: 1% quinol oxidase activity, loss of heme o. 1 Publication1
Mutagenesisi286E → Q or D: Great decrease in quinol oxidase activity. 1 Publication1
Mutagenesisi288Y → F: Great decrease in activity, 100-fold decrease in heme b-to-heme o electron transfer. 1 Publication1
Mutagenesisi333H → A: 2% quinol oxidase activity, loss of Cu(B). 1 Publication1
Mutagenesisi334H → A: 1% quinol oxidase activity, loss of Cu(B). 1 Publication1
Mutagenesisi362K → Q: Abolishes quinol oxidase activity, 100-fold decrease in heme b-to-heme o electron transfer. 1 Publication1
Mutagenesisi407D → N: Abolishes quinol oxidase activity. 1 Publication1
Mutagenesisi411H → A: 50% quinol oxidase activity. 1 Publication1
Mutagenesisi419H → A: 3% quinol oxidase activity, loss of heme o, loss of Cu(B). 1 Publication1
Mutagenesisi421H → A: 1% quinol oxidase activity, loss of heme b, some loss of Cu(B). 1 Publication1
Mutagenesisi481R → Q: No effect. 1
Mutagenesisi482R → Q: No effect. 1
Mutagenesisi540E → Q: Abolishes quinol oxidase activity. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001834761 – 663Cytochrome bo(3) ubiquinol oxidase subunit 1Add BLAST663

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki284 ↔ 2881'-histidyl-3'-tyrosine (His-Tyr)By similarity

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0ABI8

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P0ABI8

PRoteomics IDEntifications database

More...
PRIDEi
P0ABI8

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterooctamer of two A chains, two B chains, two C chains and two D chains.

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
P778063EBI-2932021,EBI-543661

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4259710, 271 interactors
849987, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2102 Cytochrome o ubiquinol oxidase complex

Database of interacting proteins

More...
DIPi
DIP-47943N

Protein interaction database and analysis system

More...
IntActi
P0ABI8, 3 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b0431

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1663
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P0ABI8

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0ABI8

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105BZ9 Bacteria
COG0843 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000085275

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P0ABI8

KEGG Orthology (KO)

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KOi
K02298

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0ABI8

Family and domain databases

Database of protein disorder

More...
DisProti
DP00088

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.210.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR023616 Cyt_c_oxase-like_su1_dom
IPR036927 Cyt_c_oxase-like_su1_sf
IPR000883 Cyt_C_Oxase_1
IPR023615 Cyt_c_Oxase_su1_BS
IPR014207 Cyt_c_ubiqinol_oxidase_su1

The PANTHER Classification System

More...
PANTHERi
PTHR10422 PTHR10422, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00115 COX1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01165 CYCOXIDASEI

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF81442 SSF81442, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02843 CyoB, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50855 COX1, 1 hit
PS00077 COX1_CUB, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P0ABI8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFGKLSLDAV PFHEPIVMVT IAGIILGGLA LVGLITYFGK WTYLWKEWLT
60 70 80 90 100
SVDHKRLGIM YIIVAIVMLL RGFADAIMMR SQQALASAGE AGFLPPHHYD
110 120 130 140 150
QIFTAHGVIM IFFVAMPFVI GLMNLVVPLQ IGARDVAFPF LNNLSFWFTV
160 170 180 190 200
VGVILVNVSL GVGEFAQTGW LAYPPLSGIE YSPGVGVDYW IWSLQLSGIG
210 220 230 240 250
TTLTGINFFV TILKMRAPGM TMFKMPVFTW ASLCANVLII ASFPILTVTV
260 270 280 290 300
ALLTLDRYLG THFFTNDMGG NMMMYINLIW AWGHPEVYIL ILPVFGVFSE
310 320 330 340 350
IAATFSRKRL FGYTSLVWAT VCITVLSFIV WLHHFFTMGA GANVNAFFGI
360 370 380 390 400
TTMIIAIPTG VKIFNWLFTM YQGRIVFHSA MLWTIGFIVT FSVGGMTGVL
410 420 430 440 450
LAVPGADFVL HNSLFLIAHF HNVIIGGVVF GCFAGMTYWW PKAFGFKLNE
460 470 480 490 500
TWGKRAFWFW IIGFFVAFMP LYALGFMGMT RRLSQQIDPQ FHTMLMIAAS
510 520 530 540 550
GAVLIALGIL CLVIQMYVSI RDRDQNRDLT GDPWGGRTLE WATSSPPPFY
560 570 580 590 600
NFAVVPHVHE RDAFWEMKEK GEAYKKPDHY EEIHMPKNSG AGIVIAAFST
610 620 630 640 650
IFGFAMIWHI WWLAIVGFAG MIITWIVKSF DEDVDYYVPV AEIEKLENQH
660
FDEITKAGLK NGN
Length:663
Mass (Da):74,368
Last modified:October 25, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i17357B8D44C7CF84
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
J05492 Genomic DNA Translation: AAA23632.1
U82664 Genomic DNA Translation: AAB40187.1
U00096 Genomic DNA Translation: AAC73534.1
AP009048 Genomic DNA Translation: BAE76211.1

