Reviewed, UniProtKB/Swiss-Prot P76472 (ARND_ECOLI)

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:	pmrJ, yfbH
Ordered Locus Names:	b2256, JW2250

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	296 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	4-deoxy-4-formamido-beta-L-arabinose undecaprenyl phosphate + H2O = 4-amino-4-deoxy-alpha-L-arabinose undecaprenyl phosphate + formate. Ref.3
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. Ref.4 Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Ref.4
Induction	Induced by basR By similarity.
Sequence similarities	Belongs to the polysaccharide deacetylase family. ArnD deformylase subfamily.

Ontologies

Keywords
Biological process	Antibiotic resistance Lipid A biosynthesis Lipid synthesis Lipopolysaccharide biosynthesis
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	lipid A biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides Inferred from electronic annotation. Source: HAMAP protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
groL	P0A6F5	1	EBI-1128209,EBI-543750

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 296	296	Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase arnD HAMAP MF_01870		PRO_0000169176

Sequences

	Sequence		Length	Mass (Da)
	P76472-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: DDD0BEE55581DE3C	FASTA	296	33,112
	10 20 30 40 50 60 MTKVGLRIDV DTFRGTREGV 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 SDCRGAMPFR 190 200 210 220 230 240 PLLESGNPGT AQIPVTLPTW DEVIGRDVKA EDFNGWLLNR ILRDKGTPVY TIHAEVEGCA 250 260 270 280 290 YQHNFVDLLK RAAQEGVTFC PLSELLSETL PLGQVVRGNI AGREGWLGCQ QIAGSR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-amino-4-deoxy-L-arabinose: identification and function of UDP-4-deoxy-4-formamido-L-arabinose." Breazeale S.D., Ribeiro A.A., McClerren A.L., Raetz C.R.H. J. Biol. Chem. 280:14154-14167(2005) [PubMed: 15695810] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli." Yan A., Guan Z., Raetz C.R.H. J. Biol. Chem. 282:36077-36089(2007) [PubMed: 17928292] [Abstract] Cited for: PATHWAY. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U00096 Genomic DNA. Translation: AAC75316.1. AP009048 Genomic DNA. Translation: BAE76673.1.
PIR	F64996.
RefSeq	AP_002853.1. NP_416759.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P76472. 1 interaction.
STRING	P76472.
Genome annotation databases
GeneID	945334.
GenomeReviews	Gene locus JW2250 in contig AP009048_GR. Gene locus b2256 in contig U00096_GR.
KEGG	ecj:JW2250. eco:b2256.
Organism-specific databases
EchoBASE	EB3845.
EcoGene	EG14092. arnD.
CMR	Search...
Phylogenomic databases
HOGENOM	HBG298639.
OMA	CSAVAGW.
Enzyme and pathway databases
BioCyc	EcoCyc:G7169-MON. ECOL168927:B2256-MON.
Gene expression databases
Genevestigator	P76472.
Family and domain databases
HAMAP	MF_01870. [Tree]
InterPro	IPR011330. Glyco_hydro/deAcase_b/a-brl. IPR002509. Polysac_deacetylase. [Graphical view]
Gene3D	G3DSA:3.20.20.370. Polysac_deacetylase. 1 hit.
Pfam	PF01522. Polysacc_deac_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARND_ECOLI

Accession

Primary (citable) accession number: P76472
Secondary accession number(s): Q2MAN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	February 1, 1997
Last modified:	December 15, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)