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Protein

UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase

Gene

arnB

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of UDP-4-keto-arabinose (UDP-Ara4O) to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides (By similarity).By similarity

Catalytic activityi

UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate = UDP-beta-L-threo-pentapyranos-4-ulose + L-glutamate.

Cofactori

Pathwayi: UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Bifunctional polymyxin resistance protein ArnA (arnA)
  2. UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase (arnB)
  3. Bifunctional polymyxin resistance protein ArnA (arnA)
This subpathway is part of the pathway UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate, the pathway UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis and in Nucleotide-sugar biosynthesis.

Pathwayi: lipopolysaccharide biosynthesis

This protein is involved in the pathway lipopolysaccharide biosynthesis, which is part of Bacterial outer membrane biogenesis.
View all proteins of this organism that are known to be involved in the pathway lipopolysaccharide biosynthesis and in Bacterial outer membrane biogenesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

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

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciSENT99287:GCTI-2312-MONOMER.
UniPathwayiUPA00030.
UPA00032; UER00493.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase (EC:2.6.1.87)
Alternative name(s):
Polymyxin resistance protein PmrH
UDP-(beta-L-threo-pentapyranosyl-4''-ulose diphosphate) aminotransferase
Short name:
UDP-Ara4O aminotransferase
UDP-4-amino-4-deoxy-L-arabinose aminotransferase
Gene namesi
Name:arnB
Synonyms:pbgP, pbgP1, pmrH
Ordered Locus Names:STM2297
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferasePRO_0000110028Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei182 – 1821N6-(pyridoxal phosphate)lysine

Proteomic databases

PaxDbiQ8ZNF3.
PRIDEiQ8ZNF3.

Expressioni

Inductioni

Induced by BasR.1 Publication

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi99287.STM2297.

Structurei

Secondary structure

1
379
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2613Combined sources
Beta strandi30 – 323Combined sources
Helixi33 – 4614Combined sources
Beta strandi49 – 557Combined sources
Helixi57 – 6711Combined sources
Beta strandi75 – 828Combined sources
Helixi84 – 929Combined sources
Beta strandi96 – 1005Combined sources
Turni104 – 1063Combined sources
Helixi111 – 1177Combined sources
Beta strandi122 – 1254Combined sources
Helixi130 – 1323Combined sources
Helixi137 – 14711Combined sources
Beta strandi151 – 1544Combined sources
Beta strandi170 – 1778Combined sources
Beta strandi182 – 1843Combined sources
Beta strandi186 – 1883Combined sources
Beta strandi190 – 1956Combined sources
Helixi197 – 20610Combined sources
Beta strandi228 – 2314Combined sources
Helixi240 – 25112Combined sources
Helixi253 – 27220Combined sources
Beta strandi293 – 2964Combined sources
Helixi299 – 3024Combined sources
Helixi306 – 31510Combined sources
Helixi327 – 3293Combined sources
Helixi331 – 3366Combined sources
Helixi343 – 3497Combined sources
Beta strandi352 – 3554Combined sources
Helixi363 – 37715Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MDOX-ray1.70A1-379[»]
1MDXX-ray1.96A1-379[»]
1MDZX-ray2.07A1-379[»]
ProteinModelPortaliQ8ZNF3.
SMRiQ8ZNF3. Positions 3-378.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8ZNF3.

