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UniProtKB - P0A6I6 (COAD_ECOLI)

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_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

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 ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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_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 4 of the subpathway that synthesizes CoA from (R)-pantothenate.UniRule annotation
    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 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 ‘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 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

    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 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
    MetaCyc: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_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:
    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_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: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_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    		EG11190 coaD

    <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 ...

    Keywords - Cellular componenti

    Cytoplasm

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001562041 – 159Phosphopantetheine adenylyltransferaseAdd BLAST159

    Proteomic databases

    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_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

    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_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    rplDP607232EBI-553173,EBI-545597

    GO - Molecular functioni

    View the 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    		316385.ECDH10B_3816

    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

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...    ProteinModelPortali    		P0A6I6

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

    More...    SMRi    		P0A6I6

    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    		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    		ENOG4108ZEF Bacteria
    COG0669 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000006518

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P0A6I6

    KEGG Orthology (KO)

    More...    KOi    		K00954

    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_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.

    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_LN832404.1

    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    		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_LN832404.1

    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[»]
    ProteinModelPortaliP0A6I6
    SMRiP0A6I6
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4263379, 238 interactors
    DIPiDIP-35966N
    IntActiP0A6I6, 10 interactors
    STRINGi316385.ECDH10B_3816

    Chemistry databases

    BindingDBiP0A6I6

    Proteomic databases

    PaxDbiP0A6I6
    PRIDEiP0A6I6

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76658; AAC76658; b3634
    BAE77658; BAE77658; BAE77658
    GeneIDi947386
    KEGGiecj:JW3609
    eco:b3634
    PATRICifig|1411691.4.peg.3072

    Organism-specific databases

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

    More...    EchoBASEi    		EB1176
    EcoGeneiEG11190 coaD

    Phylogenomic databases

    eggNOGiENOG4108ZEF Bacteria
    COG0669 LUCA
    HOGENOMiHOG000006518
    InParanoidiP0A6I6
    KOiK00954
    PhylomeDBiP0A6I6

    Enzyme and pathway databases

    UniPathwayi
    UPA00241;UER00355

    BioCyciEcoCyc:PANTEPADENYLYLTRAN-MONOMER
    MetaCyc: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

    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 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_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: March 29, 2005
    Last sequence update: March 29, 2005
    Last modified: December 5, 2018
    This is version 120 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, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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