Bifunctional polymyxin resistance protein ArnA

Details

Name
Bifunctional polymyxin resistance protein ArnA
Synonyms
  • pmrI
  • Polymyxin resistance protein PmrI
  • yfbG
Gene Name
arnA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011275|Bifunctional polymyxin resistance protein ArnA
MKTVVFAYHDMGCLGIEALLAAGYEISAIFTHTDNPGEKAFYGSVARLAAERGIPVYAPD
NVNHPLWVERIAQLSPDVIFSFYYRHLIYDEILQLAPAGAFNLHGSLLPKYRGRAPLNWV
LVNGETETGVTLHRMVKRADAGAIVAQLRIAIAPDDIAITLHHKLCHAARQLLEQTLPAI
KHGNILEIAQRENEATCFGRRTPDDSFLEWHKPASVLHNMVRAVADPWPGAFSYVGNQKF
TVWSSRVHPHASKAQPGSVISVAPLLIACGDGALEIVTGQAGDGITMQGSQLAQTLGLVQ
GSRLNSQPACTARRRTRVLILGVNGFIGNHLTERLLREDHYEVYGLDIGSDAISRFLNHP
HFHFVEGDISIHSEWIEYHVKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLRIIRYC
VKYRKRIIFPSTSEVYGMCSDKYFDEDHSNLIVGPVNKPRWIYSVSKQLLDRVIWAYGEK
EGLQFTLFRPFNWMGPRLDNLNAARIGSSRAITQLILNLVEGSPIKLIDGGKQKRCFTDI
RDGIEALYRIIENAGNRCDGEIINIGNPENEASIEELGEMLLASFEKHPLRHHFPPFAGF
RVVESSSYYGKGYQDVEHRKPSIRNAHRCLDWEPKIDMQETIDETLDFFLRTVDLTDKPS
Number of residues
660
Molecular Weight
74288.175
Theoretical pI
6.86
GO Classification
Functions
hydroxymethyl-, formyl- and related transferase activity / NAD+ binding / oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor / UDP-glucuronate decarboxylase activity
Processes
lipid A biosynthetic process / lipopolysaccharide biosynthetic process / response to antibiotic / UDP-D-xylose biosynthetic process
General Function
Udp-glucuronate decarboxylase activity
Specific Function
Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0011276|Bifunctional polymyxin resistance protein ArnA (arnA)
ATGAAAACCGTCGTTTTTGCCTACCACGATATGGGATGCCTCGGTATTGAAGCCCTGCTG
GCTGCCGGTTACGAAATTAGCGCCATTTTTACCCATACTGATAATCCCGGTGAAAAAGCC
TTTTATGGTTCGGTGGCTCGTCTGGCGGCGGAAAGAGGCATTCCGGTTTATGCGCCGGAT
AACGTTAATCATCCGCTGTGGGTGGAACGCATTGCCCAACTGTCGCCAGATGTGATTTTC
TCTTTTTATTATCGCCATCTTATTTACGACGAAATTTTGCAGCTCGCTCCCGCAGGTGCA
TTTAATCTGCATGGTTCGCTGTTACCAAAATATCGTGGTCGCGCGCCGCTGAACTGGGTG
CTGGTCAACGGTGAAACGGAAACTGGCGTTACATTGCACCGAATGGTGAAACGTGCCGAT
GCCGGGGCCATTGTGGCGCAACTGCGCATTGCCATTGCGCCAGACGATATCGCTATTACG
CTGCATCATAAATTGTGCCATGCCGCGCGCCAGCTACTGGAACAGACATTACCCGCCATT
AAACACGGTAATATTCTGGAAATCGCCCAGCGCGAAAACGAAGCCACCTGTTTTGGTCGC
AGAACGCCGGATGACAGTTTCCTTGAATGGCATAAACCGGCATCCGTACTGCACAACATG
GTACGTGCCGTTGCCGATCCGTGGCCGGGTGCCTTCAGCTATGTTGGCAATCAGAAATTC
ACCGTCTGGTCGTCGCGTGTTCATCCTCATGCCAGCAAAGCACAGCCGGGGAGCGTGATT
TCTGTTGCGCCACTGCTGATTGCCTGTGGCGATGGCGCGCTGGAAATCGTCACCGGACAG
GCGGGCGACGGCATTACTATGCAGGGCTCGCAATTAGCGCAGACGCTGGGCCTGGTGCAA
GGTTCACGCTTGAATAGCCAGCCTGCCTGCACCGCCCGACGCCGTACCCGGGTACTCATC
CTCGGGGTGAATGGCTTTATTGGCAACCATCTGACAGAACGCCTGCTGCGCGAAGATCAT
TATGAAGTTTACGGTCTGGATATTGGCAGCGATGCGATAAGCCGTTTTCTGAATCATCCG
CATTTTCACTTTGTTGAAGGCGATATCAGTATTCATTCCGAATGGATTGAGTATCATGTC
AAAAAATGTGATGTCGTCTTGCCGCTGGTGGCGATAGCCACGCCGATTGAATATACCCGC
AACCCGCTGCGCGTATTTGAACTCGATTTTGAAGAGAATCTGCGCATTATCCGCTACTGC
GTGAAGTACCGTAAGCGAATCATCTTCCCGTCAACTTCAGAAGTTTATGGGATGTGTAGC
GATAAATACTTCGATGAGGACCATTCTAATTTAATCGTCGGCCCGGTGAATAAACCACGC
