Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B5R273 (ARND_SALEP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD

EC=3.5.1.n3
Gene names
Name:arnD
Ordered Locus Names:SEN2282
OrganismSalmonella enteritidis PT4 (strain P125109) [Complete proteome] [HAMAP]
Taxonomic identifier550537 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_01870

Catalytic activity

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. HAMAP-Rule MF_01870

Pathway

Glycolipid biosynthesis; 4-amino-4-deoxy-alpha-L-arabinose undecaprenyl phosphate biosynthesis; 4-amino-4-deoxy-alpha-L-arabinose undecaprenyl phosphate from UDP-4-deoxy-4-formamido-beta-L-arabinose and undecaprenyl phosphate: step 2/2. HAMAP-Rule MF_01870

Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. HAMAP-Rule MF_01870

Sequence similarities

Belongs to the polysaccharide deacetylase family. ArnD deformylase subfamily.

Contains 1 NodB homology domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 299299Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD HAMAP-Rule MF_01870
PRO_0000383530

Regions

Domain2 – 260259NodB homology

Sequences

Sequence LengthMass (Da)Tools
B5R273 [UniParc].

Last modified November 4, 2008. Version 1.
Checksum: BE7579D1D493F4B2

FASTA29933,078
        10         20         30         40         50         60 
MTKVGLRIDV DTLRGTREGV PRLLATLHRH GVQASFFFSV GPDNMGRHLW RLIRPRFLWK 

        70         80         90        100        110        120 
MLRSNAASLY GWDILLAGTA WPGKNIGNAN AGIIRETATY HETGLHAWDH HAWQTHSGHW 

       130        140        150        160        170        180 
SIRQLEEDIA RGITALEAII GKPVTCSAAA GWRADGRVVR AKEPFNLRYN SDCRGTTLFR 

       190        200        210        220        230        240 
PLLMPGQTGT PQIPVTLPTW DEVIGPAVQA QSFNTWIISR MLQDKGTPVY TIHAEVEGIV 

       250        260        270        280        290 
HQPLFEDLLV RARDAGITFC PLGELLPTSP ESLPLGQIVR GHIPGREGWL GCQQAASAS 

« Hide

References

[1]"Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella gallinarum 287/91 provides insights into evolutionary and host adaptation pathways."
Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S., Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A., Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B., Ormond D. expand/collapse author list , Abdellah Z., Brooks K., Cherevach I., Chillingworth T., Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.
Genome Res. 18:1624-1637(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: P125109.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM933172 Genomic DNA. Translation: CAR33866.1.
RefSeqYP_002244369.1. NC_011294.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING550537.SEN2282.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR33866; CAR33866; SEN2282.
PATRIC32335089. VBISalEnt14964_2318.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0726.
HOGENOMHOG000261199.
OMALHAWDHF.
OrthoDBEOG6423D0.

Enzyme and pathway databases

BioCycSENT550537:GJFI-2311-MONOMER.
UniPathwayUPA00030.
UPA00036; UER00496.

Family and domain databases

Gene3D3.20.20.370. 2 hits.
HAMAPMF_01870. ArnD.
InterProIPR023557. ArnD.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR002509. Polysac_deacetylase.
[Graphical view]
PfamPF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
SUPFAMSSF88713. SSF88713. 2 hits.
PROSITEPS51677. NODB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARND_SALEP
AccessionPrimary (citable) accession number: B5R273
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: November 4, 2008
Last modified: June 11, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways