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

Details

Name
UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase
Synonyms
  • 2.6.1.87
  • pbgP
  • pbgP1
  • pmrH
  • Polymyxin resistance protein PmrH
  • UDP-(beta-L-threo-pentapyranosyl-4''-ulose diphosphate) aminotransferase
  • UDP-4-amino-4-deoxy-L-arabinose aminotransferase
  • UDP-Ara4O aminotransferase
Gene Name
arnB
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Amino acid sequence
>lcl|BSEQ0003002|UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase
MSDFLPFSRPAMGAEELAAVKTVLDSGWITTGPKNQELEAAFCRLTGNQYAVAVSSATAG
MHIALMALGIGEGDEVITPSMTWVSTLNMIVLLGANPVMVDVDRDTLMVTPEHIEAAITP
QTKAIIPVHYAGAPADLDAIYALGERYGIPVIEDAAHATGTSYKGRHIGARGTAIFSFHA
IKNITCAEGGIVVTDNPQFADKLRSLKFHGLGVDAWDRQSGGRAPQAEVLAPGYKYNLPD
LNAAIALAQLQKLDALNARRAAIAAQYHQAMADLPFQPLSLPSWEHIHAWHLFIIRVDEA
RCGITRDALMASLKTKGIGTGLHFRAAHTQKYYRERFPTLTLPDTEWNSERICSLPLFPD
MTESDFDRVITALHQIAGQ
Number of residues
379
Molecular Weight
41164.65
Theoretical pI
6.27
GO Classification
Functions
transaminase activity
Processes
lipid A biosynthetic process / lipopolysaccharide biosynthetic process / response to antibiotic
General Function
Transaminase activity
Specific Function
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).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0019127|UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase (arnB)
ATGTCGGACTTTTTGCCTTTCTCCCGTCCGGCGATGGGCGCGGAAGAGCTTGCTGCCGTT
AAGACCGTACTGGACTCAGGTTGGATAACAACCGGCCCGAAAAATCAGGAACTGGAAGCG
GCGTTTTGTCGGCTAACTGGCAATCAATATGCCGTTGCCGTCAGTTCAGCCACTGCCGGT
ATGCACATCGCGTTGATGGCGCTGGGCATTGGTGAAGGCGACGAGGTCATTACACCGTCA
ATGACGTGGGTTTCTACGCTAAATATGATCGTTTTACTCGGCGCGAACCCCGTCATGGTC
GATGTCGATCGCGATACGCTGATGGTCACGCCTGAACATATCGAAGCCGCGATTACGCCA
CAAACCAAAGCAATTATCCCCGTCCACTACGCTGGCGCGCCCGCCGATCTGGACGCTATT
TACGCTCTTGGCGAGCGTTATGGCATTCCAGTGATTGAAGACGCGGCGCACGCGACAGGA
ACCAGCTACAAAGGTCGCCACATTGGCGCCCGGGGCACCGCGATTTTCTCCTTCCACGCC
ATTAAGAACATTACCTGCGCTGAAGGCGGTATCGTCGTCACGGATAACCCGCAATTCGCC
GATAAACTGCGCAGTCTCAAGTTTCACGGGCTTGGCGTTGATGCCTGGGATCGACAGAGC
GGGGGACGCGCGCCACAAGCGGAAGTCCTGGCGCCGGGCTACAAATATAATTTGCCCGAC
CTCAACGCCGCTATCGCGCTTGCCCAGTTACAGAAACTGGATGCGCTTAACGCTCGACGC
GCCGCCATCGCAGCGCAGTACCACCAGGCAATGGCAGACCTGCCTTTTCAGCCTCTGAGC
CTTCCGTCGTGGGAGCATATTCACGCCTGGCATTTATTCATTATCCGGGTCGATGAAGCC
CGCTGCGGTATTACCCGGGATGCTCTGATGGCATCGCTGAAAACGAAAGGCATCGGCACA
GGGCTGCATTTCCGCGCCGCGCATACGCAAAAATATTATCGCGAACGTTTCCCAACGCTC
ACGCTGCCTGACACCGAGTGGAACAGCGAGCGGATCTGCTCACTGCCGCTCTTCCCGGAC
ATGACCGAGAGTGACTTTGATCGAGTCATTACCGCCCTTCATCAGATAGCAGGACAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ8ZNF3
UniProtKB Entry NameARNB_SALTY
GenBank Protein ID2921419
GenBank Gene IDAF036677
General References
  1. Gunn JS, Lim KB, Krueger J, Kim K, Guo L, Hackett M, Miller SI: PmrA-PmrB-regulated genes necessary for 4-aminoarabinose lipid A modification and polymyxin resistance. Mol Microbiol. 1998 Mar;27(6):1171-82. [Article]
  2. McClelland M, Sanderson KE, Spieth J, Clifton SW, Latreille P, Courtney L, Porwollik S, Ali J, Dante M, Du F, Hou S, Layman D, Leonard S, Nguyen C, Scott K, Holmes A, Grewal N, Mulvaney E, Ryan E, Sun H, Florea L, Miller W, Stoneking T, Nhan M, Waterston R, Wilson RK: Complete genome sequence of Salmonella enterica serovar Typhimurium LT2. Nature. 2001 Oct 25;413(6858):852-6. [Article]
  3. Wosten MM, Groisman EA: Molecular characterization of the PmrA regulon. J Biol Chem. 1999 Sep 17;274(38):27185-90. [Article]
  4. Noland BW, Newman JM, Hendle J, Badger J, Christopher JA, Tresser J, Buchanan MD, Wright TA, Rutter ME, Sanderson WE, Muller-Dieckmann HJ, Gajiwala KS, Buchanan SG: Structural studies of Salmonella typhimurium ArnB (PmrH) aminotransferase: a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. Structure. 2002 Nov;10(11):1569-80. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02142Pyridoxamine-5'-PhosphateexperimentalunknownDetails
DB02038D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamideexperimentalunknownDetails