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Protein

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

Gene

arnD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 (Probable).1 Publication

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 annotation1 Publication

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 annotation1 Publication
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 annotation1 Publication
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

BioCyciEcoCyc:G7169-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
Synonyms:pmrJ, yfbH
Ordered Locus Names:b2256, JW2250
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14092 arnD

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001691761 – 296Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnDAdd BLAST296

Proteomic databases

PaxDbiP76472
PRIDEiP76472

Expressioni

Inductioni

Induced by BasR.By similarity

Interactioni

Protein-protein interaction databases

BioGridi4260498, 208 interactors
IntActiP76472, 1 interactor
STRINGi316385.ECDH10B_2416

Structurei

3D structure databases

ProteinModelPortaliP76472
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

Phylogenomic databases

eggNOGiENOG4105F73 Bacteria
COG0726 LUCA
HOGENOMiHOG000261199
InParanoidiP76472
KOiK13014
OMAiKFLWKML
PhylomeDBiP76472

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.

P76472-1 [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
DEVIGRDVKA EDFNGWLLNR ILRDKGTPVY TIHAEVEGCA YQHNFVDLLK
260 270 280 290
RAAQEGVTFC PLSELLSETL PLGQVVRGNI AGREGWLGCQ QIAGSR
Length:296
Mass (Da):33,112
Last modified:February 1, 1997 - v1
Checksum:iDDD0BEE55581DE3C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC75316.1
AP009048 Genomic DNA Translation: BAE76673.1
PIRiF64996
RefSeqiNP_416759.1, NC_000913.3
WP_000169728.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC75316; AAC75316; b2256
BAE76673; BAE76673; BAE76673
GeneIDi945334
KEGGiecj:JW2250
eco:b2256
PATRICifig|1411691.4.peg.4481

Entry informationi

Entry nameiARND_ECOLI
AccessioniPrimary (citable) accession number: P76472
Secondary accession number(s): Q2MAN3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: February 1, 1997
Last modified: April 25, 2018
This is version 120 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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