DB code: T00003

CATH domain 3.90.78.10 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 1 Catalytic domain
3.30.43.10 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2
3.30.465.10 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3 Catalytic domain
E.C. 1.1.1.158
CSA 1mbb
M-CSA 1mbb
MACiE

CATH domain Related DB codes (homologues)
3.30.43.10 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2 M00001 M00004 M00039 M00179
3.30.465.10 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3 M00039

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P08373 UDP-N-acetylenolpyruvoylglucosamine reductase
EC 1.1.1.158
UDP-N-acetylmuramate dehydrogenase
NP_418403.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491484.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF01565 (FAD_binding_4)
PF02873 (MurB_C)
[Graphical View]

KEGG enzyme name
UDP-N-acetylmuramate dehydrogenase
MurB reductase
UDP-N-acetylenolpyruvoylglucosamine reductase
UDP-N-acetylglucosamine-enoylpyruvate reductase
UDP-GlcNAc-enoylpyruvate reductase
uridine diphosphoacetylpyruvoylglucosamine reductase
uridine diphospho-N-acetylglucosamine-enolpyruvate reductase
uridine-5'-diphospho-N-acetyl-2-amino-2-deoxy-3-O-lactylglucose:NADP-oxidoreductase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P08373 MURB_ECOLI UDP-N-acetylmuramate + NADP(+) = UDP-N-acetyl- 3-O-(1-carboxyvinyl)-D-glucosamine + NADPH. Monomer. Cytoplasm (Probable). FAD.

KEGG Pathways
Map code Pathways E.C.
MAP00530 Aminosugars metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00016 C01050 C00006 C04631 C00005
E.C.
Compound FAD UDP-N-acetylmuramate NADP+ UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine NADPH
Type amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide amide group,carbohydrate,carboxyl group,nucleotide amide group,amine group,nucleotide amide group,carbohydrate,carboxyl group,nucleotide amide group,amine group,nucleotide
ChEBI 16238
 16238
 		70765
 70765
 		18009
 18009
 		68507
 68507
 		16474
 16474
PubChem 643975
 643975
 		11006912
 11006912
 		5886
 5886
 		172502
 172502
 		5884
 5884
1mbbA01 Unbound Unbound Unbound Unbound Unbound
1mbrA01 Unbound Unbound Unbound Unbound Unbound
1mbtA01 Unbound Unbound Unbound Unbound Unbound
1uxyA01 Unbound Unbound Unbound Unbound Unbound
2mbrA01 Unbound Unbound Unbound Unbound Unbound
1mbbA02 Unbound Unbound Unbound Unbound Unbound
1mbrA02 Unbound Unbound Unbound Unbound Unbound
1mbtA02 Unbound Unbound Unbound Unbound Unbound
1uxyA02 Unbound Unbound Unbound Unbound Unbound
2mbrA02 Unbound Unbound Unbound Unbound Unbound
1mbbA03 Bound:FAD Analogue:EEB Unbound Unbound Unbound
1mbrA03 Bound:FAD Unbound Unbound Bound:EPU Unbound
1mbtA03 Bound:FAD Unbound Unbound Unbound Unbound
1uxyA03 Bound:FAD Unbound Unbound Bound:EPU Unbound
2mbrA03 Bound:FAD Unbound Unbound Bound:EPU Unbound

Reference for Active-site residues
resource references E.C.
PDB;1uxy

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1mbbA01 SER 229;GLU 325
1mbrA01 SER 229;GLU 325
1mbtA01 SER 229;GLU 325
1uxyA01 ;GLU 325 mutant S299A
2mbrA01 SER 229;GLU 325
1mbbA02
1mbrA02
1mbtA02
1uxyA02
2mbrA02
1mbbA03 ARG 159
1mbrA03 ARG 159
1mbtA03 ARG 159
1uxyA03 ARG 159
2mbrA03 ARG 159

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
Scheme II, p.2029-2030 3
[3]
Fig.6, p.650-651 2
[4]
Fig.2, Fig.10, Fig.11, p.1350
[6]
Fig.1
[8]
Fig.2, Fig3, Fig.10, p.804

References
[1]
Resource
Comments CHARACTERIZATION.
Medline ID 93192262
PubMed ID 8448160
Journal Biochemistry
Year 1993
Volume 32
Pages 2024-30
Authors Benson TE, Marquardt JL, Marquardt AC, Etzkorn FA, Walsh CT
Title Overexpression, purification, and mechanistic study of UDP-N-acetylenolpyruvylglucosamine reductase.
Related PDB
Related UniProtKB P08373
[2]
Resource
Comments
Medline ID
PubMed ID 7920261
Journal Protein Sci
Year 1994
Volume 3
Pages 1125-7
Authors Benson TE, Walsh CT, Hogle JM
Title Crystallization and preliminary X-ray crystallographic studies of UDP-N-acetylenolpyruvylglucosamine reductase.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 7552726
Journal Nat Struct Biol
Year 1995
Volume 2
Pages 644-53
Authors Benson TE, Filman DJ, Walsh CT, Hogle JM
Title An enzyme-substrate complex involved in bacterial cell wall biosynthesis.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8634262
Journal Biochemistry
Year 1996
Volume 35
Pages 1342-51
Authors Lees WJ, Benson TE, Hogle JM, Walsh CT
Title (E)-enolbutyryl-UDP-N-acetylglucosamine as a mechanistic probe of UDP-N-acetylenolpyruvylglucosamine reductase (MurB).
Related PDB 1mbb
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 8946851
Journal Nat Struct Biol
Year 1996
Volume 3
Pages 995-7
Authors Farmer BT 2nd, Constantine KL, Goldfarb V, Friedrichs MS, Wittekind M, Yanchunas J Jr, Robertson JG, Mueller L
Title Localizing the NADP+ binding site on the MurB enzyme by NMR.
Related PDB
Related UniProtKB
[6]
Resource
Comments X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID 96419135
PubMed ID 8805513
Journal Structure
Year 1996
Volume 4
Pages 47-54
Authors Benson TE, Walsh CT, Hogle JM
Title The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls.
Related PDB 1mbt
Related UniProtKB P08373
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Medline ID 97172910
PubMed ID 9020778
Journal Biochemistry
Year 1997
Volume 36
Pages 806-11
Authors Benson TE, Walsh CT, Hogle JM
Title 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.
Related PDB 1mbr 1uxy 2mbr
Related UniProtKB P08373
[8]
Resource
Comments
Medline ID
PubMed ID 9020777
Journal Biochemistry
Year 1997
Volume 36
Pages 796-805
Authors Benson TE, Walsh CT, Massey V
Title Kinetic characterization of wild-type and S229A mutant MurB: evidence for the role of Ser 229 as a general acid.
Related PDB
Related UniProtKB
[9]
Resource
Comments STRUCTURE BY NMR.
Medline ID 97294652
PubMed ID 9150408
Journal J Mol Biol
Year 1997
Volume 267
Pages 1223-46
Authors Constantine KL, Mueller L, Goldfarb V, Wittekind M, Metzler WJ, Yanchunas J Jr, Robertson JG, Malley MF, Friedrichs MS, Farmer BT 2nd
Title Characterization of NADP+ binding to perdeuterated MurB: backbone atom NMR assignments and chemical-shift changes.
Related PDB
Related UniProtKB P08373

Comments

Created Updated
2004-03-25 2009-02-26