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Entry version 185 (25 May 2022)
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.

4 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 NAD+1 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 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

GO - Biological processi

<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

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:2.1.2.131 Publication)
Alternative name(s):
ArnAFT
UDP-L-Ara4N formyltransferase
UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating (EC:1.1.1.3051 Publication)
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi102N → A: No formyltransferase activity. 1 Publication1
Mutagenesisi104H → A: 25-fold lower formyltransferase activity. 1 Publication1
Mutagenesisi104H → K: Less than 1% residual formyltransferase activity. 1 Publication1
Mutagenesisi140D → A or N: Less than 1% residual formyltransferase 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

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

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
P77398

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

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

Identification of Orthologs from Complete Genome Data

More...
OMAi
VRYCVKY

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P77398

Family and domain databases

Conserved Domains Database

More...
CDDi
cd05257, Arna_like_SDR_e, 1 hit

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
IPR045869, Arna-like_SDR_e
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

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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[»]
AlphaFoldDBiP77398
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
OMAiVRYCVKY
PhylomeDBiP77398

Enzyme and pathway databases

UniPathwayiUPA00030
UPA00032;UER00492
UPA00032;UER00494
BioCyciEcoCyc: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

CDDicd05257, Arna_like_SDR_e, 1 hit
HAMAPiMF_01166, ArnA, 1 hit
InterProiView protein in InterPro
IPR045869, Arna-like_SDR_e
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

MobiDB: a database of protein disorder and mobility annotations

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<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: May 25, 2022
This is version 185 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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