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
Escherichia coli O139:H28 (strain E24377A / ETEC)
Status
Reviewed-Annotation score: Annotation score: 3 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

GO - Molecular functioni

  1. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides Source: UniProtKB-HAMAP

GO - Biological processi

  1. 4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate biosynthetic process Source: UniProtKB-UniPathway
  2. lipid A biosynthetic process Source: UniProtKB-HAMAP
  3. lipopolysaccharide biosynthetic process Source: UniProtKB-UniPathway
  4. response to antibiotic Source: UniProtKB-KW
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

BioCyciECOL331111:GH7P-2533-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:EcE24377A_2551
OrganismiEscherichia coli O139:H28 (strain E24377A / ETEC)
Taxonomic identifieri331111 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001122: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 296296Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnDPRO_0000383502Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi331111.EcE24377A_2551.

Structurei

3D structure databases

ProteinModelPortaliA7ZP74.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 260259NodB homologyUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0726.
HOGENOMiHOG000261199.
KOiK13014.
OMAiLHAWDHF.
OrthoDBiEOG6423D0.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

A7ZP74-1 [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 HAWQARSSNW 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):33,142
Last modified:October 23, 2007 - v1
Checksum:i7DC4B1938195D14A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000800 Genomic DNA. Translation: ABV17216.1.
RefSeqiYP_001463603.1. NC_009801.1.

Genome annotation databases

EnsemblBacteriaiABV17216; ABV17216; EcE24377A_2551.
GeneIDi5589727.
KEGGiecw:EcE24377A_2551.
PATRICi18294382. VBIEscCol31211_2833.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000800 Genomic DNA. Translation: ABV17216.1.
RefSeqiYP_001463603.1. NC_009801.1.

3D structure databases

ProteinModelPortaliA7ZP74.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi331111.EcE24377A_2551.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV17216; ABV17216; EcE24377A_2551.
GeneIDi5589727.
KEGGiecw:EcE24377A_2551.
PATRICi18294382. VBIEscCol31211_2833.

Phylogenomic databases

eggNOGiCOG0726.
HOGENOMiHOG000261199.
KOiK13014.
OMAiLHAWDHF.
OrthoDBiEOG6423D0.

Enzyme and pathway databases

UniPathwayiUPA00030.
UPA00036; UER00496.
BioCyciECOL331111:GH7P-2533-MONOMER.

Family and domain databases

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

Publicationsi

  1. "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
    Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
    J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: E24377A / ETEC.

Entry informationi

Entry nameiARND_ECO24
AccessioniPrimary (citable) accession number: A7ZP74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: October 23, 2007
Last modified: January 7, 2015
This is version 50 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

External Data

Dasty 3

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 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.