A8A2C3 (ARND_ECOHS) Reviewed, UniProtKB/Swiss-Prot

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
Ordered Locus Names:	EcHS_A2401

Organism

Escherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]

Taxonomic identifier

331112 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	296 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Antibiotic resistance Lipid A biosynthesis Lipid biosynthesis Lipid metabolism Lipopolysaccharide biosynthesis
Molecular function	Hydrolase
Technical term	Complete 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 – 296	296	Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD HAMAP-Rule MF_01870		PRO_0000383513

Sequences

	Sequence		Length	Mass (Da)
	A8A2C3 [UniParc]. Last modified October 23, 2007. 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

[1]

"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000802 Genomic DNA. Translation: ABV06677.1.
RefSeq	YP_001459060.1. NC_009800.1.
3D structure databases
ProteinModelPortal	A8A2C3.
ModBase	Search...
Protein-protein interaction databases
STRING	331112.EcHS_A2401.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABV06677; ABV06677; EcHS_A2401.
GeneID	5592532.
KEGG	ecx:EcHS_A2401.
PATRIC	18314780. VBIEscCol77814_2352.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0726.
HOGENOM	HOG000261199.
KO	K13014.
OMA	HHGWQAN.
ProtClustDB	PRK15394.
Enzyme and pathway databases
BioCyc	ECOL331112:GHHI-2387-MONOMER.
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_ECOHS

Accession

Primary (citable) accession number: A8A2C3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	October 23, 2007
Last modified:	May 29, 2013
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program