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Protein

Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD

Gene

arnD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).1 Publication

Catalytic activityi

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.UniRule annotation1 Publication

Pathwayi

GO - Molecular functioni

  1. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides Source: UniProtKB-HAMAP

GO - Biological processi

  1. 4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate biosynthetic process Source: UniProtKB-UniPathway
  2. lipid A biosynthetic process Source: UniProtKB-HAMAP
  3. lipopolysaccharide biosynthetic process Source: UniProtKB-UniPathway
  4. response to antibiotic Source: UniProtKB-KW
  5. response to iron(III) ion Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance, Lipid A biosynthesis, Lipid biosynthesis, Lipid metabolism, Lipopolysaccharide biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:G7169-MONOMER.
ECOL316407:JW2250-MONOMER.
UniPathwayiUPA00030.
UPA00036; UER00496.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnDUniRule annotation (EC:3.5.1.n3UniRule annotation)
Gene namesi
Name:arnDUniRule annotation
Synonyms:pmrJ, yfbH
Ordered Locus Names:b2256, JW2250
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14092. arnD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 296296Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnDPRO_0000169176Add
BLAST

Proteomic databases

PaxDbiP76472.
PRIDEiP76472.

Expressioni

Inductioni

Induced by BasR.By similarity

Gene expression databases

GenevestigatoriP76472.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
groLP0A6F51EBI-1128209,EBI-543750

Protein-protein interaction databases

IntActiP76472. 1 interaction.
STRINGi511145.b2256.

Structurei

3D structure databases

ProteinModelPortaliP76472.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 260259NodB homologyUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the polysaccharide deacetylase family. ArnD deformylase subfamily.UniRule annotation
Contains 1 NodB homology domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0726.
HOGENOMiHOG000261199.
InParanoidiP76472.
KOiK13014.
OMAiLHAWDHF.
OrthoDBiEOG6423D0.
PhylomeDBiP76472.

Family and domain databases

Gene3Di3.20.20.370. 2 hits.
HAMAPiMF_01870. ArnD.
InterProiIPR023557. ArnD.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR002509. Polysac_deacetylase.
[Graphical view]
PfamiPF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
SUPFAMiSSF88713. SSF88713. 2 hits.
PROSITEiPS51677. NODB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P76472-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKVGLRIDV DTFRGTREGV PRLLEILSKH NIQASIFFSV GPDNMGRHLW
60 70 80 90 100
RLVKPQFLWK MLRSNAASLY GWDILLAGTA WPGKEIGHAN ADIIREAAKH
110 120 130 140 150
HEVGLHAWDH HAWQARSGNW DRQTMIDDIA RGLRTLEEII GQPVTCSAAA
160 170 180 190 200
GWRADQKVIE AKEAFHLRYN SDCRGAMPFR PLLESGNPGT AQIPVTLPTW
210 220 230 240 250
DEVIGRDVKA EDFNGWLLNR ILRDKGTPVY TIHAEVEGCA YQHNFVDLLK
260 270 280 290
RAAQEGVTFC PLSELLSETL PLGQVVRGNI AGREGWLGCQ QIAGSR
Length:296
Mass (Da):33,112
Last modified:February 1, 1997 - v1
Checksum:iDDD0BEE55581DE3C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75316.1.
AP009048 Genomic DNA. Translation: BAE76673.1.
PIRiF64996.
RefSeqiNP_416759.1. NC_000913.3.
YP_490495.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75316; AAC75316; b2256.
BAE76673; BAE76673; BAE76673.
GeneIDi12931504.
945334.
KEGGiecj:Y75_p2219.
eco:b2256.
PATRICi32119877. VBIEscCol129921_2348.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75316.1.
AP009048 Genomic DNA. Translation: BAE76673.1.
PIRiF64996.
RefSeqiNP_416759.1. NC_000913.3.
YP_490495.1. NC_007779.1.

3D structure databases

ProteinModelPortaliP76472.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP76472. 1 interaction.
STRINGi511145.b2256.

Proteomic databases

PaxDbiP76472.
PRIDEiP76472.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75316; AAC75316; b2256.
BAE76673; BAE76673; BAE76673.
GeneIDi12931504.
945334.
KEGGiecj:Y75_p2219.
eco:b2256.
PATRICi32119877. VBIEscCol129921_2348.

Organism-specific databases

EchoBASEiEB3845.
EcoGeneiEG14092. arnD.

Phylogenomic databases

eggNOGiCOG0726.
HOGENOMiHOG000261199.
InParanoidiP76472.
KOiK13014.
OMAiLHAWDHF.
OrthoDBiEOG6423D0.
PhylomeDBiP76472.

Enzyme and pathway databases

UniPathwayiUPA00030.
UPA00036; UER00496.
BioCyciEcoCyc:G7169-MONOMER.
ECOL316407:JW2250-MONOMER.

Miscellaneous databases

PROiP76472.

Gene expression databases

GenevestigatoriP76472.

Family and domain databases

Gene3Di3.20.20.370. 2 hits.
HAMAPiMF_01870. ArnD.
InterProiIPR023557. ArnD.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR002509. Polysac_deacetylase.
[Graphical view]
PfamiPF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
SUPFAMiSSF88713. SSF88713. 2 hits.
PROSITEiPS51677. NODB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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(2005) [PubMed] [Europe PMC] [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(2004) [PubMed] [Europe PMC] [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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PATHWAY.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Entry informationi

Entry nameiARND_ECOLI
AccessioniPrimary (citable) accession number: P76472
Secondary accession number(s): Q2MAN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: February 1, 1997
Last modified: January 7, 2015
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.