Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD - Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

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O52326 (ARND_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]

Taxonomic identifier

99287 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

Protein attributes

Sequence length	299 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Antibiotic resistance Lipid A biosynthesis Lipid biosynthesis Lipid metabolism Lipopolysaccharide biosynthesis
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway lipid A biosynthetic process Inferred from electronic annotation. Source: HAMAP lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 299

299

Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD HAMAP-Rule MF_01870

PRO_0000169177

Sequences

Sequence

Length

Mass (Da)

Tools

O52326 [UniParc].

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

299

33,010

        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' referencesShow '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. 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.
RefSeq	NP_461242.1. NC_003197.1.
3D structure databases
ProteinModelPortal	O52326.
ModBase	Search...
Protein-protein interaction databases
STRING	99287.STM2300.
Proteomic databases
PRIDE	O52326.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL21201; AAL21201; STM2300.
GeneID	1253822.
KEGG	stm:STM2300.
PATRIC	32383211. VBISalEnt20916_2435.
Phylogenomic databases
HOGENOM	HOG000261199.
KO	K13014.
OMA	HHGWQAN.
ProtClustDB	PRK15394.
Enzyme and pathway databases
UniPathway	UPA00030. UPA00036; UER00496.
Family and domain databases
Gene3D	3.20.20.370. 2 hits.
HAMAP	MF_01870. ArnD.
InterPro	IPR023557. ArnD. IPR011330. Glyco_hydro/deAcase_b/a-brl. IPR002509. Polysac_deacetylase. [Graphical view]
Pfam	PF01522. Polysacc_deac_1. 1 hit. [Graphical view]
SUPFAM	SSF88713. Glyco_hydro/deAcase_b/a-brl. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARND_SALTY

Accession

Primary (citable) accession number: O52326

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents