Bifunctional polymyxin resistance protein ArnA (P77398)

Identification
Name:Bifunctional polymyxin resistance protein ArnA
Synonyms:
  • Polymyxin resistance protein PmrI
  • UDP-4-amino-4-deoxy-L-arabinose formyltransferase
  • ArnAFT
  • UDP-L-Ara4N formyltransferase
  • UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating
  • ArnADH
  • UDP-GlcUA decarboxylase
  • UDP-glucuronic acid dehydrogenase
Gene Name:arnA
Enzyme Class:
Biological Properties
General Function:Involved in hydroxymethyl-, formyl- and related transferase 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
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
  • Amino sugar and nucleotide sugar metabolism ec00520
KEGG Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0NAD + 1.0Uridine diphosphate glucuronic acid → 1.0Carbon dioxide + 1.0NADH + 1.0UDP-4-Keto-pyranose
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0N10-Formyl-THF + 1.0Uridine 5''-diphospho-{beta}-4-deoxy-4-amino-L-arabinose ↔ 1.0Hydrogen ion + 1.0Tetrahydrofolic acid + 1.0Uridine 5''-diphospho-{beta}-4-deoxy-4-formamido-L-arabinose
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Uridine diphosphate glucuronic acid + 1.0NAD ↔ 1.0UDP-4-Keto-pyranose + 1.0Carbon dioxide + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0N10-Formyl-THF + 1.0Uridine 5''-diphospho-{beta}-4-deoxy-4-amino-L-arabinose ↔ 1.0Tetrahydrofolic acid + 1.0Uridine 5''-diphospho-{beta}-4-deoxy-4-formamido-L-arabinose
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0UDP-Glucuronic acid + 1.0NAD → 1.0Carbon dioxide + 1.0NADH + 1.0UDP-β-L-threo-pentapyranos-4-ulose
ReactionCard
1.0Thumb+1.0an N10-formyl-tetrahydrofolate+1.0Thumb → 1.0Thumb+1.0Thumb+1.0a tetrahydrofolate+1.0Thumb
1.0Uridine 5''-diphospho-{beta}-4-deoxy-4-amino-L-arabinose + 1.0an N10-formyl-tetrahydrofolate + 1.0N10-Formyl-THF → 1.0UDP-4-Deoxy-4-formamido-beta-L-arabinose + 1.0Hydrogen ion + 1.0a tetrahydrofolate + 1.0Tetrahydrofolic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0NAD + 1.0Uridine diphosphate glucuronic acid → 1.0Carbon dioxide + 1.0NADH + 1.0UDP-4-Keto-pyranose
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0N10-Formyl-THF + 1.0Uridine 5''-diphospho-{beta}-4-deoxy-4-amino-L-arabinose ↔ 1.0Hydrogen ion + 1.0Tetrahydrofolic acid + 1.0Uridine 5''-diphospho-{beta}-4-deoxy-4-formamido-L-arabinose
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0UDP-Glucuronic acid + 1.0NAD → 1.0UDP-beta-L-Threo-pentapyranos-4-ulose + 1.0Carbon dioxide + 1.0NADH
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N10-Formyl-THF + 1.04-Amino-4-deoxy-L-arabinose → 1.0Tetrahydrofolic acid + 1.0UDP-4-Deoxy-4-formamido-beta-L-arabinose
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB214974-Amino-4-deoxy-L-arabinoseMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00972N10-Formyl-THFMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB01846Tetrahydrofolic acidMetaboCard
