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UniProtKB - P0ABJ9 (CYDA_ECOLI)

Protein

Cytochrome bd-I ubiquinol oxidase subunit 1

Gene

cydA

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

A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H2O, transferring 1 proton/electron.5 Publications

<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 ‘Function’ 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

90% inhibited by cyanide and 2-heptyl-4-hydroxyquinoline N-oxide, at 1 mM and 40 µM respectively.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

pH 7.0, 37 degrees Celsius.
  1. KM=0.1 mM for ubiquinol-11 Publication
  2. KM=0.28 mM for 2,3,5,6-tetramethyl-p-phenylenediamine1 Publication
  3. KM=0.68 mM for N,N,N',N'-tetramethyl-p-phenylenediamine1 Publication
  1. Vmax=383 µmol/min/mg enzyme for ubiquinol-11 Publication
  2. Vmax=270 µmol/min/mg enzyme for 2,3,5,6-tetramethyl-p-phenylenediamine1 Publication
  3. Vmax=126 µmol/min/mg enzyme for N,N,N',N'-tetramethyl-p-phenylenediamine1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: oxidative phosphorylation

This protein is involved in the pathway oxidative phosphorylation, which is part of Energy metabolism.
View all proteins of this organism that are known to be involved in the pathway oxidative phosphorylation and in Energy metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi19Iron (heme b595 axial ligand)Sequence analysis1
Metal bindingi186Iron (heme b558 axial ligand)1
Metal bindingi393Iron (heme b558 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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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, Transport
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:CYDA-MONOMER
MetaCyc:CYDA-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.10.3.14 2026

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi
UPA00705

Protein family/group databases

Transport Classification Database

More...TCDBi		3.D.4.3.2 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 bd-I ubiquinol oxidase subunit 1 (EC:7.1.1.72 Publications)
Alternative name(s):
Cytochrome bd-I oxidase subunit I
Cytochrome d ubiquinol oxidase subunit I
<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:cydA
Synonyms:cyd-1
Ordered Locus Names:b0733, JW0722
<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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

Organism-specific databases

Escherichia coli strain K12 genome database

More...EcoGenei		EG10173 cydA

<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

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 – 15PeriplasmicCuratedAdd BLAST15
<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>Transmembranei16 – 35HelicalCuratedAdd BLAST20
Topological domaini36 – 54CytoplasmicCuratedAdd BLAST19
Transmembranei55 – 69HelicalCuratedAdd BLAST15
Topological domaini70 – 96PeriplasmicCuratedAdd BLAST27
Transmembranei97 – 114HelicalCuratedAdd BLAST18
Topological domaini115 – 128CytoplasmicCuratedAdd BLAST14
Transmembranei129 – 146HelicalCuratedAdd BLAST18
Topological domaini147 – 186PeriplasmicCuratedAdd BLAST40
Transmembranei187 – 203HelicalCuratedAdd BLAST17
Topological domaini204 – 219CytoplasmicCuratedAdd BLAST16
Transmembranei220 – 235HelicalCuratedAdd BLAST16
Topological domaini236 – 390PeriplasmicCuratedAdd BLAST155
Transmembranei391 – 407HelicalCuratedAdd BLAST17
Topological domaini408 – 423CytoplasmicCuratedAdd BLAST16
Transmembranei424 – 441HelicalCuratedAdd BLAST18
Topological domaini442 – 472PeriplasmicCuratedAdd BLAST31
Transmembranei473 – 487HelicalCuratedAdd BLAST15
Topological domaini488 – 522CytoplasmicCuratedAdd BLAST35

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

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

A double cydA/cydB deletion shows increased sensitivity to reductant (beta-mercapoethanol).3 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>Mutagenesisi19H → L or R: Loss of cytochrome b595 and heme d, no aerobic growth, complex assembles. 1 Publication1
Mutagenesisi86H → R: No effect. 1 Publication1
Mutagenesisi126H → P: Loss of all cofactors, no aerobic growth, complex assembles. 1 Publication1
Mutagenesisi126H → R: No effect. 1 Publication1
Mutagenesisi186H → L: Loss of cytochrome b558, no aerobic growth, complex assembles, this subunit is more susceptible to proteolysis. 1 Publication1
Mutagenesisi314H → L: Grows aerobically, has altered cytochrome b/d ratio, complex assembles. 1 Publication1
Mutagenesisi314H → P: Loss of cytochrome b595 and heme d, no aerobic growth, loss of complex. 1 Publication1
Mutagenesisi393M → L: Cytochrome b558 shifts to a high spin configuration, complex assembles. Retains about 1% quinol oxidoreductase activity after purification. 1
Mutagenesisi510H → L: No effect. 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_00001839191 – 522Cytochrome bd-I ubiquinol oxidase subunit 1Add BLAST522

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-formylmethionine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Formylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P0ABJ9

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0ABJ9

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

More...PaxDbi		P0ABJ9

PRoteomics IDEntifications database

More...PRIDEi		P0ABJ9

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Under conditions of low aeration, in stationary phase (at protein level).1 Publication

<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

Heterodimer of subunits I and II. Probably interacts with CydX, and overexpressed AppX.4 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
cydBP0ABK25EBI-906928,EBI-1213195

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4263539, 372 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-268 Cytochrome bd-I ubiquinol oxidase complex

Database of interacting proteins

More...DIPi		DIP-36181N

Protein interaction database and analysis system

More...IntActi		P0ABJ9, 4 interactors

Molecular INTeraction database

More...MINTi		P0ABJ9

STRING: functional protein association networks

More...STRINGi		316385.ECDH10B_0799

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P0ABJ9

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

More...SMRi		P0ABJ9

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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

Belongs to the cytochrome ubiquinol oxidase subunit 1 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105C4M Bacteria
COG1271 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000084938

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0ABJ9

KEGG Orthology (KO)

More...KOi		K00425

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0ABJ9

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR002585 Cyt-d_ubiquinol_oxidase_su_1

The PANTHER Classification System

More...PANTHERi		PTHR30365 PTHR30365, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01654 Cyt_bd_oxida_I, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF006446 Cyt_quinol_oxidase_1, 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>.<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.

P0ABJ9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLDIVELSRL QFALTAMYHF LFVPLTLGMA FLLAIMETVY VLSGKQIYKD 
        60         70         80         90        100
MTKFWGKLFG INFALGVATG LTMEFQFGTN WSYYSHYVGD IFGAPLAIEG 
       110        120        130        140        150
LMAFFLESTF VGLFFFGWDR LGKVQHMCVT WLVALGSNLS ALWILVANGW 
       160        170        180        190        200
MQNPIASDFN FETMRMEMVS FSELVLNPVA QVKFVHTVAS GYVTGAMFIL 
       210        220        230        240        250
GISAWYMLKG RDFAFAKRSF AIAASFGMAA VLSVIVLGDE SGYEMGDVQK 
       260        270        280        290        300
TKLAAIEAEW ETQPAPAAFT LFGIPDQEEE TNKFAIQIPY ALGIIATRSV 
       310        320        330        340        350
DTPVIGLKEL MVQHEERIRN GMKAYSLLEQ LRSGSTDQAV RDQFNSMKKD 
       360        370        380        390        400
LGYGLLLKRY TPNVADATEA QIQQATKDSI PRVAPLYFAF RIMVACGFLL 
       410        420        430        440        450
LAIIALSFWS VIRNRIGEKK WLLRAALYGI PLPWIAVEAG WFVAEYGRQP 
       460        470        480        490        500
WAIGEVLPTA VANSSLTAGD LIFSMVLICG LYTLFLVAEL FLMFKFARLG 
       510        520 
PSSLKTGRYH FEQSSTTTQP AR
Length:522
Mass (Da):58,205
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:iE757442068BCFCFE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti213F → L in AAA18804 (PubMed:2843510).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
J03939 Unassigned DNA Translation: AAA18804.1
U00096 Genomic DNA Translation: AAC73827.2
AP009048 Genomic DNA Translation: BAA35399.1

NCBI Reference Sequences

More...RefSeqi		NP_415261.2, NC_000913.3
WP_000884361.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC73827; AAC73827; b0733
BAA35399; BAA35399; BAA35399

Database of genes from NCBI RefSeq genomes

More...GeneIDi		945341

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW0722
eco:b0733

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.1540

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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
J03939 Unassigned DNA Translation: AAA18804.1
U00096 Genomic DNA Translation: AAC73827.2
AP009048 Genomic DNA Translation: BAA35399.1
RefSeqiNP_415261.2, NC_000913.3
WP_000884361.1, NZ_LN832404.1

3D structure databases

ProteinModelPortaliP0ABJ9
SMRiP0ABJ9
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263539, 372 interactors
ComplexPortaliCPX-268 Cytochrome bd-I ubiquinol oxidase complex
DIPiDIP-36181N
IntActiP0ABJ9, 4 interactors
MINTiP0ABJ9
STRINGi316385.ECDH10B_0799

Protein family/group databases

TCDBi3.D.4.3.2 the proton-translocating cytochrome oxidase (cox) superfamily

Proteomic databases

EPDiP0ABJ9
jPOSTiP0ABJ9
PaxDbiP0ABJ9
PRIDEiP0ABJ9

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73827; AAC73827; b0733
BAA35399; BAA35399; BAA35399
GeneIDi945341
KEGGiecj:JW0722
eco:b0733
PATRICifig|1411691.4.peg.1540

Organism-specific databases

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

More...EchoBASEi		EB0170
EcoGeneiEG10173 cydA

Phylogenomic databases

eggNOGiENOG4105C4M Bacteria
COG1271 LUCA
HOGENOMiHOG000084938
InParanoidiP0ABJ9
KOiK00425
PhylomeDBiP0ABJ9

Enzyme and pathway databases

UniPathwayi
UPA00705

BioCyciEcoCyc:CYDA-MONOMER
MetaCyc:CYDA-MONOMER
BRENDAi1.10.3.14 2026

Miscellaneous databases

Protein Ontology

More...PROi		PR:P0ABJ9

Family and domain databases

InterProiView protein in InterPro
IPR002585 Cyt-d_ubiquinol_oxidase_su_1
PANTHERiPTHR30365 PTHR30365, 1 hit
PfamiView protein in Pfam
PF01654 Cyt_bd_oxida_I, 1 hit
PIRSFiPIRSF006446 Cyt_quinol_oxidase_1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<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 nameiCYDA_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: P0ABJ9
Secondary accession number(s): P11026, P75754, P76823
<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: January 16, 2019
This is version 114 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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