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A7ZP74

- ARND_ECO24

UniProt

A7ZP74 - ARND_ECO24

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Protein
Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD
Gene
arnD, EcE24377A_2551
Organism
Escherichia coli O139:H28 (strain E24377A / ETEC)
Status
Reviewed - 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 By similarity.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 ArnD (EC:3.5.1.n3)
Gene namesi
Name:arnD
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 ArnDUniRule annotation
PRO_0000383502Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi331111.EcE24377A_2551.

Structurei

3D structure databases

ProteinModelPortaliA7ZP74.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 260259NodB homology
Add
BLAST

Sequence similaritiesi

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

MTKVGLRIDV DTFRGTREGV PRLLEILSKH NIQASIFFSV GPDNMGRHLW    50
RLVKPQFLWK MLRSNAASLY GWDILLAGTA WPGKEIGHAN ADIIREAAKH 100
HEVGLHAWDH HAWQARSSNW DRQTMIDDIA RGLRTLEEII GQPVTCSAAA 150
GWRADQKVIE AKEAFHLRYN SDCRGAMPFR PLLESGNPGT AQIPVTLPTW 200
DEVIGRDVKA EDFNGWLLNR ILRDKGTPVY TIHAEVEGCA YQHNFVDLLK 250
RAAQEGVTFC PLSELLSETL PLGQVVRGNI AGREGWLGCQ QIAGSR 296
Length:296
Mass (Da):33,142
Last modified:October 23, 2007 - v1
Checksum:i7DC4B1938195D14A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CP000800 Genomic DNA. Translation: ABV17216.1 .
RefSeqi YP_001463603.1. NC_009801.1.

3D structure databases

ProteinModelPortali A7ZP74.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 331111.EcE24377A_2551.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABV17216 ; ABV17216 ; EcE24377A_2551 .
GeneIDi 5589727.
KEGGi ecw:EcE24377A_2551.
PATRICi 18294382. VBIEscCol31211_2833.

Phylogenomic databases

eggNOGi COG0726.
HOGENOMi HOG000261199.
KOi K13014.
OMAi LHAWDHF.
OrthoDBi EOG6423D0.

Enzyme and pathway databases

UniPathwayi UPA00030 .
UPA00036 ; UER00496 .
BioCyci ECOL331111:GH7P-2533-MONOMER.

Family and domain databases

Gene3Di 3.20.20.370. 2 hits.
HAMAPi MF_01870. ArnD.
InterProi IPR023557. ArnD.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR002509. Polysac_deacetylase.
[Graphical view ]
Pfami PF01522. Polysacc_deac_1. 1 hit.
[Graphical view ]
SUPFAMi SSF88713. SSF88713. 2 hits.
PROSITEi PS51677. NODB. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: May 14, 2014
This is version 48 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

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