ECMDB23199UDP-4-Deoxy-4-formamido-beta-L-arabinoseMetaboCard
ECMDB21293UDP-4-Keto-pyranoseMetaboCard
ECMDB23202UDP-beta-L-Threo-pentapyranos-4-uloseMetaboCard
ECMDB01384UDP-Glucuronic acidMetaboCard
ECMDB24240UDP-β-L-threo-pentapyranos-4-uloseMetaboCard
ECMDB21366Uridine 5''-diphospho-{beta}-4-deoxy-4-amino-L-arabinoseMetaboCard
ECMDB21367Uridine 5''-diphospho-{beta}-4-deoxy-4-formamido-L-arabinoseMetaboCard
ECMDB04166Uridine diphosphate glucuronic acidMetaboCard
GO Classification:
Function
binding
catalytic activity
coenzyme binding
cofactor binding
glycine hydroxymethyltransferase activity
hydroxymethyl-, formyl- and related transferase activity
methyltransferase activity
transferase activity
transferase activity, transferring one-carbon groups
Process
biosynthetic process
cellular metabolic process
metabolic process
Gene Properties
Blattner:b2255
Gene OrientationClockwise
Centisome Percentage:51.00
Left Sequence End2366061
Right Sequence End2368043
Gene Sequence:
>1983 bp
GTGAGTAAACGAATTGCGCTTTTCCCGGCGTTATTGCTGGCGCTGTTAGTGATTGTCGCT
ACGGCGCTCACCTGGATGAACTTCTCGCAGGCGCTGCCGCGTAGCCAGTGGGCGCAGGCT
GCCTGGTCGCCGGATATTGACGTCATCGAGCAGATGATTTTTCACTACAGCTTGTTGCCG
CGTCTGGCGATTTCGCTGCTGGTGGGCGCGGGTCTGGGGCTGGTGGGCGTGCTGTTTCAG
CAAGTGCTGCGTAACCCGCTGGCGGAGCCGACGACGCTTGGCGTTGCTACAGGCGCGCAA
CTGGGGATTACCGTCACTACGCTCTGGGCGATCCCTGGTGCGATGGCGAGCCAGTTTGCT
GCGCAGGCAGGGGCTTGTGTTGTTGGCTTAATTGTCTTTGGCGTCGCGTGGGGGAAACGG
CTGTCGCCGGTAACGCTGATTCTCGCGGGGTTGGTAGTGAGCCTTTATTGCGGCGCAATC
AATCAGTTACTGGTTATCTTCCATCATGACCAACTGCAAAGCATGTTTCTGTGGAGCACT
GGAACGCTGACGCAAACCGACTGGGGCGGCGTTGAGCGTTTATGGCCGCAGCTGCTGGGC
GGTGTGATGCTGACGTTGCTGCTACTTCGTCCGTTAACCCTGATGGGGCTTGATGATGGC
GTGGCGCGCAATCTCGGGCTGGCCTTGTCGCTTGCGCGTCTGGCAGCGCTGTCGCTGGCG
ATTGTCATCAGTGCGCTGCTGGTGAACGCTGTGGGGATTATCGGCTTTATCGGGTTGTTC
GCGCCGCTGCTGGCAAAAATGCTGGGGGCGCGGCGTCTGCTGCCACGACTGATGCTGGCG
TCGTTGATTGGTGCGCTGATCCTCTGGCTTTCCGATCAAATCATCCTCTGGCTGACTCGC
GTGTGGATGGAAGTGTCCACCGGTTCGGTCACTGCGTTGATCGGTGCGCCGCTGCTACTG
TGGCTGTTGCCGCGTTTACGCAGCATTAGCGCGCCGGATATGAAGGTCAACGATCGTGTC
GCGGCTGAACGCCAACATGTGCTGGCGTTTGCCCTCGCGGGCGGCGTGCTGCTGTTGATG
GCTGTGGTGGTGGCGCTGTCGTTTGGTCGTGATGCGCACGGCTGGACGTGGGCGAGCGGG
GCGTTGCTCGAGGATTTAATGCCCTGGCGCTGGCCGCGAATTATGGCGGCGCTGTTTGCG
GGCGTCATGCTGGCGGTGGCGGGCTGTATTATTCAGCGACTGACCGGAAACCCGATGGCA
AGCCCGGAAGTGCTGGGGATTAGCTCCGGCGCGGCGTTTGGCGTGGTGTTGATGCTGTTT
CTGGTGCCGGGTAATGCCTTTGGCTGGCTGTTACCTGCAGGCAGTCTCGGCGCGGCGGTG
ACGCTGTTGATCATTATGATCGCCGCCGGCCGCGGTGGATTTTCCCCACACCGTATGTTA
CTGGCGGGGATGGCGTTAAGCACCGCGTTCACCATGCTTTTGATGATGTTGCAGGCAAGT
GGTGACCCGCGAATGGCGCAAGTGCTGACCTGGATTTCCGGTTCGACCTACAACGCGACC
GATGCGCAGGTCTGGCGCACCGGAATTGTGATGGTGATTTTGCTGGCGATTACCCCGCTG
TGCCGCCGCTGGCTGACCATTTTACCGCTGGGTGGTGATACCGCCCGAGCCGTAGGAATG
GCGCTGACGCCGACGCGAATTGCGCTGCTGCTGTTAGCGGCTTGCCTGACGGCGACCGCG
ACGATGACTATTGGACCGTTGAGTTTTGTTGGTTTAATGGCACCGCATATTGCGCGGATG
ATGGGCTTTCGACGGACGATGCCACACATCGTAATTTCGGCGCTGGTGGGTGGTTTACTG
