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UniProtKB - P77398 (ARNA_ECOLI)

Entry version 178 (12 Aug 2020)
Sequence version 1 (01 Feb 1997)
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Protein

Bifunctional polymyxin resistance protein ArnA

Gene

arnA

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

Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.2 Publications

<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 describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.76 mM for NAD1 Publication
  2. KM=0.086 mM for UDP-GlcUA1 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: UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis

    This protein is involved in step 1 and 3 of the subpathway that synthesizes UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate.1 Publication
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Bifunctional polymyxin resistance protein ArnA (arnA), Bifunctional polymyxin resistance protein ArnA (arnA)
    2. UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase (arnB), UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase (arnB)
    3. Bifunctional polymyxin resistance protein ArnA (arnA), Bifunctional polymyxin resistance protein ArnA (arnA)
    This subpathway is part of the pathway UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate, the pathway UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis and in Nucleotide-sugar biosynthesis.

    Pathwayi: lipopolysaccharide biosynthesis

    This protein is involved in the pathway lipopolysaccharide biosynthesis, which is part of Bacterial outer membrane biogenesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway lipopolysaccharide biosynthesis and in Bacterial outer membrane biogenesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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>Sitei102Transition state stabilizer1
    <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 sitei104Proton donor; for formyltransferase activity1
    <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 sitei11410-formyltetrahydrofolate1
    Sitei140Raises pKa of active site His1
    Binding sitei347NAD1
    Binding sitei393UDP-glucuronate; via carbonyl oxygen1
    Binding sitei398UDP-glucuronate1
    Active sitei434Proton acceptor; for decarboxylase activity1
    Binding sitei460UDP-glucuronate1
    Binding sitei492UDP-glucuronate1
    Binding sitei613UDP-glucuronate1
    Active sitei619Proton donor; for decarboxylase activity1

    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 bindingi368 – 369NAD binding2

    <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 functionMultifunctional enzyme, Oxidoreductase, Transferase
    Biological processAntibiotic resistance, Lipid A biosynthesis, Lipid biosynthesis, Lipid metabolism, Lipopolysaccharide biosynthesis
    LigandNAD

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:G7168-MONOMER
    ECOL316407:JW2249-MONOMER
    MetaCyc:G7168-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		1.1.1.305, 2026
    2.1.2.13, 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P77398

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

    More...    UniPathwayi    		UPA00030
    UPA00032;UER00492
    UPA00032;UER00494

    <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:
    Bifunctional polymyxin resistance protein ArnA
    Alternative name(s):
    Polymyxin resistance protein PmrI
    Including the following 2 domains:
    UDP-4-amino-4-deoxy-L-arabinose formyltransferase (EC:2.1.2.13)
    Alternative name(s):
    ArnAFT
    UDP-L-Ara4N formyltransferase
    UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating (EC:1.1.1.305)
    Alternative name(s):
    ArnADH
    UDP-GlcUA decarboxylase
    UDP-glucuronic acid dehydrogenase
    <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:arnA
    Synonyms:pmrI, yfbG
    Ordered Locus Names:b2255, JW2249
    <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 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>Mutagenesisi102N → A: No activity. 1 Publication1
    Mutagenesisi104H → A: 25-fold lower activity. 1 Publication1
    Mutagenesisi104H → K: Less than 1% residual activity. 1 Publication1
    Mutagenesisi140D → A or N: Less than 1% residual activity. 1 Publication1
    Mutagenesisi433S → A: 40-fold lower specific activity. 2 Publications1
    Mutagenesisi433S → T: No activity. 2 Publications1
    Mutagenesisi434E → A: 100-fold lower specific activity. 1 Publication1
    Mutagenesisi434E → Q: No activity. 1 Publication1
    Mutagenesisi619R → E or Y: No activity. 1 Publication1
    Mutagenesisi619R → M: 400-fold lower activity. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...    DrugBanki    		DB03256, (6R)-Folinic acid
    DB03685, Uridine monophosphate

    <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_00000830981 – 660Bifunctional polymyxin resistance protein ArnAAdd BLAST660

    Proteomic databases

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

    More...    PaxDbi    		P77398

    PRoteomics IDEntifications database

    More...    PRIDEi    		P77398

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Induced by BasR.1 Publication

    <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, formed by a dimer of trimers.

