Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
We will be switching to the new UniProt website soon. Please explore and share your feedback. Take me to the new website.

UniProtKB - P0A6I6 (COAD_ECOLI)

Entry version 138 (23 Feb 2022)
Sequence version 1 (29 Mar 2005)
Previous versions | rss
Add a publicationFeedback
Protein

Phosphopantetheine adenylyltransferase

Gene

coaD

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

Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate (PubMed:10480925, PubMed:17873050).

CoA is not a substrate for the enzyme (PubMed:10480925).

UniRule annotation2 Publications

Miscellaneous

The crystal structures in complex with substrates suggest the enzyme stabilizes the transition state but the functional groups of the enzyme are not directly involved in reaction catalysis.1 Publication

Caution

Was originally thought to have an essential function in lipopolysaccharide biosynthesis.1 Publication

<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

Mg2+1 PublicationNote: Crystallized in the absence of Mg2+, the catalytic metal is not bound by the protein but probably by non-esterified oxygen atoms from ATP and/or ordered H(2)O (PubMed:11812124).1 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

Feedback inhibited by CoA, which is competitive with ATP, 4'-phosphopantetheine and 3'-dephospho-CoA (PubMed:17873050, PubMed:10480925). Binds 0.5 CoA tightly per monomer in the same position as 3'-dephospho-CoA but in a different fashion (PubMed:12837781, PubMed:17873050). Is inhibited by the very potent and specific inhibitor PTX042695 dipeptide, with an IC50 of 6 nM, a compound which has no activity against porcine PPAT (PubMed:12750020). A series of pyrazoloquinolones were also characterized as ATP-competitive inhibitors of PPAT (PubMed:20486930).1 Publication4 Publications

<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

kcat is 1.37 sec(-1) for the forward reaction, with ATP and pantetheine 4'-phosphate as substrates (PubMed:17873050). kcat is 3.3 sec(-1) for the reverse reaction, with diphosphate and 3'-dephospho-CoA as substrates (PubMed:10480925). kcat is 1.37 sec(-1) for the reverse reaction, with diphosphate and 3'-dephospho-CoA as substrates (PubMed:17873050).2 Publications
  1. KM=7.0 µM for 3'-dephospho-CoA1 Publication
  2. KM=17.0 µM for 3'-dephospho-CoA1 Publication
  3. KM=0.22 mM for diphosphate1 Publication
  4. KM=0.23 mM for diphosphate1 Publication
  5. KM=220 µM for ATP1 Publication
  6. KM=4.7 µM for 4'-phosphopantetheine1 Publication

pH dependencei

Optimum pH is 6.9.1 Publication

<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: coenzyme A biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes CoA from (R)-pantothenate.UniRule annotation 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 <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 sitei10SubstrateCombined sources2 Publications1
Binding sitei18ATPCombined sources1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei18Transition state stabilizer1 Publication1
Binding sitei42SubstrateCombined sources2 Publications1
Binding sitei74Substrate; via amide nitrogenCombined sources2 Publications1
Binding sitei88SubstrateCombined sources1 Publication1
Binding sitei99ATPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi7 – 11ATPCombined sources1 Publication5
Nucleotide bindingi89 – 91ATPCombined sources1 Publication3
Nucleotide bindingi124 – 130ATPCombined sources1 Publication7

<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 functionNucleotidyltransferase, Transferase
Biological processCoenzyme A biosynthesis
LigandATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:PANTEPADENYLYLTRAN-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.7.3, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P0A6I6

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

More...UniPathwayi		UPA00241;UER00355

<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:
Phosphopantetheine adenylyltransferase1 PublicationUniRule annotation (EC:2.7.7.3UniRule annotation2 Publications)
Alternative name(s):
Dephospho-CoA pyrophosphorylaseUniRule annotation
Pantetheine-phosphate adenylyltransferaseUniRule annotation
Short name:
PPAT1 PublicationUniRule 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:coaD1 PublicationUniRule annotation
Synonyms:kdtB1 Publication, yicA
Ordered Locus Names:b3634, JW3609
<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

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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4523175

<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_00001562041 – 159Phosphopantetheine adenylyltransferaseAdd BLAST159

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0A6I6

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

More...PaxDbi		P0A6I6

PRoteomics IDEntifications database

More...PRIDEi		P0A6I6

<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

Homohexamer, a dimerized trimer with a solvent channel through the middle (PubMed:10480925, PubMed:10205156, PubMed:11812124, PubMed:12837781, PubMed:17873050). In crystals only 1 trimer is seen to bind substrate/product at a time (PubMed:10205156, PubMed:11812124).

5 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

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4263379, 238 interactors

Database of interacting proteins

More...DIPi		DIP-35966N

Protein interaction database and analysis system

More...IntActi		P0A6I6, 10 interactors

STRING: functional protein association networks

More...STRINGi		511145.b3634

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P0A6I6

<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

1159
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		P0A6I6

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		P0A6I6

<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 bacterial CoaD family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0669, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_100149_0_1_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A6I6

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A6I6

Family and domain databases

Conserved Domains Database

More...CDDi		cd02163, PPAT, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.620, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00151, PPAT_bact, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR004821, Cyt_trans-like
IPR001980, PPAT
IPR014729, Rossmann-like_a/b/a_fold

The PANTHER Classification System

More...PANTHERi		PTHR21342:SF1, PTHR21342:SF1, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01467, CTP_transf_like, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01020, LPSBIOSNTHSS

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01510, coaD_prev_kdtB, 1 hit
TIGR00125, cyt_tran_rel, 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.

