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

Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD

Gene

arnD

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

Functioni

Catalyzes the deformylation of 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol to 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.UniRule annotation

Catalytic activityi

4-deoxy-4-formamido-beta-L-arabinose di-trans,poly-cis-undecaprenyl phosphate + H2O = 4-amino-4-deoxy-alpha-L-arabinose di-trans,poly-cis-undecaprenyl phosphate + formate.UniRule annotation

Pathwayi: 4-amino-4-deoxy-alpha-L-arabinose undecaprenyl phosphate biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 4-amino-4-deoxy-alpha-L-arabinose undecaprenyl phosphate from UDP-4-deoxy-4-formamido-beta-L-arabinose and undecaprenyl phosphate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD (arnD)
This subpathway is part of the pathway 4-amino-4-deoxy-alpha-L-arabinose undecaprenyl phosphate biosynthesis, which is itself part of Glycolipid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 4-amino-4-deoxy-alpha-L-arabinose undecaprenyl phosphate from UDP-4-deoxy-4-formamido-beta-L-arabinose and undecaprenyl phosphate, the pathway 4-amino-4-deoxy-alpha-L-arabinose undecaprenyl phosphate biosynthesis and in Glycolipid 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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

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

Enzyme and pathway databases

UniPathwayiUPA00030.
UPA00036; UER00496.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnDUniRule annotation (EC:3.5.1.n3UniRule annotation)
Gene namesi
Name:arnDUniRule annotation
Ordered Locus Names:SbBS512_E2632
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_00003835421 – 296Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnDAdd BLAST296

Structurei

3D structure databases

ProteinModelPortaliB2TW39.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 260NodB homologyUniRule annotationAdd BLAST259

Sequence similaritiesi

Belongs to the polysaccharide deacetylase family. ArnD deformylase subfamily.UniRule annotation
Contains 1 NodB homology domain.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000261199.
KOiK13014.
OMAiKFLWKML.

Family and domain databases

Gene3Di3.20.20.370. 2 hits.
HAMAPiMF_01870. ArnD. 1 hit.
InterProiIPR023557. ArnD.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR002509. NODB_dom.
[Graphical view]
PfamiPF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
SUPFAMiSSF88713. SSF88713. 2 hits.
PROSITEiPS51677. NODB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B2TW39-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKVGLRIDV DTFRGTREGV PRLLEILSKH NIQASIFFSV GPDNMGRHLW
60 70 80 90 100
RLVKPQFLWK MLRSNAASLY GWDILLAGTA WPGKEIGHAN ADIIREAAKH
110 120 130 140 150
HEVGLHAWDH HAWQARSGNW DRQTMIDDIA RGLRTLEEII GQPVTCSAAA
160 170 180 190 200
GWRADQKVIE AKEAFHLRYN SDCRGAMPFR PLLESGNPGT AQIPVTLPTW
210 220 230 240 250
DEVIGRDVKT EDFNGWLLNR ILRDKGTPVY TIHAEVEGCA YQHNFVDLLK
260 270 280 290
RAAQEGVTFC PLSELLSETL PLGQVVRGNI AGREGWLGCQ QIAGSR
Length:296
Mass (Da):33,142
Last modified:July 1, 2008 - v1
Checksum:i2981FBF11081C526
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001063 Genomic DNA. Translation: ACD09528.1.
RefSeqiWP_000169731.1. NC_010658.1.

Genome annotation databases

EnsemblBacteriaiACD09528; ACD09528; SbBS512_E2632.
KEGGisbc:SbBS512_E2632.
PATRICi18672311. VBIShiBoy129590_2915.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001063 Genomic DNA. Translation: ACD09528.1.
RefSeqiWP_000169731.1. NC_010658.1.

3D structure databases

ProteinModelPortaliB2TW39.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACD09528; ACD09528; SbBS512_E2632.
KEGGisbc:SbBS512_E2632.
PATRICi18672311. VBIShiBoy129590_2915.

Phylogenomic databases

HOGENOMiHOG000261199.
KOiK13014.
OMAiKFLWKML.

Enzyme and pathway databases

UniPathwayiUPA00030.
UPA00036; UER00496.

Family and domain databases

Gene3Di3.20.20.370. 2 hits.
HAMAPiMF_01870. ArnD. 1 hit.
InterProiIPR023557. ArnD.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR002509. NODB_dom.
[Graphical view]
PfamiPF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
SUPFAMiSSF88713. SSF88713. 2 hits.
PROSITEiPS51677. NODB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiARND_SHIB3
AccessioniPrimary (citable) accession number: B2TW39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 1, 2008
Last modified: November 30, 2016
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

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.