    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

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4260497, 265 interactors
    851996, 2 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-11961N

    Protein interaction database and analysis system

    More...    IntActi    		P77398, 15 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b2255

    <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

    1660
    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    		P77398

    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    		P77398

    <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>Regioni1 – 304Formyltransferase ArnAFTAdd BLAST304
    Regioni86 – 8810-formyltetrahydrofolate binding3
    Regioni136 – 14010-formyltetrahydrofolate binding5
    Regioni314 – 660Dehydrogenase ArnADHAdd BLAST347
    Regioni432 – 433UDP-glucuronate binding2
    Regioni526 – 535UDP-glucuronate binding10

    <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 Fmt family. UDP-L-Ara4N formyltransferase subfamily.Curated
    In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG0223, Bacteria
    COG0451, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_007383_23_1_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P77398

    KEGG Orthology (KO)

    More...    KOi    		K10011

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P77398

    Family and domain databases

    HAMAP database of protein families

    More...    HAMAPi    		MF_01166, ArnA, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR021168, Bifun_polymyxin_resist_ArnA
    IPR001509, Epimerase_deHydtase
    IPR005793, Formyl_trans_C
    IPR002376, Formyl_transf_N
    IPR036477, Formyl_transf_N_sf
    IPR011034, Formyl_transferase-like_C_sf
    IPR036291, NAD(P)-bd_dom_sf

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF01370, Epimerase, 1 hit
    PF02911, Formyl_trans_C, 1 hit
    PF00551, Formyl_trans_N, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF036506, Bifun_polymyxin_resist_ArnA, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF50486, SSF50486, 1 hit
    SSF51735, SSF51735, 1 hit
    SSF53328, SSF53328, 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.

    P77398-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKTVVFAYHD MGCLGIEALL AAGYEISAIF THTDNPGEKA FYGSVARLAA 
            60         70         80         90        100
    ERGIPVYAPD NVNHPLWVER IAQLSPDVIF SFYYRHLIYD EILQLAPAGA 
           110        120        130        140        150
    FNLHGSLLPK YRGRAPLNWV LVNGETETGV TLHRMVKRAD AGAIVAQLRI 
           160        170        180        190        200
    AIAPDDIAIT LHHKLCHAAR QLLEQTLPAI KHGNILEIAQ RENEATCFGR 
           210        220        230        240        250
    RTPDDSFLEW HKPASVLHNM VRAVADPWPG AFSYVGNQKF TVWSSRVHPH 
           260        270        280        290        300
    ASKAQPGSVI SVAPLLIACG DGALEIVTGQ AGDGITMQGS QLAQTLGLVQ 
           310        320        330        340        350
    GSRLNSQPAC TARRRTRVLI LGVNGFIGNH LTERLLREDH YEVYGLDIGS 
           360        370        380        390        400
    DAISRFLNHP HFHFVEGDIS IHSEWIEYHV KKCDVVLPLV AIATPIEYTR 
           410        420        430        440        450
    NPLRVFELDF EENLRIIRYC VKYRKRIIFP STSEVYGMCS DKYFDEDHSN 
           460        470        480        490        500
    LIVGPVNKPR WIYSVSKQLL DRVIWAYGEK EGLQFTLFRP FNWMGPRLDN 
           510        520        530        540        550
    LNAARIGSSR AITQLILNLV EGSPIKLIDG GKQKRCFTDI RDGIEALYRI 
           560        570        580        590        600
    IENAGNRCDG EIINIGNPEN EASIEELGEM LLASFEKHPL RHHFPPFAGF 
           610        620        630        640        650
    RVVESSSYYG KGYQDVEHRK PSIRNAHRCL DWEPKIDMQE TIDETLDFFL 
           660
    RTVDLTDKPS
    Length:660
    Mass (Da):74,289
    Last modified:February 1, 1997 - 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:iA430928AB4041FA3
    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
    		AY057445 Genomic DNA Translation: AAL23678.1
    U00096 Genomic DNA Translation: AAC75315.1
    AP009048 Genomic DNA Translation: BAA16078.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		E64996

