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UniProtKB - P24182 (ACCC_ECOLI)

Entry version 199 (02 Jun 2021)
Sequence version 2 (01 Feb 1994)
Previous versions | rss
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Protein

Biotin carboxylase

Gene

accC

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

This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.

<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 <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. 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 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 sitei116ATP1 Publication1
Binding sitei201ATP1 Publication1
Binding sitei236ATP1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei292Sequence analysis1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

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 functionLigase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-binding, Biotin, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:BIOTIN-CARBOXYL-MONOMER
MetaCyc:BIOTIN-CARBOXYL-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		6.3.4.14, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P24182

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:
Biotin carboxylase (EC:6.3.4.14)
Alternative name(s):
Acetyl-CoA carboxylase subunit A (EC:6.4.1.2)
Short name:
ACC
<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:accC
Synonyms:fabG
Ordered Locus Names:b3256, JW3224
<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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

<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>Mutagenesisi19R → E: Loss of homodimerization. No effect on ATP binding. 1 Publication1
Mutagenesisi23E → R: Loss of homodimerization. No effect on ATP binding. 1 Publication1
Mutagenesisi363F → A: Loss of homodimerization. No effect on ATP binding. 1 Publication1
Mutagenesisi366R → E: Loss of homodimerization. No effect on ATP binding. 1 Publication1

Chemistry databases

Drug and drug target database

More...DrugBanki		DB08314, (2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE
DB08315, 2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE
DB08074, 3-(3-Methyl-2-buten-1-yl)-3H-purin-6-amine
DB08075, 4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine
DB08076, 4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine
DB08316, 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one
DB08317, 5-methyl-6-phenylquinazoline-2,4-diamine
DB08144, 6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
DB08145, 6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE
DB08318, 6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine
DB08146, 7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine

<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_00001467911 – 449Biotin carboxylaseAdd BLAST449

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P24182

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

More...PaxDbi		P24182

PRoteomics IDEntifications database

More...PRIDEi		P24182

<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 of biotin carboxyl carrier protein, biotin carboxylase and the two subunits of carboxyl transferase in a 2:2 complex.

2 Publications

<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		4262456, 269 interactors
852073, 6 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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

Database of interacting proteins

More...DIPi		DIP-9035N

Protein interaction database and analysis system

More...IntActi		P24182, 20 interactors

STRING: functional protein association networks

More...STRINGi		511145.b3256

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P24182

<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

1449
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		P24182

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		P24182

<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>Domaini1 – 445Biotin carboxylationAdd BLAST445
Domaini120 – 317ATP-graspPROSITE-ProRule annotationAdd BLAST198

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0439, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000395_3_2_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P24182

Database for complete collections of gene phylogenies

More...PhylomeDBi		P24182

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.1490.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR004549, Acetyl_CoA_COase_biotin_COase
IPR011761, ATP-grasp
IPR013815, ATP_grasp_subdomain_1
IPR005481, BC-like_N
IPR011764, Biotin_carboxylation_dom
IPR005482, Biotin_COase_C
IPR005479, CbamoylP_synth_lsu-like_ATP-bd
IPR016185, PreATP-grasp_dom_sf
IPR011054, Rudment_hybrid_motif

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02785, Biotin_carb_C, 1 hit
PF00289, Biotin_carb_N, 1 hit
PF02786, CPSase_L_D2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00878, Biotin_carb_C, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51246, SSF51246, 1 hit
SSF52440, SSF52440, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00514, accC, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50975, ATP_GRASP, 1 hit
PS50979, BC, 1 hit
PS00866, CPSASE_1, 1 hit
PS00867, CPSASE_2, 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.

