UDP-N-acetylenolpyruvoylglucosamine reductase (P08373)

Identification
Name:UDP-N-acetylenolpyruvoylglucosamine reductase
Synonyms:
  • UDP-N-acetylmuramate dehydrogenase
Gene Name:murB
Enzyme Class:
Biological Properties
General Function:Involved in flavin adenine dinucleotide binding
Specific Function:Cell wall formation
Cellular Location:Cytoplasm (Probable)
SMPDB Pathways:
KEGG Pathways:
  • Amino sugar and nucleotide sugar metabolism ec00520
  • Peptidoglycan biosynthesis ec00550
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Hydrogen ion + 1.0NADPH + 1.0UDP-N-Acetyl-3-(1-carboxyvinyl)-D-glucosamine ↔ 1.0NADP + 1.0UDP-N-Acetylmuraminate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0UDP-N-Acetylmuraminate + 1.0NAD ↔ 1.0UDP-N-Acetyl-3-(1-carboxyvinyl)-D-glucosamine + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0UDP-N-Acetylmuraminate + 1.0NADP ↔ 1.0UDP-N-Acetyl-3-(1-carboxyvinyl)-D-glucosamine + 1.0NADPH + 1.0Hydrogen ion
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0NADPH+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0UDP-N-acetyl-α-D-glucosamine-enolpyruvate + 1.0NADPH + 1.0Hydrogen ion + 1.0NADPH → 1.0NADP + 1.0UDP-N-acetyl-α-D-muramate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Hydrogen ion + 1.0NADPH + 1.0UDP-N-Acetyl-3-(1-carboxyvinyl)-D-glucosamine ↔ 1.0NADP + 1.0UDP-N-Acetylmuraminate
ReactionCard
1.0Thumb+1.0Thumb ← 1.0Thumb+1.0Thumb+1.0Thumb
1.0NADP + 1.0UDP-N-Acetylmuraminate ← 1.0Hydrogen ion + 1.0NADPH + 1.0UDP-N-Acetyl-3-(1-carboxyvinyl)-D-glucosamine
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0UDP-N-Acetylmuraminate + 1.0NADP → 1.0UDP-N-Acetyl-3-(1-carboxyvinyl)-D-glucosamine + 1.0NADPH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB21225Hydrogen ionMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
ECMDB04167UDP-N-Acetyl-3-(1-carboxyvinyl)-D-glucosamineMetaboCard
ECMDB24237UDP-N-acetyl-α-D-glucosamine-enolpyruvateMetaboCard
ECMDB24238UDP-N-acetyl-α-D-muramateMetaboCard
ECMDB03266UDP-N-AcetylmuraminateMetaboCard
GO Classification:
Function
adenyl nucleotide binding
binding
catalytic activity
FAD or FADH2 binding
nucleoside binding
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
purine nucleoside binding
UDP-N-acetylmuramate dehydrogenase activity
Process
aminoglycan metabolic process
carbohydrate metabolic process
glycosaminoglycan metabolic process
metabolic process
oxidation reduction
peptidoglycan biosynthetic process
peptidoglycan metabolic process
polysaccharide metabolic process
primary metabolic process
Gene Properties
Blattner:b3972
Gene OrientationClockwise
Centisome Percentage:89.88
Left Sequence End4170080
Right Sequence End4171108
Gene Sequence:
>1029 bp
ATGCGCGTACTGCTATTTTTACTTCTTTCCCTTTTCATGTTGCCGGCATTTTCGGCTGAT
AACCTGTTGCGCTGGCATGATGCGCAGCATTTCACGGTGCAAGCCTCTACGCCGCTTAAA
GCCAAACGCGCATGGAAACTGTGCGCGCTTTATCCCAGCCTGAAAGATTCATATTGGTTA
TCGTTGAACTATGGTATGCAGGAGGCTGCTCGCCGCTACGGTGTGGATTTAAAAGTGCTG
GAGGCAGGCGGCTACAGCCAGTTGGCTACCCAGCAAGCACAAATCGACCAGTGTAAACAG
TGGGGCGCAGAGGCCATTTTGCTCGGTAGTAGCACGACCTCATTTCCCGACCTGCAAAAG
CAGGTAGCAAGTCTGCCGGTGATCGAACTGGTAAATGCTATTGATGCTCCCCAGGTGAAA
AGCCGCGTTGGTGTGCCCTGGTTTCAGATGGGCTATCAACCGGGGCGATATCTGGTGCAA
TGGGCGCACGGTAAACCACTGAATGTGCTGTTGATGCCCGGACCCGATAACGCCGGGGGC