TGGATTTATTCGGTATCAAAACAATTACTTGATCGGGTGATCTGGGCCTATGGCGAAAAA
GAGGGTTTACAGTTCACCCTCTTCCGCCCGTTTAACTGGATGGGACCACGACTGGATAAC
CTTAATGCAGCGCGAATTGGCAGCTCCCGCGCTATTACGCAACTCATTCTCAATCTGGTA
GAAGGTTCACCGATTAAGCTGATTGATGGCGGAAAACAAAAACGCTGCTTTACTGATATT
CGCGATGGTATCGAGGCGTTATACCGCATTATCGAAAATGCGGGAAATCGCTGCGACGGT
GAAATTATCAACATTGGCAATCCTGAGAACGAAGCGAGCATTGAGGAACTGGGCGAGATG
CTGCTGGCGAGCTTCGAAAAACATCCGCTGCGCCATCATTTCCCACCGTTTGCGGGCTTT
CGCGTTGTCGAAAGTAGCAGCTACTACGGCAAAGGATATCAGGACGTAGAGCATCGTAAA
CCGAGCATCCGCAATGCCCACCGCTGCCTGGACTGGGAGCCGAAAATTGATATGCAGGAA
ACCATCGACGAAACGCTGGATTTCTTCCTGCGCACCGTTGATCTTACGGATAAACCATCA
TGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP77398
UniProtKB Entry NameARNA_ECOLI
GenBank Protein ID16555376
GenBank Gene IDAY057445
General References
  1. Breazeale SD, Ribeiro AA, Raetz CR: Oxidative decarboxylation of UDP-glucuronic acid in extracts of polymyxin-resistant Escherichia coli. Origin of lipid a species modified with 4-amino-4-deoxy-L-arabinose. J Biol Chem. 2002 Jan 25;277(4):2886-96. Epub 2001 Nov 8. [Article]
  2. Yamamoto Y, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kimura S, Kitagawa M, Makino K, Miki T, Mitsuhashi N, Mizobuchi K, Mori H, Nakade S, Nakamura Y, Nashimoto H, Oshima T, Oyama S, Saito N, Sampei G, Satoh Y, Sivasundaram S, Tagami H, Horiuchi T, et al.: Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features. DNA Res. 1997 Apr 28;4(2):91-113. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Winfield MD, Groisman EA: Phenotypic differences between Salmonella and Escherichia coli resulting from the disparate regulation of homologous genes. Proc Natl Acad Sci U S A. 2004 Dec 7;101(49):17162-7. Epub 2004 Nov 29. [Article]
  6. Breazeale SD, Ribeiro AA, McClerren AL, Raetz CR: 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. J Biol Chem. 2005 Apr 8;280(14):14154-67. Epub 2005 Jan 28. [Article]
  7. Yan A, Guan Z, Raetz CR: An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli. J Biol Chem. 2007 Dec 7;282(49):36077-89. Epub 2007 Oct 10. [Article]
  8. Gatzeva-Topalova PZ, May AP, Sousa MC: Crystal structure of Escherichia coli ArnA (PmrI) decarboxylase domain. A key enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance. Biochemistry. 2004 Oct 26;43(42):13370-9. [Article]
  9. Gatzeva-Topalova PZ, May AP, Sousa MC: Crystal structure and mechanism of the Escherichia coli ArnA (PmrI) transformylase domain. An enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance. Biochemistry. 2005 Apr 12;44(14):5328-38. [Article]
  10. Williams GJ, Breazeale SD, Raetz CR, Naismith JH: Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis. J Biol Chem. 2005 Jun 17;280(24):23000-8. Epub 2005 Apr 4. [Article]
  11. Gatzeva-Topalova PZ, May AP, Sousa MC: Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance. Structure. 2005 Jun;13(6):929-42. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03256(6R)-Folinic acidexperimentalunknownDetails
DB03685Uridine monophosphateexperimentalunknownDetails