    NCBI Reference Sequences

    More...    RefSeqi    		NP_416758.1, NC_000913.3
    WP_000860273.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC75315; AAC75315; b2255
    BAA16078; BAA16078; BAA16078

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		947683

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW2249
    eco:b2255

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.4482

    <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
    		AY057445 Genomic DNA Translation: AAL23678.1
    U00096 Genomic DNA Translation: AAC75315.1
    AP009048 Genomic DNA Translation: BAA16078.1
    PIRiE64996
    RefSeqiNP_416758.1, NC_000913.3
    WP_000860273.1, 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
    1U9JX-ray2.40A306-660[»]
    1YRWX-ray1.70A1-300[»]
    1Z73X-ray2.50A306-660[»]
    1Z74X-ray2.70A306-660[»]
    1Z75X-ray2.40A306-660[»]
    1Z7BX-ray2.31A306-660[»]
    1Z7EX-ray3.00A/B/C/D/E/F1-660[»]
    2BLLX-ray2.30A317-660[»]
    2BLNX-ray1.20A/B1-305[»]
    4WKGX-ray2.70A/B/C/D/E/F1-660[»]
    6PIHelectron microscopy6.60A/B/C/D/E/F1-300[»]
    G/H/I/J/K/L317-660[»]
    6PIKelectron microscopy7.80A/B/C/D1-300[»]
    E/F/G/H317-660[»]
    SMRiP77398
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4260497, 265 interactors
    851996, 2 interactors
    DIPiDIP-11961N
    IntActiP77398, 15 interactors
    STRINGi511145.b2255

    Chemistry databases

    DrugBankiDB03256, (6R)-Folinic acid
    DB03685, Uridine monophosphate

    Proteomic databases

    PaxDbiP77398
    PRIDEiP77398

    Genome annotation databases

    EnsemblBacteriaiAAC75315; AAC75315; b2255
    BAA16078; BAA16078; BAA16078
    GeneIDi947683
    KEGGiecj:JW2249
    eco:b2255
    PATRICifig|1411691.4.peg.4482

    Organism-specific databases

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

    More...    EchoBASEi    		EB3844

    Phylogenomic databases

    eggNOGiCOG0223, Bacteria
    COG0451, Bacteria
    HOGENOMiCLU_007383_23_1_6
    InParanoidiP77398
    KOiK10011
    PhylomeDBiP77398

    Enzyme and pathway databases

    UniPathwayiUPA00030
    UPA00032;UER00492
    UPA00032;UER00494
    BioCyciEcoCyc:G7168-MONOMER
    ECOL316407:JW2249-MONOMER
    MetaCyc:G7168-MONOMER
    BRENDAi1.1.1.305, 2026
    2.1.2.13, 2026
    SABIO-RKiP77398

    Miscellaneous databases

    EvolutionaryTraceiP77398

    Protein Ontology

    More...    PROi    		PR:P77398

    Family and domain databases

    HAMAPiMF_01166, ArnA, 1 hit
    InterProiView protein in InterPro
    IPR021168, Bifun_polymyxin_resist_ArnA
    IPR001509, Epimerase_deHydtase
    IPR005793, Formyl_trans_C
    IPR002376, Formyl_transf_N
    IPR036477, Formyl_transf_N_sf
    IPR011034, Formyl_transferase-like_C_sf
    IPR036291, NAD(P)-bd_dom_sf
    PfamiView protein in Pfam
    PF01370, Epimerase, 1 hit
    PF02911, Formyl_trans_C, 1 hit
    PF00551, Formyl_trans_N, 1 hit
    PIRSFiPIRSF036506, Bifun_polymyxin_resist_ArnA, 1 hit
    SUPFAMiSSF50486, SSF50486, 1 hit
    SSF51735, SSF51735, 1 hit
    SSF53328, SSF53328, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    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 nameiARNA_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: P77398
    Secondary accession number(s): Q56VX0
    <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: July 15, 1999
    Last sequence update: February 1, 1997
    Last modified: August 12, 2020
    This is version 178 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Reference proteome

    Documents

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