AGTAAGGAGATGGTCGAGGGTTTTCGCGCAGCCATTGCCGGAAGCCCGGTGCGTATTGTT
GATATTGCGCTTGGTGATAACGATATTGAAATCCAGCGTAACCTGTTGCAGGAGATGCTG
GAACGCCATCCAGAAATCGACGTCGTTGCCGGAACGGCCATTGCGGCAGAGGCGGCAATG
GGGGAAGGGCGTAACCTGAAAACGCCGCTTACCGTGGTGTCGTTTTATCTTTCACATCAG
GTGTATCGCGGGCTGAAGCGGGGAAGAGTGATTATGGCTGCCAGCGATCAAATGGTCTGG
CAGGGGGAACTGGCGGTTGAGCAGGCCATCAGGCAATTACAGGGGCAATCGGTTTCTGAT
AATGTCAGCCCACCGATTTTAGTTCTGACGCCGAAAAATGCCGACCGTGAACATATTCGC
CGCTCGCTGTCACCAGGGGGATTTCGTCCGGTCTATTTTTATCAGCACACATCAGCGGCT
AAGAAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:342
Protein Molecular Weight:37851
Protein Theoretical pI:6
PDB File:1MBT
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>UDP-N-acetylenolpyruvoylglucosamine reductase
MNHSLKPWNTFGIDHNAQHIVCAEDEQQLLNAWQYATAEGQPVLILGEGSNVLFLEDYRG
TVIINRIKGIEIHDEPDAWYLHVGAGENWHRLVKYTLQEGMPGLENLALIPGCVGSSPIQ
NIGAYGVELQRVCAYVDSVELATGKQVRLTAKECRFGYRDSIFKHEYQDRFAIVAVGLRL
PKEWQPVLTYGDLTRLDPTTVTPQQVFNAVCHMRTTKLPDPKVNGNAGSFFKNPVVSAET
AKALLSQFPTAPNYPQADGSVKLAAGWLIDQCQLKGMQIGGAAVHRQQALVLINEDNAKS
EDVVQLAHHVRQKVGEKFNVWLEPEVRFIGASGEVSAVETIS
References
External Links:
ResourceLink
Uniprot ID:P08373
Uniprot Name:MURB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062711
PDB ID:1MBT
Ecogene ID:EG11205
Ecocyc:EG11205
ColiBase:b3972
Kegg Gene:b3972
EchoBASE ID:EB1190
CCDB:MURB_ECOLI
BacMap:16131806
General Reference:
  • Benson, T. E., Marquardt, J. L., Marquardt, A. C., Etzkorn, F. A., Walsh, C. T. (1993). "Overexpression, purification, and mechanistic study of UDP-N-acetylenolpyruvylglucosamine reductase." Biochemistry 32:2024-2030. Pubmed: 8448160
  • Benson, T. E., Walsh, C. T., Hogle, J. M. (1996). "The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls." Structure 4:47-54. Pubmed: 8805513
  • Benson, T. E., Walsh, C. T., Hogle, J. M. (1997). "X-ray crystal structures of the S229A mutant and wild-type MurB in the presence of the substrate enolpyruvyl-UDP-N-acetylglucosamine at 1.8-A resolution." Biochemistry 36:806-811. Pubmed: 9020778
  • Blattner, F. R., Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L. (1993). "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Nucleic Acids Res 21:5408-5417. Pubmed: 8265357
  • 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
  • Brosius, J., Dull, T. J., Sleeter, D. D., Noller, H. F. (1981). "Gene organization and primary structure of a ribosomal RNA operon from Escherichia coli." J Mol Biol 148:107-127. Pubmed: 7028991
  • Constantine, K. L., Mueller, L., Goldfarb, V., Wittekind, M., Metzler, W. J., Yanchunas, J. Jr, Robertson, J. G., Malley, M. F., Friedrichs, M. S., Farmer, B. T. 2nd (1997). "Characterization of NADP+ binding to perdeuterated MurB: backbone atom NMR assignments and chemical-shift changes." J Mol Biol 267:1223-1246. Pubmed: 9150408
  • 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
  • Howard, P. K., Shaw, J., Otsuka, A. J. (1985). "Nucleotide sequence of the birA gene encoding the biotin operon repressor and biotin holoenzyme synthetase functions of Escherichia coli." Gene 35:321-331. Pubmed: 3899863
  • Pucci, M. J., Discotto, L. F., Dougherty, T. J. (1992). "Cloning and identification of the Escherichia coli murB DNA sequence, which encodes UDP-N-acetylenolpyruvoylglucosamine reductase." J Bacteriol 174:1690-1693. Pubmed: 1311302