P0A6I6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQKRAIYPGT FDPITNGHID IVTRATQMFD HVILAIAASP SKKPMFTLEE 
        60         70         80         90        100
RVALAQQATA HLGNVEVVGF SDLMANFARN QHATVLIRGL RAVADFEYEM 
       110        120        130        140        150
QLAHMNRHLM PELESVFLMP SKEWSFISSS LVKEVARHQG DVTHFLPENV 

HQALMAKLA
Length:159
Mass (Da):17,837
Last modified:March 29, 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:iC4D7B8715A061B91
GO

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
M60670 Genomic DNA Translation: AAA24044.1
M86305 Genomic DNA Translation: AAA03746.1
U00039 Genomic DNA Translation: AAB18611.1
U00096 Genomic DNA Translation: AAC76658.1
AP009048 Genomic DNA Translation: BAE77658.1

Protein sequence database of the Protein Information Resource

More...PIRi		JU0468

NCBI Reference Sequences

More...RefSeqi		NP_418091.1, NC_000913.3
WP_001171866.1, NZ_STEB01000024.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76658; AAC76658; b3634
BAE77658; BAE77658; BAE77658

Database of genes from NCBI RefSeq genomes

More...GeneIDi		67417636
947386

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3609
eco:b3634

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.3072

<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
M60670 Genomic DNA Translation: AAA24044.1
M86305 Genomic DNA Translation: AAA03746.1
U00039 Genomic DNA Translation: AAB18611.1
U00096 Genomic DNA Translation: AAC76658.1
AP009048 Genomic DNA Translation: BAE77658.1
PIRiJU0468
RefSeqiNP_418091.1, NC_000913.3
WP_001171866.1, NZ_STEB01000024.1

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
1B6TX-ray1.80A/B1-159[»]
1GN8X-ray1.83A/B1-159[»]
1H1TX-ray1.78A/B1-159[»]
1QJCX-ray1.63A/B2-159[»]
5JBNX-ray1.45A/B1-159[»]
6B7AX-ray1.99A/B1-159[»]
6B7BX-ray1.98A/B1-159[»]
6B7CX-ray1.56A/B1-159[»]
6B7DX-ray1.80A/B1-159[»]
6B7EX-ray2.10A/B1-159[»]
6B7FX-ray2.56A/B1-159[»]
6CCKX-ray1.61A/B1-159[»]
6CCLX-ray1.77A/B1-159[»]
6CCMX-ray1.79A/B1-159[»]
6CCNX-ray1.87A/B1-159[»]
6CCOX-ray1.82A/B1-159[»]
6CCQX-ray1.92A/B1-159[»]
6CCSX-ray2.06A/B1-159[»]
6CHLX-ray2.20A/B1-159[»]
6CHMX-ray2.28A/B1-159[»]
6CHNX-ray2.03A/B1-159[»]
6CHOX-ray1.85A/B1-159[»]
6CHPX-ray1.94A/B1-159[»]
6CHQX-ray1.79A/B1-159[»]
6CKWX-ray2.06A/B1-159[»]
SMRiP0A6I6
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4263379, 238 interactors
DIPiDIP-35966N
IntActiP0A6I6, 10 interactors
STRINGi511145.b3634

Chemistry databases

BindingDBiP0A6I6
ChEMBLiCHEMBL4523175

Proteomic databases

jPOSTiP0A6I6
PaxDbiP0A6I6
PRIDEiP0A6I6

Genome annotation databases

EnsemblBacteriaiAAC76658; AAC76658; b3634
BAE77658; BAE77658; BAE77658
GeneIDi67417636
947386
KEGGiecj:JW3609
eco:b3634
PATRICifig|1411691.4.peg.3072

Organism-specific databases

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

More...EchoBASEi		EB1176

Phylogenomic databases

eggNOGiCOG0669, Bacteria
HOGENOMiCLU_100149_0_1_6
InParanoidiP0A6I6
PhylomeDBiP0A6I6

Enzyme and pathway databases

UniPathwayiUPA00241;UER00355
BioCyciEcoCyc:PANTEPADENYLYLTRAN-MONOMER
BRENDAi2.7.7.3, 2026
SABIO-RKiP0A6I6

Miscellaneous databases

EvolutionaryTraceiP0A6I6

Protein Ontology

More...PROi		PR:P0A6I6

Family and domain databases

CDDicd02163, PPAT, 1 hit
Gene3Di3.40.50.620, 1 hit
HAMAPiMF_00151, PPAT_bact, 1 hit
InterProiView protein in InterPro
IPR004821, Cyt_trans-like
IPR001980, PPAT
IPR014729, Rossmann-like_a/b/a_fold
PANTHERiPTHR21342:SF1, PTHR21342:SF1, 1 hit
PfamiView protein in Pfam
PF01467, CTP_transf_like, 1 hit
PRINTSiPR01020, LPSBIOSNTHSS
TIGRFAMsiTIGR01510, coaD_prev_kdtB, 1 hit
TIGR00125, cyt_tran_rel, 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 nameiCOAD_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: P0A6I6
Secondary accession number(s): P23875, Q2M7U8
<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 29, 2005
Last sequence update: March 29, 2005
Last modified: February 23, 2022
This is version 138 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, 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
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again