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Entry version 131 (23 Feb 2022)
Sequence version 1 (19 Jul 2005)
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Protein

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

Gene

accD

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

Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO2 group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.

Controls translation of mRNA for both itself and the alpha-subunit (accA) by binding to a probable hairpin in the 5' of the mRNA. Binding to mRNA inhibits translation; this is partially relieved by acetyl-CoA. Increasing amounts of mRNA also inhibit enzyme activity.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Zn2+UniRule annotation1 PublicationNote: Binds 1 zinc ion per subunit. The zinc is involved in both translation regulation via mRNA-binding and catalysis.UniRule annotation1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 pyrrolidine dione antibiotic moiramide B (CPD1).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=40.0 µM for malonyl-CoA2 Publications
  2. KM=11.4 mM for biocytin2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: malonyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.UniRule annotation This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi27Zinc1
Metal bindingi30Zinc1
Metal bindingi46Zinc1
Metal bindingi49Zinc1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri27 – 49C4-typeCuratedAdd BLAST23

<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 functionRNA-binding, Transferase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Translation regulation
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:CARBOXYL-TRANSFERASE-BETA-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.4.1.2, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P0A9Q5

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

More...
UniPathwayi
UPA00655;UER00711

<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%5Fand%5Ftaxonomy%5Fsection">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:
Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaUniRule annotation (EC:2.1.3.15UniRule annotation)
Short name:
ACCase subunit betaUniRule annotation
Short name:
Acetyl-CoA carboxylase carboxyltransferase subunit betaUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:accDUniRule annotation
Synonyms:dedB, usg
Ordered Locus Names:b2316, JW2313
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

Keywords - Cellular componenti

Cytoplasm

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi27C → A: Vmax decreases 9-fold. 1 Publication1
Mutagenesisi30C → A: Vmax decreases 140-fold. Loss of nucleic acid-binding. 1 Publication1
Mutagenesisi46C → A: Vmax decreases 11-fold. 1 Publication1
Mutagenesisi49C → A: Vmax decreases 8-fold. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001997701 – 304Acetyl-coenzyme A carboxylase carboxyl transferase subunit betaAdd BLAST304

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A9Q5

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

More...
PaxDbi
P0A9Q5

PRoteomics IDEntifications database

More...
PRIDEi
P0A9Q5

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD).

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4261361, 233 interactors
851137, 11 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-3206, Acetyl-CoA carboxylase complex

Database of interacting proteins

More...
DIPi
DIP-35878N

Protein interaction database and analysis system

More...
IntActi
P0A9Q5, 28 interactors

Molecular INTeraction database

More...
MINTi
P0A9Q5

STRING: functional protein association networks

More...
STRINGi
511145.b2316

<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

1304
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

More...
SMRi
P0A9Q5

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
P0A9Q5

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini23 – 292CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST270

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni284 – 304DisorderedSequence analysisAdd BLAST21

<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 AccD/PCCB family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri27 – 49C4-typeCuratedAdd BLAST23

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0777, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_015486_1_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A9Q5

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A9Q5

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_01395, AcetylCoA_CT_beta, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR034733, AcCoA_carboxyl
IPR000438, Acetyl_CoA_COase_Trfase_b_su
IPR029045, ClpP/crotonase-like_dom_sf
IPR011762, COA_CT_N
IPR041010, Znf-ACC

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01039, Carboxyl_trans, 1 hit
PF17848, zf-ACC, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01070, ACCCTRFRASEB

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52096, SSF52096, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00515, accD, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50980, COA_CT_NTER, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P0A9Q5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSWIERIKSN ITPTRKASIP EGVWTKCDSC GQVLYRAELE RNLEVCPKCD
60 70 80 90 100
HHMRMTARNR LHSLLDEGSL VELGSELEPK DVLKFRDSKK YKDRLASAQK
110 120 130 140 150
ETGEKDALVV MKGTLYGMPV VAAAFEFAFM GGSMGSVVGA RFVRAVEQAL
160 170 180 190 200
EDNCPLICFS ASGGARMQEA LMSLMQMAKT SAALAKMQER GLPYISVLTD
210 220 230 240 250
PTMGGVSASF AMLGDLNIAE PKALIGFAGP RVIEQTVREK LPPGFQRSEF
260 270 280 290 300
LIEKGAIDMI VRRPEMRLKL ASILAKLMNL PAPNPEAPRE GVVVPPVPDQ