Family & Domainsi

Sequence similaritiesi

Belongs to the DegT/DnrJ/EryC1 family. ArnB subfamily.Curated

Phylogenomic databases

eggNOGiENOG4105CF4. Bacteria.
COG0399. LUCA.
HOGENOMiHOG000230163.
KOiK07806.
OMAiLHAWHLF.
OrthoDBiEOG6JQH30.
PhylomeDBiQ8ZNF3.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01167. ArnB_transfer.
InterProiIPR022850. ArnB_NH2Trfase.
IPR000653. DegT/StrS_aminotransferase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF01041. DegT_DnrJ_EryC1. 1 hit.
[Graphical view]
PIRSFiPIRSF000390. PLP_StrS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8ZNF3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDFLPFSRP AMGAEELAAV KTVLDSGWIT TGPKNQELEA AFCRLTGNQY
60 70 80 90 100
AVAVSSATAG MHIALMALGI GEGDEVITPS MTWVSTLNMI VLLGANPVMV
110 120 130 140 150
DVDRDTLMVT PEHIEAAITP QTKAIIPVHY AGAPADLDAI YALGERYGIP
160 170 180 190 200
VIEDAAHATG TSYKGRHIGA RGTAIFSFHA IKNITCAEGG IVVTDNPQFA
210 220 230 240 250
DKLRSLKFHG LGVDAWDRQS GGRAPQAEVL APGYKYNLPD LNAAIALAQL
260 270 280 290 300
QKLDALNARR AAIAAQYHQA MADLPFQPLS LPSWEHIHAW HLFIIRVDEA
310 320 330 340 350
RCGITRDALM ASLKTKGIGT GLHFRAAHTQ KYYRERFPTL TLPDTEWNSE
360 370
RICSLPLFPD MTESDFDRVI TALHQIAGQ
Length:379
Mass (Da):41,165
Last modified:June 21, 2005 - v2
Checksum:iE7478E05DA21CDC0
GO

Sequence cautioni

The sequence AAC04770.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAL21198.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti279 – 2791L → V in AAC04770 (PubMed:11677609).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036677 Genomic DNA. Translation: AAC04770.1. Different initiation.
AE006468 Genomic DNA. Translation: AAL21198.1. Different initiation.
RefSeqiNP_461239.2. NC_003197.1.
WP_001279284.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL21198; AAL21198; STM2297.
GeneIDi1253819.
KEGGistm:STM2297.
PATRICi32383205. VBISalEnt20916_2432.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036677 Genomic DNA. Translation: AAC04770.1. Different initiation.
AE006468 Genomic DNA. Translation: AAL21198.1. Different initiation.
RefSeqiNP_461239.2. NC_003197.1.
WP_001279284.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MDOX-ray1.70A1-379[»]
1MDXX-ray1.96A1-379[»]
1MDZX-ray2.07A1-379[»]
ProteinModelPortaliQ8ZNF3.
SMRiQ8ZNF3. Positions 3-378.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM2297.

Proteomic databases

PaxDbiQ8ZNF3.
PRIDEiQ8ZNF3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL21198; AAL21198; STM2297.
GeneIDi1253819.
KEGGistm:STM2297.
PATRICi32383205. VBISalEnt20916_2432.

Phylogenomic databases

eggNOGiENOG4105CF4. Bacteria.
COG0399. LUCA.
HOGENOMiHOG000230163.
KOiK07806.
OMAiLHAWHLF.
OrthoDBiEOG6JQH30.
PhylomeDBiQ8ZNF3.

Enzyme and pathway databases

UniPathwayiUPA00030.
UPA00032; UER00493.
BioCyciSENT99287:GCTI-2312-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ8ZNF3.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01167. ArnB_transfer.
InterProiIPR022850. ArnB_NH2Trfase.
IPR000653. DegT/StrS_aminotransferase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF01041. DegT_DnrJ_EryC1. 1 hit.
[Graphical view]
PIRSFiPIRSF000390. PLP_StrS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PmrA-PmrB-regulated genes necessary for 4-aminoarabinose lipid A modification and polymyxin resistance."
    Gunn J.S., Lim K.B., Krueger J., Kim K., Guo L., Hackett M., Miller S.I.
    Mol. Microbiol. 27:1171-1182(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 14028s / SGSG 2262.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  3. "Molecular characterization of the PmrA regulon."
    Woesten M.M.S.M., Groisman E.A.
    J. Biol. Chem. 274:27185-27190(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: ATCC 14028s / SGSG 2262.
  4. "Structural studies of Salmonella typhimurium ArnB (PmrH) aminotransferase: a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme."
    Noland B.W., Newman J.M., Hendle J., Badger J., Christopher J.A., Tresser J., Buchanan M.D., Wright T.A., Rutter M.E., Sanderson W.E., Mueller-Dieckmann H.-J., Gajiwala K.S., Buchanan S.G.
    Structure 10:1569-1580(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

Entry informationi

Entry nameiARNB_SALTY
AccessioniPrimary (citable) accession number: Q8ZNF3
Secondary accession number(s): O52323
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: June 21, 2005
Last modified: May 11, 2016
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.