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Protein

Putative bifunctional polymyxin resistance protein ArnA

Gene

arnA

Organism
Shigella boydii serotype 18 (strain CDC 3083-94 / BS512)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein uncertaini

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 (By similarity).By similarity

Catalytic activityi

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

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.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Putative bifunctional polymyxin resistance protein ArnA (arnA)
  2. no protein annotated in this organism
  3. Putative 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.
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
Sitei6Raises pKa of active site HisBy similarity1
Binding sitei213NADBy similarity1
Binding sitei259UDP-glucuronate; via carbonyl oxygenBy similarity1
Binding sitei264UDP-glucuronateBy similarity1
Active sitei300Proton acceptor; for decarboxylase activityBy similarity1
Binding sitei326UDP-glucuronateBy similarity1
Binding sitei358UDP-glucuronateBy similarity1
Binding sitei479UDP-glucuronateBy similarity1
Active sitei485Proton donor; for decarboxylase activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi234 – 235NAD bindingBy similarity2

GO - Molecular functioni

GO - Biological processi

Keywords - Molecular functioni

Oxidoreductase, Transferase

Keywords - Biological processi

Antibiotic resistance, Lipid A biosynthesis, Lipid biosynthesis, Lipid metabolism, Lipopolysaccharide biosynthesis

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00030.
UPA00032; UER00492.
UPA00032; UER00494.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative bifunctional polymyxin resistance protein ArnA
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
Gene namesi
Name:arnA
Ordered Locus Names:SbBS512_E2631
OrganismiShigella boydii serotype 18 (strain CDC 3083-94 / BS512)
Taxonomic identifieri344609 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000001030 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003799911 – 526Putative bifunctional polymyxin resistance protein ArnAAdd BLAST526

Interactioni

Subunit structurei

Homohexamer, formed by a dimer of trimers.By similarity

Structurei

3D structure databases

ProteinModelPortaliB2TW38.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 170Formyltransferase ArnAFTAdd BLAST170
Regioni2 – 610-formyltetrahydrofolate bindingBy similarity5
Regioni180 – 526Dehydrogenase ArnADHAdd BLAST347
Regioni298 – 299UDP-glucuronate bindingBy similarity2
Regioni392 – 401UDP-glucuronate bindingBy similarity10

Sequence similaritiesi

In the N-terminal section; belongs to the Fmt family. UDP-L-Ara4N formyltransferase subfamily.Curated

Phylogenomic databases

HOGENOMiHOG000247761.
KOiK10011.
OMAiVRYCVKY.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR001509. Epimerase_deHydtase.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01370. Epimerase. 1 hit.
PF02911. Formyl_trans_C. 1 hit.
[Graphical view]
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF51735. SSF51735. 1 hit.
SSF53328. SSF53328. 1 hit.

Sequencei

Sequence statusi: Complete.

B2TW38-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKRADAGAI VAQLRVAIAP DDIAITLHHK LCHAARQLLE QTLPAIKHGN
60 70 80 90 100
ILEIAQRENE ATCFGRRTPD DSFLEWHKPA SVLHNMVRAV ADPWPSAFSY
110 120 130 140 150
VGNQKFTVWS SRVHPHASKA QPGSVISIAP LLIACGDGAL EIVTGQAGDG
160 170 180 190 200
ITMQGSQLAQ TLGLVQGSRL NSQPACTARR RTRVLILGVN GFIGNHLTER
210 220 230 240 250
LLREDHYEVY GLDIGSDAIS RFLNHPHFHF VEGDISIHSE WIEYHVKKCD
260 270 280 290 300
VVLPLVAIAT PIEYTRNPLR VFELDFEENL RIIRYCVKYR KRIIFPSTSE
310 320 330 340 350
VYGMCSDKYF DEDHSNLIVG PVNKPRWIYS VSKQLLDRVI WAYGEKEGLQ
360 370 380 390 400
FTLFRPFNWM GPRLDNLNAA RIGSSRAITQ LILNLVEGSP IKLIDGGKQK
410 420 430 440 450
RCFTDIRDGI EALYRIIENA GNRCDGEIIN IGNPENEASI EELGKMLLAS
460 470 480 490 500
FEKHPLRHHF PPFAGFRVVE SSSYYGKGYQ DVEHRKPSIR NAHRCLDWEP
510 520
KIDMQETIDE TLDFFLRTVD LTDKPS
Length:526
Mass (Da):59,435
Last modified:July 1, 2008 - v1
Checksum:iAF2E061948764B2A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001063 Genomic DNA. Translation: ACD07332.1.
RefSeqiWP_012421336.1. NC_010658.1.

Genome annotation databases

EnsemblBacteriaiACD07332; ACD07332; SbBS512_E2631.
KEGGisbc:SbBS512_E2631.
PATRICi18672309. VBIShiBoy129590_2914.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001063 Genomic DNA. Translation: ACD07332.1.
RefSeqiWP_012421336.1. NC_010658.1.

3D structure databases

ProteinModelPortaliB2TW38.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACD07332; ACD07332; SbBS512_E2631.
KEGGisbc:SbBS512_E2631.
PATRICi18672309. VBIShiBoy129590_2914.

Phylogenomic databases

HOGENOMiHOG000247761.
KOiK10011.
OMAiVRYCVKY.

Enzyme and pathway databases

UniPathwayiUPA00030.
UPA00032; UER00492.
UPA00032; UER00494.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR001509. Epimerase_deHydtase.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01370. Epimerase. 1 hit.
PF02911. Formyl_trans_C. 1 hit.
[Graphical view]
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF51735. SSF51735. 1 hit.
SSF53328. SSF53328. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiARNA_SHIB3
AccessioniPrimary (citable) accession number: B2TW38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 1, 2008
Last modified: November 30, 2016
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Could be the product of a pseudogene. The N-terminal region is truncated when compared to orthologs.Curated

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.