Protein sequence database of the Protein Information Resource

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PIRi
B42226

NCBI Reference Sequences

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RefSeqi
NP_414965.1, NC_000913.3
WP_000467180.1, NZ_STEB01000007.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73534; AAC73534; b0431
BAE76211; BAE76211; BAE76211

Database of genes from NCBI RefSeq genomes

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GeneIDi
945615

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0421
eco:b0431

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1846

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05492 Genomic DNA Translation: AAA23632.1
U82664 Genomic DNA Translation: AAB40187.1
U00096 Genomic DNA Translation: AAC73534.1
AP009048 Genomic DNA Translation: BAE76211.1
PIRiB42226
RefSeqiNP_414965.1, NC_000913.3
WP_000467180.1, NZ_STEB01000007.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FFTX-ray3.50A/F1-663[»]
SMRiP0ABI8
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4259710, 271 interactors
849987, 1 interactor
ComplexPortaliCPX-2102 Cytochrome o ubiquinol oxidase complex
DIPiDIP-47943N
IntActiP0ABI8, 3 interactors
STRINGi511145.b0431

Protein family/group databases

TCDBi3.D.4.5.1 the proton-translocating cytochrome oxidase (cox) superfamily

Proteomic databases

jPOSTiP0ABI8
PaxDbiP0ABI8
PRIDEiP0ABI8

Genome annotation databases

EnsemblBacteriaiAAC73534; AAC73534; b0431
BAE76211; BAE76211; BAE76211
GeneIDi945615
KEGGiecj:JW0421
eco:b0431
PATRICifig|1411691.4.peg.1846

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

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EchoBASEi
EB0176

Phylogenomic databases

eggNOGiENOG4105BZ9 Bacteria
COG0843 LUCA
HOGENOMiHOG000085275
InParanoidiP0ABI8
KOiK02298
PhylomeDBiP0ABI8

Enzyme and pathway databases

BioCyciEcoCyc:CYOB-MONOMER
ECOL316407:JW0421-MONOMER
MetaCyc:CYOB-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0ABI8

Protein Ontology

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PROi
PR:P0ABI8

Family and domain databases

DisProtiDP00088
Gene3Di1.20.210.10, 1 hit
InterProiView protein in InterPro
IPR023616 Cyt_c_oxase-like_su1_dom
IPR036927 Cyt_c_oxase-like_su1_sf
IPR000883 Cyt_C_Oxase_1
IPR023615 Cyt_c_Oxase_su1_BS
IPR014207 Cyt_c_ubiqinol_oxidase_su1
PANTHERiPTHR10422 PTHR10422, 1 hit
PfamiView protein in Pfam
PF00115 COX1, 1 hit
PRINTSiPR01165 CYCOXIDASEI
SUPFAMiSSF81442 SSF81442, 1 hit
TIGRFAMsiTIGR02843 CyoB, 1 hit
PROSITEiView protein in PROSITE
PS50855 COX1, 1 hit
PS00077 COX1_CUB, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCYOB_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0ABI8
Secondary accession number(s): P18401, Q2MBZ5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: November 13, 2019
This is version 124 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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