P24182-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLDKIVIANR GEIALRILRA CKELGIKTVA VHSSADRDLK HVLLADETVC 
        60         70         80         90        100
IGPAPSVKSY LNIPAIISAA EITGAVAIHP GYGFLSENAN FAEQVERSGF 
       110        120        130        140        150
IFIGPKAETI RLMGDKVSAI AAMKKAGVPC VPGSDGPLGD DMDKNRAIAK 
       160        170        180        190        200
RIGYPVIIKA SGGGGGRGMR VVRGDAELAQ SISMTRAEAK AAFSNDMVYM 
       210        220        230        240        250
EKYLENPRHV EIQVLADGQG NAIYLAERDC SMQRRHQKVV EEAPAPGITP 
       260        270        280        290        300
ELRRYIGERC AKACVDIGYR GAGTFEFLFE NGEFYFIEMN TRIQVEHPVT 
       310        320        330        340        350
EMITGVDLIK EQLRIAAGQP LSIKQEEVHV RGHAVECRIN AEDPNTFLPS 
       360        370        380        390        400
PGKITRFHAP GGFGVRWESH IYAGYTVPPY YDSMIGKLIC YGENRDVAIA 
       410        420        430        440 
RMKNALQELI IDGIKTNVDL QIRIMNDENF QHGGTNIHYL EKKLGLQEK
Length:449
Mass (Da):49,321
Last modified:February 1, 1994 - v2
<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:i68C55F10ACB4F170
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 conflicti136G → A (PubMed:2575489).Curated1
Sequence conflicti160A → P (PubMed:2575489).Curated1
Sequence conflicti260 – 261CA → SR (PubMed:1370469).Curated2
Sequence conflicti313L → M in AAA23748 (PubMed:1682920).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
M79446 Genomic DNA Translation: AAA23748.1
M80458 Genomic DNA Translation: AAA23409.1
M83198 Genomic DNA Translation: AAA23746.1
U18997 Genomic DNA Translation: AAA58059.1
U00096 Genomic DNA Translation: AAC76288.1
AP009048 Genomic DNA Translation: BAE77297.1
M32214 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

More...PIRi		JS0632

NCBI Reference Sequences

More...RefSeqi		NP_417722.1, NC_000913.3
WP_000884639.1, NZ_STEB01000012.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76288; AAC76288; b3256
BAE77297; BAE77297; BAE77297

Database of genes from NCBI RefSeq genomes

More...GeneIDi		61730792
947761

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3224
eco:b3256

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|511145.12.peg.3355

<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
M79446 Genomic DNA Translation: AAA23748.1
M80458 Genomic DNA Translation: AAA23409.1
M83198 Genomic DNA Translation: AAA23746.1
U18997 Genomic DNA Translation: AAA58059.1
U00096 Genomic DNA Translation: AAC76288.1
AP009048 Genomic DNA Translation: BAE77297.1
M32214 Genomic DNA No translation available.
PIRiJS0632
RefSeqiNP_417722.1, NC_000913.3
WP_000884639.1, NZ_STEB01000012.1

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
1BNCX-ray2.40A/B1-449[»]
1DV1X-ray1.90A/B1-449[»]
1DV2X-ray2.50A/B1-449[»]
1K69model-A1-447[»]
2GPSX-ray2.80A/B1-449[»]
2GPWX-ray2.20A/B/C/D1-449[»]
2J9GX-ray2.05A/B1-449[»]
2V58X-ray2.10A/B1-449[»]
2V59X-ray2.40A/B1-449[»]
2V5AX-ray2.31A/B1-449[»]
2VR1X-ray2.60A/B1-449[»]
2W6MX-ray2.00A/B1-449[»]
2W6NX-ray1.87A/B1-449[»]
2W6OX-ray2.50A/C1-449[»]
2W6PX-ray1.85A/B1-449[»]
2W6QX-ray2.05A/B1-449[»]
2W6ZX-ray1.90A/B1-449[»]
2W70X-ray1.77A/B1-449[»]
2W71X-ray1.99A/C1-449[»]
3G8CX-ray2.00A/B1-444[»]
3G8DX-ray1.90A/B1-444[»]
3JZFX-ray2.13A/B1-449[»]
3JZIX-ray2.31A/B1-449[»]
3RUPX-ray1.99A/B1-449[»]
3RV3X-ray1.91A/B1-449[»]
3RV4X-ray1.98A1-449[»]
4HR7X-ray2.50A/C/E/F1-449[»]
6OI9X-ray2.06A/B1-449[»]
SMRiP24182
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4262456, 269 interactors
852073, 6 interactors
ComplexPortaliCPX-3206, Acetyl-CoA carboxylase complex
DIPiDIP-9035N
IntActiP24182, 20 interactors
STRINGi511145.b3256

