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UniProtKB - P0ABQ0 (COABC_ECOLI)

Protein

Coenzyme A biosynthesis bifunctional protein CoaBC

Gene

coaBC

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

Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine (PubMed:11278255). In the second the latter compound is decarboxylated to form 4'-phosphopantotheine (PubMed:10922366).2 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 <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: coenzyme A biosynthesis

This protein is involved in step 2 and 3 of the subpathway that synthesizes CoA from (R)-pantothenate.1 Publication
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Pantothenate kinase (coaA)
  2. Coenzyme A biosynthesis bifunctional protein CoaBC (coaBC)
  3. Coenzyme A biosynthesis bifunctional protein CoaBC (coaBC)
  4. Phosphopantetheine adenylyltransferase (coaD)
  5. Dephospho-CoA kinase (coaE)
This subpathway is part of the pathway coenzyme A biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CoA from (R)-pantothenate, the pathway coenzyme A biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei125SubstrateBy similarity1
<p>This subsection of the ‘Function’ 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 sitei158Proton donorCurated1
Binding sitei279CTPCombined sources1 Publication1
Binding sitei289CTPCombined sources1 Publication1
Binding sitei327CTP; via amide nitrogenCombined sources1 Publication1
Binding sitei341CTPCombined sources1 Publication1
Binding sitei345CTPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi273 – 275CTPCombined sources1 Publication3
Nucleotide bindingi308 – 311CTPCombined sources1 Publication4

<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 functionDecarboxylase, Ligase, Lyase, Multifunctional enzyme
LigandFlavoprotein, FMN, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10004-MONOMER
MetaCyc:EG10004-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		6.3.2.5 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P0ABQ0

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

More...UniPathwayi
UPA00241;UER00353

UPA00241;UER00354

<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:
Coenzyme A biosynthesis bifunctional protein CoaBC
Alternative name(s):
DNA/pantothenate metabolism flavoprotein
Including the following 2 domains:
Phosphopantothenoylcysteine decarboxylase (EC:4.1.1.361 Publication)
Short name:
PPCDC
Alternative name(s):
CoaC
Phosphopantothenate--cysteine ligase (EC:6.3.2.51 Publication)
Alternative name(s):
CoaB
PPC synthetase
Short name:
PPCS
Phosphopantothenoylcysteine synthase
<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:coaBC1 Publication
Synonyms:dfp1 Publication
Ordered Locus Names:b3639, JW5642
<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		EG10004 dfp

<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

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

<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_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>Mutagenesisi11G → D in Dfp-707; temperature-sensitive, impairs folding. 1 Publication1
Mutagenesisi14G → S: No FMN binding. 1 Publication1
Mutagenesisi15G → A: Less than 5% of wild-type activity. 1 Publication1
Mutagenesisi16I → L: Severely reduced activity. 1 Publication1
Mutagenesisi16I → V: Slightly reduced activity. 1 Publication1
Mutagenesisi17A → D: Less than 5% of wild-type activity. 1 Publication1
Mutagenesisi17A → G or S: Almost wild-type activity. 1 Publication1
Mutagenesisi19Y → F: Almost wild-type activity. 1 Publication1
Mutagenesisi19Y → L: Reduced activity. 1 Publication1
Mutagenesisi20K → N or Q: Reduced activity. 1 Publication1
Mutagenesisi20K → R: Almost wild-type activity. 1 Publication1
Mutagenesisi46F → L: Reduced activity. 1 Publication1
Mutagenesisi75H → N: Loss of activity. 1 Publication1
Mutagenesisi89P → A: Binds FMN, but more loosely than wild-type. 1 Publication1
Mutagenesisi89P → D: No FMN binding. 1 Publication1
Mutagenesisi91T → V: Binds FMN. 1 Publication1
Mutagenesisi124M → L: No effect. 1 Publication1
Mutagenesisi125N → D or Q: Loss of activity. 2 Publications1
Mutagenesisi128M → L: Severely reduced activity. 1 Publication1
Mutagenesisi158C → A or S: Loss of activity. 1
Mutagenesisi194T → V: Loss of dimerization. 1 Publication1
Mutagenesisi198T → V: Loss of dimerization. 1 Publication1
Mutagenesisi203D → N: Loss of dimerization. 1 Publication1
Mutagenesisi210N → D: Loss of activity, reaction intermediate detectable. 2 Publications1
Mutagenesisi210N → H or K: Loss of activity, reaction intermediate not detectable. 2 Publications1
Mutagenesisi212S → A: Small effect on activity. 1 Publication1
Mutagenesisi215K → Q: No effect. 1 Publication1
Mutagenesisi275A → V: Loss of dimerization. 2 Publications1
Mutagenesisi289K → Q: Loss of activity. 1 Publication1
Mutagenesisi291K → Q: Reduced activity. 1 Publication1
Mutagenesisi292K → Q: Small effect on activity. 1 Publication1

