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O52326 (ARND_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 83. 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
Synonyms:pbgP4, pmrJ
Ordered Locus Names:STM2300
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 Probable. Ref.4

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

Induction

Induced by BasR. Ref.3

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_0000169177

Regions

Domain2 – 260259NodB homology

Sequences

Sequence LengthMass (Da)Tools
O52326 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 5A33F6D1D494859F

FASTA29933,010
        10         20         30         40         50         60 
MTKVGLRIDV DTLRGTREGV PRLLATLHRH GVQASFFFSV GPDNMGRHLW RLIKPRFLWK 

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

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

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

       250        260        270        280        290 
HQPLFEDLLV RARDAGITFC PLGELLPASP ESLPLGQIVR GHIPGREGWL GCQQAASAS 

« Hide

References

« Hide 'large scale' references
[1]"PmrA-PmrB-regulated genes necessary for 4-aminoarabinose lipid A modification and polymyxin resistance."
Gunn J.S., Lim K.B., Krueger J., Kim K., Guo L., Hackett M., Miller S.I.
Mol. Microbiol. 27:1171-1182(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 14028s / SGSG 2262.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"Molecular characterization of the PmrA regulon."
Woesten M.M.S.M., Groisman E.A.
J. Biol. Chem. 274:27185-27190(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
Strain: ATCC 14028s / SGSG 2262.
[4]"Genetic and functional analysis of a PmrA-PmrB-regulated locus necessary for lipopolysaccharide modification, antimicrobial peptide resistance, and oral virulence of Salmonella enterica serovar typhimurium."
Gunn J.S., Ryan S.S., Van Velkinburgh J.C., Ernst R.K., Miller S.I.
Infect. Immun. 68:6139-6146(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN POLYMYXIN RESISTANCE.
Strain: ATCC 14028s / SGSG 2262.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF036677 Genomic DNA. Translation: AAC04773.1.
AE006468 Genomic DNA. Translation: AAL21201.1.
RefSeqNP_461242.1. NC_003197.1.

3D structure databases

ProteinModelPortalO52326.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM2300.

Proteomic databases

PRIDEO52326.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL21201; AAL21201; STM2300.
GeneID1253822.
KEGGstm:STM2300.
PATRIC32383211. VBISalEnt20916_2435.

Phylogenomic databases

HOGENOMHOG000261199.
KOK13014.
OMALHAWDHF.
OrthoDBEOG6423D0.
ProtClustDBPRK15394.

Enzyme and pathway databases

BioCycSENT99287:GCTI-2315-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_SALTY
AccessionPrimary (citable) accession number: O52326
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: June 1, 1998
Last modified: February 19, 2014
This is version 83 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