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Entry version 85 (08 May 2019)
Sequence version 1 (15 May 2007)
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Protein

Bifunctional polymyxin resistance protein ArnA

Gene

arnA

Organism
Yersinia pestis (strain Pestoides F)
Status
Reviewed-Annotation score:

Annotation score:4 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>
-Protein inferred from homologyi <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.UniRule annotation

<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 <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: 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.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Bifunctional polymyxin resistance protein ArnA (arnA)
  2. UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase (arnB)
  3. 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.UniRule annotation
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 stabilizerUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 activityUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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-formyltetrahydrofolateUniRule annotation1
Sitei140Raises pKa of active site HisUniRule annotation1
Binding sitei347NADUniRule annotation1
Binding sitei393UDP-glucuronate; via carbonyl oxygenUniRule annotation1
Binding sitei398UDP-glucuronateUniRule annotation1
Active sitei434Proton acceptor; for decarboxylase activityUniRule annotation1
Binding sitei460UDP-glucuronateUniRule annotation1
Binding sitei492UDP-glucuronateUniRule annotation1
Binding sitei613UDP-glucuronateUniRule annotation1
Active sitei619Proton donor; for decarboxylase activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingUniRule annotation2

<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

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_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:
Bifunctional polymyxin resistance protein ArnAUniRule annotation
Including the following 2 domains:
UDP-4-amino-4-deoxy-L-arabinose formyltransferaseUniRule annotation (EC:2.1.2.13UniRule annotation)
Alternative name(s):
ArnAFTUniRule annotation
UDP-L-Ara4N formyltransferaseUniRule annotation
UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylatingUniRule annotation (EC:1.1.1.305UniRule annotation)
Alternative name(s):
ArnADHUniRule annotation
UDP-GlcUA decarboxylaseUniRule annotation
UDP-glucuronic acid dehydrogenaseUniRule 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:arnAUniRule annotation
Ordered Locus Names:YPDSF_0730
<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>OrganismiYersinia pestis (strain Pestoides F)
<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 identifieri386656 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeYersinia

<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_10000656811 – 667Bifunctional polymyxin resistance protein ArnAAdd BLAST667

<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, formed by a dimer of trimers.

UniRule annotation

<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

3D structure databases

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

More...
SMRi
A4TIM4

Database of comparative protein structure models

More...
ModBasei
Search...

<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
Regioni136 – 14010-formyltetrahydrofolate bindingUniRule annotation5
Regioni314 – 667Dehydrogenase ArnADHAdd BLAST354
Regioni432 – 433UDP-glucuronate bindingUniRule annotation2
Regioni526 – 535UDP-glucuronate bindingUniRule annotation10

<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.UniRule annotation
In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.UniRule annotation

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000247761

KEGG Orthology (KO)

More...
KOi
K10011

Identification of Orthologs from Complete Genome Data

More...
OMAi
VRYCVKY

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_length">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_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.

A4TIM4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKAIVFAYHD IGCVGLNALA EAGYDIQAVF THTDNPGENR FFSSVARVAA
60 70 80 90 100
DLALPVFAPE DVNHPLWVER IRELQPDIIF SFYYRNMLSD EILSLAPQGG
110 120 130 140 150
FNLHGSLLPQ YRGRAPINWV LVNGETETGV TLHQMVKKAD AGPIAGQYKV
160 170 180 190 200
AISDVDTALT LHAKMRDAAQ ELLRNLLPRM KEGPLPLTPQ KEADASYFGR
210 220 230 240 250
RTAADGEIHW QKSAFTINNL VRAVTEPYPG AFSYLGQRKL TIWRSRPLDL
260 270 280 290 300
VHNKLPGTVL STAPLTVACG EGALEIITGQ GEAGLYVQGD RLAQEMGIVT
310 320 330 340 350
DVRLGNKPSN TLKRRTRVLI LGVNGFIGNH LTERLLQDDR YEVYGLDIGS
360 370 380 390 400
DAISRFLGNP AFHFVEGDIS IHSEWIEYHI KKCDVILPLV AIATPIEYTR
410 420 430 440 450
NPLRVFELDF EENLKIVRDC VKYNKRIVFP STSEVYGMCD DKEFDEDTSR
460 470 480 490 500
LIVGPINKQR WIYSVSKQLL DRVIWAYGVK EGLKFTLFRP FNWMGPRLDN
510 520 530 540 550
LDAARIGSSR AITQLILNLV EGSPIKLVDG GAQKRCFTDI HDGIEALFRI
560 570 580 590 600
IENRDGCCDG RIINIGNPTN EASIRELAEM LLTSFENHEL RDHFPPFAGF
610 620 630 640 650
KDIESSAYYG KGYQDVEYRT PSIKNARRIL HWQPEIAMQQ TVTETLDFFL
660
RAAVIEKTAA PKDELNA
Length:667
Mass (Da):74,921
Last modified:May 15, 2007 - 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:i934903C30E3E1163
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
CP000668 Genomic DNA Translation: ABP39136.1

NCBI Reference Sequences

More...
RefSeqi
WP_002211823.1, NZ_CP009715.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ABP39136; ABP39136; YPDSF_0730

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ypp:YPDSF_0730

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|386656.14.peg.3139

<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
CP000668 Genomic DNA Translation: ABP39136.1
RefSeqiWP_002211823.1, NZ_CP009715.1

3D structure databases

SMRiA4TIM4
ModBaseiSearch...

Genome annotation databases

EnsemblBacteriaiABP39136; ABP39136; YPDSF_0730
KEGGiypp:YPDSF_0730
PATRICifig|386656.14.peg.3139

Phylogenomic databases

HOGENOMiHOG000247761
KOiK10011
OMAiVRYCVKY

Enzyme and pathway databases

UniPathwayiUPA00030
UPA00032;UER00492
UPA00032;UER00494

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_YERPP
<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: A4TIM4
<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: February 5, 2008
Last sequence update: May 15, 2007
Last modified: May 8, 2019
This is version 85 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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