Chemistry databases

Drug and drug target database

More...DrugBanki		DB03403 Cytidine-5'-Monophosphate
DB02431 Cytidine-5'-Triphosphate

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00001820222 – 406Coenzyme A biosynthesis bifunctional protein CoaBCAdd BLAST405

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P0ABQ0

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0ABQ0

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

More...PaxDbi		P0ABQ0

PRoteomics IDEntifications database

More...PRIDEi		P0ABQ0

<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

Homododecamer, the CoaB domains form homodimers.

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4261256, 26 interactors

Database of interacting proteins

More...DIPi		DIP-48472N

Protein interaction database and analysis system

More...IntActi		P0ABQ0, 2 interactors

STRING: functional protein association networks

More...STRINGi		316385.ECDH10B_3821

<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

1406
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1U7UX-ray2.40A181-406[»]
1U7WX-ray2.50A/B/C181-406[»]
1U7ZX-ray2.30A/B/C181-406[»]
1U80X-ray2.85A/B/C181-406[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P0ABQ0

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

More...SMRi		P0ABQ0

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P0ABQ0

<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

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>Regioni2 – 188Phosphopantothenoylcysteine decarboxylaseAdd BLAST187
Regioni189 – 406Phosphopantothenate--cysteine ligaseAdd BLAST218

<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

In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily.Curated
In the C-terminal section; belongs to the PPC synthetase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105CJS Bacteria
COG0452 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000037526

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0ABQ0

KEGG Orthology (KO)

More...KOi		K13038

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0ABQ0

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.10300, 1 hit
3.40.50.1950, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR035929 CoaB-like_sf
IPR005252 CoaBC
IPR007085 DNA/pantothenate-metab_flavo_C
IPR036551 Flavin_trans-like
IPR003382 Flavoprotein

Pfam protein domain database

More...Pfami		View protein in Pfam
PF04127 DFP, 1 hit
PF02441 Flavoprotein, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF102645 SSF102645, 1 hit
SSF52507 SSF52507, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00521 coaBC_dfp, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0ABQ0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLAGKKIVL GVSGGIAAYK TPELVRRLRD RGADVRVAMT EAAKAFITPL 
        60         70         80         90        100
SLQAVSGYPV SDSLLDPAAE AAMGHIELGK WADLVILAPA TADLIARVAA 
       110        120        130        140        150
GMANDLVSTI CLATPAPVAV LPAMNQQMYR AAATQHNLEV LASRGLLIWG 
       160        170        180        190        200
PDSGSQACGD IGPGRMLDPL TIVDMAVAHF SPVNDLKHLN IMITAGPTRE 
       210        220        230        240        250
PLDPVRYISN HSSGKMGFAI AAAAARRGAN VTLVSGPVSL PTPPFVKRVD 
       260        270        280        290        300
VMTALEMEAA VNASVQQQNI FIGCAAVADY RAATVAPEKI KKQATQGDEL 
       310        320        330        340        350
TIKMVKNPDI VAGVAALKDH RPYVVGFAAE TNNVEEYARQ KRIRKNLDLI 
       360        370        380        390        400
CANDVSQPTQ GFNSDNNALH LFWQDGDKVL PLERKELLGQ LLLDEIVTRY 