EPEA
Length:304
Mass (Da):33,322
Last modified:July 19, 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:i401FEC94D728F3CB
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 conflicti76 – 77EL → SV in AAA23965 (PubMed:3040734).Curated2
Sequence conflicti225 – 239IGFAG…QTVRE → MALPVRVLSNRPFAK in AAA23807 (PubMed:3040739).CuratedAdd BLAST15
Sequence conflicti225 – 239IGFAG…QTVRE → MALPVRVLSNRPFAK in AAA23801 (PubMed:3040739).CuratedAdd BLAST15
Sequence conflicti226 – 235GFAGPRVIEQ → ALPVRVLSNR in AAA23965 (PubMed:3040734).Curated10

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
M32445 Genomic DNA Translation: AAA23807.1
J02808 Genomic DNA Translation: AAA23801.1
M68934 Genomic DNA Translation: AAA23965.1
U00096 Genomic DNA Translation: AAC75376.1
AP009048 Genomic DNA Translation: BAA16173.1
S53037 mRNA Translation: AAB24894.2

Protein sequence database of the Protein Information Resource

More...
PIRi
B65004, XMECBD

NCBI Reference Sequences

More...
RefSeqi
NP_416819.1, NC_000913.3
WP_000118404.1, NZ_STEB01000008.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75376; AAC75376; b2316
BAA16173; BAA16173; BAA16173

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
66673801
946796

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2313
eco:b2316

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|511145.12.peg.2411

<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
M32445 Genomic DNA Translation: AAA23807.1
J02808 Genomic DNA Translation: AAA23801.1
M68934 Genomic DNA Translation: AAA23965.1
U00096 Genomic DNA Translation: AAC75376.1
AP009048 Genomic DNA Translation: BAA16173.1
S53037 mRNA Translation: AAB24894.2
PIRiB65004, XMECBD
RefSeqiNP_416819.1, NC_000913.3
WP_000118404.1, NZ_STEB01000008.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F9YX-ray3.20B1-304[»]
SMRiP0A9Q5
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261361, 233 interactors
851137, 11 interactors
ComplexPortaliCPX-3206, Acetyl-CoA carboxylase complex
DIPiDIP-35878N
IntActiP0A9Q5, 28 interactors
MINTiP0A9Q5
STRINGi511145.b2316

Proteomic databases

jPOSTiP0A9Q5
PaxDbiP0A9Q5
PRIDEiP0A9Q5

Genome annotation databases

EnsemblBacteriaiAAC75376; AAC75376; b2316
BAA16173; BAA16173; BAA16173
GeneIDi66673801
946796
KEGGiecj:JW2313
eco:b2316
PATRICifig|511145.12.peg.2411

Organism-specific databases

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

More...
EchoBASEi
EB0213

Phylogenomic databases

eggNOGiCOG0777, Bacteria
HOGENOMiCLU_015486_1_0_6
InParanoidiP0A9Q5
PhylomeDBiP0A9Q5

Enzyme and pathway databases

UniPathwayiUPA00655;UER00711
BioCyciEcoCyc:CARBOXYL-TRANSFERASE-BETA-MONOMER
BRENDAi6.4.1.2, 2026
SABIO-RKiP0A9Q5

Miscellaneous databases

EvolutionaryTraceiP0A9Q5

Protein Ontology

More...
PROi
PR:P0A9Q5

Family and domain databases

HAMAPiMF_01395, AcetylCoA_CT_beta, 1 hit
InterProiView protein in InterPro
IPR034733, AcCoA_carboxyl
IPR000438, Acetyl_CoA_COase_Trfase_b_su
IPR029045, ClpP/crotonase-like_dom_sf
IPR011762, COA_CT_N
IPR041010, Znf-ACC
PfamiView protein in Pfam
PF01039, Carboxyl_trans, 1 hit
PF17848, zf-ACC, 1 hit
PRINTSiPR01070, ACCCTRFRASEB
SUPFAMiSSF52096, SSF52096, 1 hit
TIGRFAMsiTIGR00515, accD, 1 hit
PROSITEiView protein in PROSITE
PS50980, COA_CT_NTER, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiACCD_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: P0A9Q5
Secondary accession number(s): P08193, P76937, P78251
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 19, 2005
Last modified: February 23, 2022
This is version 131 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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