Q6D2F2 (ARND_ERWCT) 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:	ECA3143

Organism

Erwinia carotovora subsp. atroseptica (strain SCRI 1043 / ATCC BAA-672) (Pectobacterium atrosepticum) [Complete proteome] [HAMAP]

Taxonomic identifier

218491 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium › Erwinia carotovora subsp. atroseptica

Protein attributes

Sequence length	297 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 – 297	297	Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD HAMAP-Rule MF_01870		PRO_0000383493

Sequences

	Sequence		Length	Mass (Da)
	Q6D2F2 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 83F59EC57E0954AA	FASTA	297	33,439
	10 20 30 40 50 60 MTRVGLRIDV DTWRGTRDGV PALLKVLAEF DIQASFFFSV GPDNMGRHLW RLLRPRFLWK 70 80 90 100 110 120 MLRSNAASLY GWDILLAGTA WPGRHIGARF GSLIRQTHDA GHEVGLHSWD HHGWQANVAR 130 140 150 160 170 180 WSDAQLAAQF HEGMDALTQI LPSPVRCSAV AGWRADARVV EMKQRWNLDY NSDCRGTQPF 190 200 210 220 230 240 RPRLKNGGLG TTQIPVTLPT YDEVIGERVS DGEFNDFILD AIEQDRGVPV YTIHAEVEGG 250 260 270 280 290 AKLALFRQLL LLARQRHIEF CPLSSLLPDD STTLPVGRIE RAPFPGREGW LGVQTEE

References

[1]

"Genome sequence of the enterobacterial phytopathogen Erwinia carotovora subsp. atroseptica and characterization of virulence factors." Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J., Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K., Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z. , Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K. Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SCRI 1043 / ATCC BAA-672.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX950851 Genomic DNA. Translation: CAG76042.1.
RefSeq	YP_051233.1. NC_004547.2.
3D structure databases
ProteinModelPortal	Q6D2F2.
ModBase	Search...
Protein-protein interaction databases
STRING	218491.ECA3143.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAG76042; CAG76042; ECA3143.
GeneID	2882942.
KEGG	eca:ECA3143.
PATRIC	20481609. VBIPecAtr54885_3180.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0726.
HOGENOM	HOG000261199.
KO	K13014.
OMA	HHGWQAN.
ProtClustDB	PRK15394.
Enzyme and pathway databases
BioCyc	PATR218491:GJNB-3193-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_ERWCT

Accession

Primary (citable) accession number: Q6D2F2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program