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Q83KB7 (ARND_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:SF2335, S2468
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length296 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 – 296296Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD HAMAP-Rule MF_01870
PRO_0000383545

Regions

Domain2 – 260259NodB homology

Sequences

Sequence LengthMass (Da)Tools
Q83KB7 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: C162658450D49B2E

FASTA29633,064
        10         20         30         40         50         60 
MTKVGLRIDV DAFRGTREGV PRLLEILSKH NIQASIFFSV GPDNMGRHLW RLVKPQFLWK 

        70         80         90        100        110        120 
MLRSNAASLY GWDILLAGTA WPGKEIGHAN ADIIREAAKH HEVGLHAWDH HAWQARSGNW 

       130        140        150        160        170        180 
DRQTMIDDIA RGLRTLEEII GQPVTCSAAA GWRADQKVIE AKEAFHLRYN SDCRGAIPFR 

       190        200        210        220        230        240 
PLLESGNPGT AQIPVTLPTW DEVIGRDVKA EDFNGWLLNR ILRDKGTPVY TIHAEVEGCA 

       250        260        270        280        290 
YQHNFVDLLK RAAQEGVTFC PLSELLSETL PLGQVVRGNI AGREGWLGCQ QIAGSR 

« Hide

References

[1]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005674 Genomic DNA. Translation: AAN43849.1.
AE014073 Genomic DNA. Translation: AAP17668.1.
RefSeqNP_708142.1. NC_004337.2.
NP_837858.1. NC_004741.1.

3D structure databases

ProteinModelPortalQ83KB7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198214.SF2335.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN43849; AAN43849; SF2335.
AAP17668; AAP17668; S2468.
GeneID1025486.
1078760.
KEGGsfl:SF2335.
sfx:S2468.
PATRIC18706527. VBIShiFle31049_2739.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0726.
HOGENOMHOG000261199.
KOK13014.
OMALHAWDHF.
OrthoDBEOG6423D0.
ProtClustDBPRK15394.

Enzyme and pathway databases

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_SHIFL
AccessionPrimary (citable) accession number: Q83KB7
Secondary accession number(s): Q7C0R3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 74 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