DEKNRR
Length:406
Mass (Da):43,438
Last modified:January 23, 2007 - 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:iCBD11B9347E8C6AB
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA61992 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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
L10328 Genomic DNA Translation: AAA61992.1 Different initiation.
U00096 Genomic DNA Translation: AAC76663.2
AP009048 Genomic DNA Translation: BAE77653.1
V01578 Genomic DNA No translation available.

NCBI Reference Sequences

More...RefSeqi		NP_418096.4, NC_000913.3
WP_000050139.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76663; AAC76663; b3639
BAE77653; BAE77653; BAE77653

Database of genes from NCBI RefSeq genomes

More...GeneIDi		949047

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW5642
eco:b3639

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.3067

<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
L10328 Genomic DNA Translation: AAA61992.1 Different initiation.
U00096 Genomic DNA Translation: AAC76663.2
AP009048 Genomic DNA Translation: BAE77653.1
V01578 Genomic DNA No translation available.
RefSeqiNP_418096.4, NC_000913.3
WP_000050139.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U7UX-ray2.40A181-406[»]
1U7WX-ray2.50A/B/C181-406[»]
1U7ZX-ray2.30A/B/C181-406[»]
1U80X-ray2.85A/B/C181-406[»]
ProteinModelPortaliP0ABQ0
SMRiP0ABQ0
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261256, 26 interactors
DIPiDIP-48472N
IntActiP0ABQ0, 2 interactors
STRINGi316385.ECDH10B_3821

Chemistry databases

DrugBankiDB03403 Cytidine-5'-Monophosphate
DB02431 Cytidine-5'-Triphosphate

Proteomic databases

EPDiP0ABQ0
jPOSTiP0ABQ0
PaxDbiP0ABQ0
PRIDEiP0ABQ0

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76663; AAC76663; b3639
BAE77653; BAE77653; BAE77653
GeneIDi949047
KEGGiecj:JW5642
eco:b3639
PATRICifig|1411691.4.peg.3067

Organism-specific databases

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

More...EchoBASEi		EB0004
EcoGeneiEG10004 dfp

Phylogenomic databases

eggNOGiENOG4105CJS Bacteria
COG0452 LUCA
HOGENOMiHOG000037526
InParanoidiP0ABQ0
KOiK13038
PhylomeDBiP0ABQ0

Enzyme and pathway databases

UniPathwayi
UPA00241;UER00353

UPA00241;UER00354

BioCyciEcoCyc:EG10004-MONOMER
MetaCyc:EG10004-MONOMER
BRENDAi6.3.2.5 2026
SABIO-RKiP0ABQ0

Miscellaneous databases

EvolutionaryTraceiP0ABQ0

Protein Ontology

More...PROi		PR:P0ABQ0

Family and domain databases

Gene3Di3.40.50.10300, 1 hit
3.40.50.1950, 1 hit
InterProiView protein in InterPro
IPR035929 CoaB-like_sf
IPR005252 CoaBC
IPR007085 DNA/pantothenate-metab_flavo_C
IPR036551 Flavin_trans-like
IPR003382 Flavoprotein
PfamiView protein in Pfam
PF04127 DFP, 1 hit
PF02441 Flavoprotein, 1 hit
SUPFAMiSSF102645 SSF102645, 1 hit
SSF52507 SSF52507, 1 hit
TIGRFAMsiTIGR00521 coaBC_dfp, 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 nameiCOABC_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: P0ABQ0
Secondary accession number(s): P24285, P76718, Q2M7V3
<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: November 8, 2005
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 107 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, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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