Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase (P76473)

Identification
Name:Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
Synonyms:
  • 4-amino-4-deoxy-L-arabinose lipid A transferase
  • Polymyxin resistance protein pmrK
  • Undecaprenyl phosphate-alpha-L-Ara4N transferase
Gene Name:arnT
Enzyme Class:
Biological Properties
General Function:Involved in transferase activity, transferring pentosyl groups
Specific Function:Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides
Cellular Location:Cell inner membrane; Multi-pass membrane protein
SMPDB Pathways:
KEGG Pathways:
  • Cationic antimicrobial peptide (CAMP) resistance eco01503
KEGG Reactions:
1.0Undecaprenyl phosphate alpha-L-Ara4N+1.0Thumb ↔ 1.0Lipid IIA+1.0Thumb
1.0Undecaprenyl phosphate alpha-L-Ara4N + 1.02,3,2'3'-Tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate ↔ 1.0Lipid IIA + 1.0Di-trans,poly-cis-undecaprenyl phosphate
ReactionCard
1.0Undecaprenyl phosphate alpha-L-Ara4N+1.0Di[3-deoxy-D-manno-octulosonyl]-lipid IV(A) ↔ 1.0alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[4-P-L-Ara4N]-lipid IVA+1.0Thumb
1.0Undecaprenyl phosphate alpha-L-Ara4N + 1.0Di[3-deoxy-D-manno-octulosonyl]-lipid IV(A) ↔ 1.0alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[4-P-L-Ara4N]-lipid IVA + 1.0Di-trans,poly-cis-undecaprenyl phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0undecaprenyl phosphate-4-amino-4-deoxy-L-arabinose + 1.0KDO2-Lipid A + 1.02,3,2'3'-Tetrakis(beta-hydroxymyristoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphate ↔ 1.0alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[4-P-L-Ara4N]-lipid A + 1.0Di-trans,poly-cis-undecaprenyl phosphate + 1.0Lipid IIA
ReactionCard
SMPDB Reactions:
2.0Thumb+1.0Thumb → 2.0di-trans,octa-cis-undecaprenyl diphosphate+1.0Thumb
2.04-Amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + 1.0(KDO)2-lipid A → 2.0di-trans,octa-cis-undecaprenyl diphosphate + 1.0L-Ara4N-modified KDO2-Lipid A
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.04-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate → 1.0Thumb+1.0Thumb
1.0KDO2-Lipid A + 1.04-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate → 1.0L-Ara4N-modified KDO2-Lipid A + 1.0Di-trans,poly-cis-undecaprenyl phosphate
ReactionCard
Complex Reactions:
1.0core oligosaccharide lipid A+1.0Thumb → 1.0Thumb+1.0Thumb
1.0core oligosaccharide lipid A + 1.0undecaprenyl phosphate-4-amino-4-deoxy-L-arabinose → 1.04-Amino-4-deoxy-L-arabinose modified core oligosaccharide lipid A + 1.0Undecaprenyl phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB24179(KDO)2-lipid AMetaboCard
ECMDB200572,3,2'3'-Tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphateMetaboCard
ECMDB211362,3,2'3'-Tetrakis(beta-hydroxymyristoyl)-D-glucosaminyl-1,6-beta-D-glucosamine 1,4'-bisphosphateMetaboCard
ECMDB231004-Amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphateMetaboCard
ECMDB214974-Amino-4-deoxy-L-arabinoseMetaboCard
ECMDB211734-Amino-4-deoxy-L-arabinose modified core oligosaccharide lipid AMetaboCard
ECMDB20310Di-trans,poly-cis-undecaprenyl phosphateMetaboCard
ECMDB21235KDO(2)-lipid IV(A)MetaboCard
ECMDB21031KDO2-Lipid AMetaboCard
ECMDB20576L-Ara4N-modified KDO2-Lipid AMetaboCard
ECMDB23023lipid II(A)MetaboCard
ECMDB23844Lipid IIAMetaboCard
ECMDB20208Undecaprenyl phosphateMetaboCard
ECMDB21364undecaprenyl phosphate-4-amino-4-deoxy-L-arabinoseMetaboCard
GO Classification:
Component
cell part
membrane
Function
catalytic activity
mannosyltransferase activity
transferase activity
transferase activity, transferring glycosyl groups
transferase activity, transferring hexosyl groups
Process
macromolecule metabolic process
macromolecule modification
