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A9R092

- ARND_YERPG

UniProt

A9R092 - ARND_YERPG

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Protein
Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD
Gene
arnD, YpAngola_A2609
Organism
Yersinia pestis bv. Antiqua (strain Angola)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

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 By similarity.UniRule annotation

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 annotation

Pathwayi

GO - Molecular functioni

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

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
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

BioCyciYPES349746:GHPB-2615-MONOMER.
UniPathwayiUPA00030.
UPA00036; UER00496.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD (EC:3.5.1.n3)
Gene namesi
Name:arnD
Ordered Locus Names:YpAngola_A2609
OrganismiYersinia pestis bv. Antiqua (strain Angola)
Taxonomic identifieri349746 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000001204: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 301301Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnDUniRule annotation
PRO_0000383553Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi349746.YpAngola_A2609.

Structurei

3D structure databases

ProteinModelPortaliA9R092.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 261260NodB homology
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0726.
HOGENOMiHOG000261199.
KOiK13014.
OMAiLHAWDHF.
OrthoDBiEOG6423D0.

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.

A9R092-1 [UniParc]FASTAAdd to Basket

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MKQVGLRIDV DTYRGTQYGV PSLLTVLEKH DIRASFFFSV GPDNMGRHLW    50
RLFRPRFLWK MLRSNAASLY GWDILLAGTA WPGKKIAKDF GPLMKAAAMA 100
GHEVGLHAWD HQGWQANVAS WSQQQLTEQV QRGVDTLQQS IGQPISCSAA 150
AGWRADERVL AVKQQFDFSY NSDCRGTHPF RPLLPNGSLG SVQIPVTLPT 200
YDEVVGGEVQ AENFNDFIID AILRDSGVSV YTIHAEVEGM SQAAMFEQLL 250
MRAKQQDIEF CPLSKLLPSD LQLLPVGKVI RAAFPGREGW LGCQSDIKDA 300
E 301
Length:301
Mass (Da):33,504
Last modified:February 5, 2008 - v1
Checksum:iABA3A1132D09A864
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000901 Genomic DNA. Translation: ABX85183.1.
RefSeqiYP_001607016.1. NC_010159.1.

Genome annotation databases

EnsemblBacteriaiABX85183; ABX85183; YpAngola_A2609.
GeneIDi5801081.
KEGGiypg:YpAngola_A2609.
PATRICi18574657. VBIYerPes97331_3101.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000901 Genomic DNA. Translation: ABX85183.1 .
RefSeqi YP_001607016.1. NC_010159.1.

3D structure databases

ProteinModelPortali A9R092.
ModBasei Search...

Protein-protein interaction databases

STRINGi 349746.YpAngola_A2609.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABX85183 ; ABX85183 ; YpAngola_A2609 .
GeneIDi 5801081.
KEGGi ypg:YpAngola_A2609.
PATRICi 18574657. VBIYerPes97331_3101.

Phylogenomic databases

eggNOGi COG0726.
HOGENOMi HOG000261199.
KOi K13014.
OMAi LHAWDHF.
OrthoDBi EOG6423D0.

Enzyme and pathway databases

UniPathwayi UPA00030 .
UPA00036 ; UER00496 .
BioCyci YPES349746:GHPB-2615-MONOMER.

Family and domain databases

Gene3Di 3.20.20.370. 2 hits.
HAMAPi MF_01870. ArnD.
InterProi IPR023557. ArnD.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR002509. Polysac_deacetylase.
[Graphical view ]
Pfami PF01522. Polysacc_deac_1. 1 hit.
[Graphical view ]
SUPFAMi SSF88713. SSF88713. 2 hits.
PROSITEi PS51677. NODB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
    Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
    J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Angola.

Entry informationi

Entry nameiARND_YERPG
AccessioniPrimary (citable) accession number: A9R092
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: February 5, 2008
Last modified: May 14, 2014
This is version 48 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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