Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bifunctional polymyxin resistance protein ArnA

Gene

arnA

Organism
Shigella flexneri
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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

Catalytic activityi

UDP-alpha-D-glucuronate + NAD+ = UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH.UniRule annotation
10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinose.UniRule annotation

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 UDP-glucuronic acid oxidase/UDP-4-amino-4-deoxy-L-arabinose formyltransferase (CBL25_09745), Bifunctional polymyxin resistance protein ArnA (arnA), 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), UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase (arnB)
  3. Bifunctional UDP-glucuronic acid oxidase/UDP-4-amino-4-deoxy-L-arabinose formyltransferase (CBL25_09745), Bifunctional polymyxin resistance protein ArnA (arnA), 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.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
Sitei102Transition state stabilizerUniRule annotation1
Active sitei104Proton donor; for formyltransferase activityUniRule annotation1
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
Nucleotide bindingi368 – 369NAD bindingUniRule annotation2

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase, Transferase
Biological processAntibiotic resistance, Lipid A biosynthesis, Lipid biosynthesis, Lipid metabolism, Lipopolysaccharide biosynthesis
LigandNAD

Enzyme and pathway databases

UniPathwayiUPA00030.
UPA00032; UER00492.
UPA00032; UER00494.

Names & Taxonomyi

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
Gene namesi
Name:arnAUniRule annotation
Ordered Locus Names:SF2334, S2467
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000002673 Componenti: Chromosome
  • UP000001006 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000831101 – 660Bifunctional polymyxin resistance protein ArnAAdd BLAST660

Proteomic databases

PaxDbiQ83QT8.

Interactioni

Subunit structurei

Homohexamer, formed by a dimer of trimers.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ83QT8.
SMRiQ83QT8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 304Formyltransferase ArnAFTAdd BLAST304
Regioni86 – 8810-formyltetrahydrofolate bindingUniRule annotation3
Regioni136 – 14010-formyltetrahydrofolate bindingUniRule annotation5
Regioni314 – 660Dehydrogenase ArnADHAdd BLAST347
Regioni432 – 433UDP-glucuronate bindingUniRule annotation2
Regioni526 – 535UDP-glucuronate bindingUniRule annotation10

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

eggNOGiCOG0223. LUCA.
COG0451. LUCA.
HOGENOMiHOG000247761.
KOiK10011.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_01166. ArnA. 1 hit.
InterProiView protein in InterPro
IPR021168. Bifun_polymyxin_resist_ArnA.
IPR001509. Epimerase_deHydtase.
IPR005793. Formyl_trans_C.
IPR037022. Formyl_trans_C_sf.
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.

Sequencei

Sequence statusi: Complete.

Q83QT8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTVVFAYHD MGCLGIEALL AAGYEISAIF THTDNPGEKA FYGSVAHLAA
60 70 80 90 100
ERDIPVYAPD NVNHPLWVER IAQLSPEVIF SFYYRHLICD EIFQLAPAGA
110 120 130 140 150
FNLHGSLLPK YRGRAPLNWV LVNGETETGV TLHRMVKRAD AGAIVAQLRV
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 QLAQMLGLVQ
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 EGLQFTLFLP FNWMGPRLDN
510 520 530 540 550
LNAARIGSSR AITQLILNLV EGSPIKLIDG GKQKRCFTDI RDGIEALYHI
560 570 580 590 600
IENAGNRCDG EIINIGNPEN EASIEELGEM LLASFEKHPL RHHFPPFAGF
610 620 630 640 650
RVVESSCYYG KGYQDVEHRK PSIRNAHRCL DWEPKIDMQE TIDETLDFFL
660
RTVDLTDKPS
Length:660
Mass (Da):74,286
Last modified:December 6, 2005 - v2
Checksum:i28C35336C4605F07
GO

Sequence cautioni

The sequence AAN43848 differs from that shown. Reason: Frameshift at position 136.Curated
The sequence AAP17667 differs from that shown. Reason: Frameshift at position 136.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN43848.1. Frameshift.
AE014073 Genomic DNA. Translation: AAP17667.1. Frameshift.

Genome annotation databases

EnsemblBacteriaiAAN43848; AAN43848; SF2334.
AAP17667; AAP17667; S2467.
KEGGisfx:S2467.

Similar proteinsi

Entry informationi

Entry nameiARNA_SHIFL
AccessioniPrimary (citable) accession number: Q83QT8
Secondary accession number(s): Q7C0R4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: November 22, 2017
This is version 111 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

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