metabolic process
protein amino acid glycosylation
protein amino acid O-linked glycosylation
protein modification process
Gene Properties
Blattner:b2257
Gene OrientationClockwise
Centisome Percentage:51.06
Left Sequence End2368930
Right Sequence End2370582
Gene Sequence:
>1653 bp
ATGAAATTATTGCAGCGGGGCGTGGCGTTAGCGCTGTTAACCACATTTACACTGGCGAGT
GAAACTGCTCTGGCGTATGAGCAGGATAAAACCTACAAAATTACAGTTCTGCATACCAAT
GATCATCATGGGCATTTTTGGCGCAATGAATATGGCGAATATGGTCTGGCGGCGCAAAAA
ACGCTGGTGGATGGTATCCGCAAAGAGGTTGCGGCTGAAGGCGGTAGCGTGCTGCTACTT
TCCGGTGGCGACATTAACACTGGCGTGCCCGAGTCTGACTTACAGGATGCCGAACCTGAT
TTTCGCGGTATGAATCTGGTGGGCTATGACGCGATGGCGATCGGTAATCATGAATTTGAT
AATCCGCTCACCGTATTACGCCAGCAGGAAAAGTGGGCCAAGTTCCCGTTGCTTTCCGCG
AATATCTACCAGAAAAGTACTGGCGAGCGCCTGTTTAAACCGTGGGCGCTGTTTAAGCGT
CAGGATCTGAAAATTGCCGTTATTGGGCTGACAACCGATGACACAGCAAAAATTGGTAAC
CCGGAATACTTCACTGATATCGAATTTCGTAAGCCCGCCGATGAAGCGAAGCTGGTGATT
CAGGAGCTGCAACAGACAGAAAAGCCAGACATTATTATCGCGGCGACCCATATGGGGCAT
TACGATAATGGTGAGCACGGCTCTAACGCACCGGGCGATGTGGAGATGGCACGCGCGCTG
CCTGCCGGATCGCTGGCGATGATCGTCGGTGGTCACTCGCAAGATCCGGTCTGCATGGCG
GCAGAAAACAAAAAACAGGTCGATTACGTGCCGGGTACGCCATGCAAACCAGATCAACAA
AACGGCATCTGGATTGTGCAGGCGCATGAGTGGGGCAAATACGTGGGACGGGCTGATTTT
GAGTTTCGTAATGGCGAAATGAAAATGGTTAACTACCAGCTGATTCCGGTGAACCTGAAG
AAGAAAGTGACCTGGGAAGACGGGAAAAGCGAGCGCGTGCTTTACACTCCTGAAATCGCT
GAAAACCAGCAAATGATCTCGCTGTTATCACCGTTCCAGAACAAAGGCAAAGCGCAGCTG
GAAGTGAAAATAGGCGAAACCAATGGTCGTCTGGAAGGCGATCGTGACAAAGTGCGTTTT
GTACAGACCAATATGGGGCGGTTGATTCTGGCAGCCCAAATGGATCGCACTGGTGCCGAC
TTTGCGGTGATGAGCGGAGGCGGAATTCGTGATTCTATCGAAGCAGGCGATATCAGCTAT
AAAAACGTGCTGAAAGTGCAGCCATTCGGCAATGTGGTGGTGTATGCCGACATGACCGGT
AAAGAGGTGATTGATTACCTGACCGCCGTCGCGCAGATGAAGCCAGATTCAGGTGCCTAC
CCGCAATTTGCCAACGTTAGCTTTGTGGCGAAAGACGGCAAACTGAACGACCTTAAAATC
AAAGGCGAACCGGTCGATCCGGCGAAAACTTACCGTATGGCGACATTAAACTTCAATGCC
ACCGGCGGTGATGGATATCCGCGCCTTGATAACAAACCGGGCTATGTGAATACCGGCTTT
ATTGATGCCGAAGTGCTGAAAGCGTATATCCAGAAAAGCTCGCCGCTGGATGTGAGTGTT
TATGAACCGAAAGGTGAGGTGAGCTGGCAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:550
Protein Molecular Weight:62542
Protein Theoretical pI:9
Signaling Regions:
  • None
Transmembrane Regions:
  • 7-27
  • 81-101
  • 110-131
  • 137-154
  • 165-185
  • 204-224
  • 255-275
  • 288-308
  • 315-335
  • 346-366
  • 383-403
  • 406-426
Protein Sequence:
>Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
MKSVRYLIGLFAFIACYYLLPISTRLLWQPDETRYAEISREMLASGDWIVPHLLGLRYFE
KPIAGYWINSIGQWLFGANNFGVRAGVIFATLLTAALVTWFTLRLWRDKRLALLATVIYL
SLFIVYAIGTYAVLDPFIAFWLVAGMCSFWLAMQAQTWKGKSAGFLLLGITCGMGVMTKG
FLALAVPVLSVLPWVATQKRWKDLFIYGWLAVISCVLTVLPWGLAIAQREPNFWHYFFWV
EHIQRFALDDAQHRAPFWYYVPVIIAGSLPWLGLLPGALYTGWKNRKHSATVYLLSWTIM
PLLFFSVAKGKLPTYILSCFASLAMLMAHYALLAAKNNPLALRINGWINIAFGVTGIIAT
FVVSPWGPMNTPVWQTFESYKVFCAWSIFSLWAFFGWYTLTNVEKTWPFAALCPLGLALL
VGFSIPDRVMEGKHPQFFVEMTQESLQPSRYILTDSVGVAAGLAWSLQRDDIIMYRQTGE
LKYGLNYPDAKGRFVSGDEFANWLNQHRQEGIITLVLSVDRDEDINSLAIPPADAIDRQE
RLVLIQYRPK
References
External Links:
ResourceLink
Uniprot ID:P76473
Uniprot Name:ARNT_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674619
Ecogene ID:EG14093
Ecocyc:EG14093
ColiBase:b2257
Kegg Gene:b2257
EchoBASE ID:EB3846
CCDB:ARNT_ECOLI
BacMap:16130192
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
  • Daley, D. O., Rapp, M., Granseth, E., Melen, K., Drew, D., von Heijne, G. (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308:1321-1323. Pubmed: 15919996
  • 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
  • Trent, M. S., Ribeiro, A. A., Lin, S., Cotter, R. J., Raetz, C. R. (2001). "An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A: induction on polymyxin-resistant mutants and role of a novel lipid-linked donor." J Biol Chem 276:43122-43131. Pubmed: 11535604