Chemistry databases

BindingDBiP24182
DrugBankiDB08314, (2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE
DB08315, 2-AMINO-N,N-BIS(PHENYLMETHYL)-1,3-OXAZOLE-5-CARBOXAMIDE
DB08074, 3-(3-Methyl-2-buten-1-yl)-3H-purin-6-amine
DB08075, 4-(2-amino-1,3-thiazol-4-yl)pyrimidin-2-amine
DB08076, 4-[1-(2,6-dichlorobenzyl)-2-methyl-1H-imidazol-4-yl]pyrimidin-2-amine
DB08316, 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one
DB08317, 5-methyl-6-phenylquinazoline-2,4-diamine
DB08144, 6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
DB08145, 6-(2,6-DIMETHOXYPHENYL)PYRIDO[2,3-D]PYRIMIDINE-2,7-DIAMINE
DB08318, 6-(2-phenoxyethoxy)-1,3,5-triazine-2,4-diamine
DB08146, 7-(2,5-dihydropyrrol-1-yl)-6-phenyl-pyrido[6,5-d]pyrimidin-2-amine

Proteomic databases

jPOSTiP24182
PaxDbiP24182
PRIDEiP24182

Genome annotation databases

EnsemblBacteriaiAAC76288; AAC76288; b3256
BAE77297; BAE77297; BAE77297
GeneIDi61730792
947761
KEGGiecj:JW3224
eco:b3256
PATRICifig|511145.12.peg.3355

Organism-specific databases

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

More...EchoBASEi		EB0272

Phylogenomic databases

eggNOGiCOG0439, Bacteria
HOGENOMiCLU_000395_3_2_6
InParanoidiP24182
PhylomeDBiP24182

Enzyme and pathway databases

UniPathwayiUPA00655;UER00711
BioCyciEcoCyc:BIOTIN-CARBOXYL-MONOMER
MetaCyc:BIOTIN-CARBOXYL-MONOMER
BRENDAi6.3.4.14, 2026
SABIO-RKiP24182

Miscellaneous databases

EvolutionaryTraceiP24182

Protein Ontology

More...PROi		PR:P24182

Family and domain databases

Gene3Di3.30.1490.20, 1 hit
InterProiView protein in InterPro
IPR004549, Acetyl_CoA_COase_biotin_COase
IPR011761, ATP-grasp
IPR013815, ATP_grasp_subdomain_1
IPR005481, BC-like_N
IPR011764, Biotin_carboxylation_dom
IPR005482, Biotin_COase_C
IPR005479, CbamoylP_synth_lsu-like_ATP-bd
IPR016185, PreATP-grasp_dom_sf
IPR011054, Rudment_hybrid_motif
PfamiView protein in Pfam
PF02785, Biotin_carb_C, 1 hit
PF00289, Biotin_carb_N, 1 hit
PF02786, CPSase_L_D2, 1 hit
SMARTiView protein in SMART
SM00878, Biotin_carb_C, 1 hit
SUPFAMiSSF51246, SSF51246, 1 hit
SSF52440, SSF52440, 1 hit
TIGRFAMsiTIGR00514, accC, 1 hit
PROSITEiView protein in PROSITE
PS50975, ATP_GRASP, 1 hit
PS50979, BC, 1 hit
PS00866, CPSASE_1, 1 hit
PS00867, CPSASE_2, 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 nameiACCC_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: P24182
Secondary accession number(s): Q2M8V9
<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: March 1, 1992
Last sequence update: February 1, 1994
Last modified: June 2, 2021
This is version 199 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

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