CTGGTGTTCGCTGACTGGTGTGGGCGGATGGTGCTGTTTCCATTCCAGATCCCGGCGGGG
CTGCTGTCAACCTTTATCGGCGCGCCATATTTTATCTATTTGTTGAGAAAGCAGAGCCGT
TAA
Protein Properties
Pfam Domain Function:
Protein Residues:660
Protein Molecular Weight:74288
Protein Theoretical pI:7
PDB File:1U9J
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Bifunctional polymyxin resistance protein ArnA
MKTVVFAYHDMGCLGIEALLAAGYEISAIFTHTDNPGEKAFYGSVARLAAERGIPVYAPD
NVNHPLWVERIAQLSPDVIFSFYYRHLIYDEILQLAPAGAFNLHGSLLPKYRGRAPLNWV
LVNGETETGVTLHRMVKRADAGAIVAQLRIAIAPDDIAITLHHKLCHAARQLLEQTLPAI
KHGNILEIAQRENEATCFGRRTPDDSFLEWHKPASVLHNMVRAVADPWPGAFSYVGNQKF
TVWSSRVHPHASKAQPGSVISVAPLLIACGDGALEIVTGQAGDGITMQGSQLAQTLGLVQ
GSRLNSQPACTARRRTRVLILGVNGFIGNHLTERLLREDHYEVYGLDIGSDAISRFLNHP
HFHFVEGDISIHSEWIEYHVKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLRIIRYC
VKYRKRIIFPSTSEVYGMCSDKYFDEDHSNLIVGPVNKPRWIYSVSKQLLDRVIWAYGEK
EGLQFTLFRPFNWMGPRLDNLNAARIGSSRAITQLILNLVEGSPIKLIDGGKQKRCFTDI
RDGIEALYRIIENAGNRCDGEIINIGNPENEASIEELGEMLLASFEKHPLRHHFPPFAGF
RVVESSSYYGKGYQDVEHRKPSIRNAHRCLDWEPKIDMQETIDETLDFFLRTVDLTDKPS
References
External Links:
ResourceLink
Uniprot ID:P77398
Uniprot Name:ARNA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674359
PDB ID:1U9J
Ecogene ID:EG14091
Ecocyc:EG14091
ColiBase:b2255
Kegg Gene:b2255
EchoBASE ID:EB3844
CCDB:ARNA_ECOLI
BacMap:16130190
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Breazeale, S. D., Ribeiro, A. A., McClerren, A. L., Raetz, C. R. (2005). "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 280:14154-14167. Pubmed: 15695810
  • Breazeale, S. D., Ribeiro, A. A., Raetz, C. R. (2002). "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 277:2886-2896. Pubmed: 11706007
  • Gatzeva-Topalova, P. Z., May, A. P., Sousa, M. C. (2004). "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 43:13370-13379. Pubmed: 15491143
  • Gatzeva-Topalova, P. Z., May, A. P., Sousa, M. C. (2005). "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 44:5328-5338. Pubmed: 15807526
  • Gatzeva-Topalova, P. Z., May, A. P., Sousa, M. C. (2005). "Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance." Structure 13:929-942. Pubmed: 15939024
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Williams, G. J., Breazeale, S. D., Raetz, C. R., Naismith, J. H. (2005). "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 280:23000-23008. Pubmed: 15809294
  • Winfield, M. D., Groisman, E. A. (2004). "Phenotypic differences between Salmonella and Escherichia coli resulting from the disparate regulation of homologous genes." Proc Natl Acad Sci U S A 101:17162-17167. Pubmed: 15569938
  • 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, a. l. .. (1997). "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 4:91-113. Pubmed: 9205837
  • Yan, A., Guan, Z., Raetz, C. R. (2007). "An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli." J Biol Chem 282:36077-36089. Pubmed: 17928292