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
Shewanella sediminis (strain HAW-EB3)
Status
Reviewed-Annotation score: -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. Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase (arnC)
  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

Keywordsi

Molecular functionHydrolase
Biological processAntibiotic resistance, Lipid A biosynthesis, Lipid biosynthesis, Lipid metabolism, Lipopolysaccharide biosynthesis

Enzyme and pathway databases

BioCyciSSED425104:G1G9Y-964-MONOMER
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:Ssed_0923
OrganismiShewanella sediminis (strain HAW-EB3)
Taxonomic identifieri425104 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000002015 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003835411 – 305Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnDAdd BLAST305

Proteomic databases

PRIDEiA8FRR1

Interactioni

Protein-protein interaction databases

STRINGi425104.Ssed_0923

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 262NodB homologyUniRule annotationAdd BLAST256

Sequence similaritiesi

Belongs to the polysaccharide deacetylase family. ArnD deformylase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105F73 Bacteria
COG0726 LUCA
HOGENOMiHOG000261199
OMAiKFLWKML
OrthoDBiPOG091H0IAQ

Family and domain databases

HAMAPiMF_01870 ArnD, 1 hit
InterProiView protein in InterPro
IPR023557 ArnD
IPR011330 Glyco_hydro/deAcase_b/a-brl
IPR002509 NODB_dom
PfamiView protein in Pfam
PF01522 Polysacc_deac_1, 1 hit
SUPFAMiSSF88713 SSF88713, 2 hits
PROSITEiView protein in PROSITE
PS51677 NODB, 1 hit

Sequencei

Sequence statusi: Complete.

A8FRR1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQQNVTKVG LRIDVDTYRG TRLGVPKLLE IFQRHDISAS FFFTVGPDNM
60 70 80 90 100
GRHIWRLLRP AFLKKMLRSK AASLYGWDIL IRGTLWPGPI IGKKLAHIIK
110 120 130 140 150
QADDAGHEIG LHAWDHHKWQ MKTDVMTPAE LHSEIDKGYQ LLSTLTGKPI
160 170 180 190 200
PCSAVAGWRC TDATLEQKQR FGFRYNSDCR GESIFIPQLG MAPQIPVTLP
210 220 230 240 250
TYDELVGKDN IDHSNYNAEI IKLVNPDGLN VYTIHAEVEG IVCAQLFEEL
260 270 280 290 300
IIQAKENNIE FVPMIELLDH EDIDWPLDEI LNIEIDGREG WLSHQASMIN

KQKSA
Length:305
Mass (Da):34,631
Last modified:November 13, 2007 - v1
Checksum:iDB5FA35891813801
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000821 Genomic DNA Translation: ABV35534.1
RefSeqiWP_012141270.1, NC_009831.1

Genome annotation databases

EnsemblBacteriaiABV35534; ABV35534; Ssed_0923
KEGGisse:Ssed_0923

Similar proteinsi

Entry informationi

Entry nameiARND_SHESH
AccessioniPrimary (citable) accession number: A8FRR1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: November 13, 2007
Last modified: May 23, 2018
This is version 66 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health