EzCatDB: T00003
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DB codeT00003
CATH domainDomain 13.90.78.10 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 1Catalytic domain
Domain 23.30.43.10 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2
Domain 33.30.465.10 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3Catalytic domain
E.C.1.1.1.158
CSA1mbb

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

Enzyme Name
UniProtKBKEGG

P08373
Protein nameUDP-N-acetylenolpyruvoylglucosamine reductaseUDP-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
SynonymsEC 1.1.1.158
UDP-N-acetylmuramate dehydrogenase
RefSeqNP_418403.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491484.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PfamPF01565 (FAD_binding_4)
PF02873 (MurB_C)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00530Aminosugars metabolism

UniProtKB:Accession NumberP08373
Entry nameMURB_ECOLI
ActivityUDP-N-acetylmuramate + NADP(+) = UDP-N-acetyl- 3-O-(1-carboxyvinyl)-D-glucosamine + NADPH.
SubunitMonomer.
Subcellular locationCytoplasm (Probable).
CofactorFAD.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00016C01050C00006C04631C00005
CompoundFADUDP-N-acetylmuramateNADP+UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamineNADPH
Typeamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotideamide group,carbohydrate,carboxyl group,nucleotideamide group,amine group,nucleotideamide group,carbohydrate,carboxyl group,nucleotideamide group,amine group,nucleotide
ChEBI16238
70765
18009
68507
16474
PubChem643975
11006912
5886
172502
5884
             
1mbbA01UnboundUnboundUnboundUnboundUnbound
1mbrA01UnboundUnboundUnboundUnboundUnbound
1mbtA01UnboundUnboundUnboundUnboundUnbound
1uxyA01UnboundUnboundUnboundUnboundUnbound
2mbrA01UnboundUnboundUnboundUnboundUnbound
1mbbA02UnboundUnboundUnboundUnboundUnbound
1mbrA02UnboundUnboundUnboundUnboundUnbound
1mbtA02UnboundUnboundUnboundUnboundUnbound
1uxyA02UnboundUnboundUnboundUnboundUnbound
2mbrA02UnboundUnboundUnboundUnboundUnbound
1mbbA03Bound:FADAnalogue:EEBUnboundUnboundUnbound
1mbrA03Bound:FADUnboundUnboundBound:EPUUnbound
1mbtA03Bound:FADUnboundUnboundUnboundUnbound
1uxyA03Bound:FADUnboundUnboundBound:EPUUnbound
2mbrA03Bound:FADUnboundUnboundBound:EPUUnbound

Active-site residues
resource
PDB;1uxy
pdbCatalytic residuescomment
          
1mbbA01SER 229;GLU 325
 
1mbrA01SER 229;GLU 325
 
1mbtA01SER 229;GLU 325
 
1uxyA01       ;GLU 325
mutant S299A
2mbrA01SER 229;GLU 325
 
1mbbA02 
 
1mbrA02 
 
1mbtA02 
 
1uxyA02 
 
2mbrA02 
 
1mbbA03ARG 159
 
1mbrA03ARG 159
 
1mbtA03ARG 159
 
1uxyA03ARG 159
 
2mbrA03ARG 159
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]Scheme II, p.2029-20303
[3]Fig.6, p.650-6512
[4]Fig.2, Fig.10, Fig.11, p.1350
[6]Fig.1
[8]Fig.2, Fig3, Fig.10, p.804

references
[1]
CommentsCHARACTERIZATION.
Medline ID93192262
PubMed ID8448160
JournalBiochemistry
Year1993
Volume32
Pages2024-30
AuthorsBenson TE, Marquardt JL, Marquardt AC, Etzkorn FA, Walsh CT
TitleOverexpression, purification, and mechanistic study of UDP-N-acetylenolpyruvylglucosamine reductase.
Related UniProtKBP08373
[2]
PubMed ID7920261
JournalProtein Sci
Year1994
Volume3
Pages1125-7
AuthorsBenson TE, Walsh CT, Hogle JM
TitleCrystallization and preliminary X-ray crystallographic studies of UDP-N-acetylenolpyruvylglucosamine reductase.
[3]
PubMed ID7552726
JournalNat Struct Biol
Year1995
Volume2
Pages644-53
AuthorsBenson TE, Filman DJ, Walsh CT, Hogle JM
TitleAn enzyme-substrate complex involved in bacterial cell wall biosynthesis.
[4]
CommentsX-ray crystallography
PubMed ID8634262
JournalBiochemistry
Year1996
Volume35
Pages1342-51
AuthorsLees WJ, Benson TE, Hogle JM, Walsh CT
Title(E)-enolbutyryl-UDP-N-acetylglucosamine as a mechanistic probe of UDP-N-acetylenolpyruvylglucosamine reductase (MurB).
Related PDB1mbb
[5]
PubMed ID8946851
JournalNat Struct Biol
Year1996
Volume3
Pages995-7
AuthorsFarmer BT 2nd, Constantine KL, Goldfarb V, Friedrichs MS, Wittekind M, Yanchunas J Jr, Robertson JG, Mueller L
TitleLocalizing the NADP+ binding site on the MurB enzyme by NMR.
[6]
CommentsX-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID96419135
PubMed ID8805513
JournalStructure
Year1996
Volume4
Pages47-54
AuthorsBenson TE, Walsh CT, Hogle JM
TitleThe structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls.
Related PDB1mbt
Related UniProtKBP08373
[7]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Medline ID97172910
PubMed ID9020778
JournalBiochemistry
Year1997
Volume36
Pages806-11
AuthorsBenson TE, Walsh CT, Hogle JM
TitleX-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 PDB1mbr,1uxy,2mbr
Related UniProtKBP08373
[8]
PubMed ID9020777
JournalBiochemistry
Year1997
Volume36
Pages796-805
AuthorsBenson TE, Walsh CT, Massey V
TitleKinetic characterization of wild-type and S229A mutant MurB: evidence for the role of Ser 229 as a general acid.
[9]
CommentsSTRUCTURE BY NMR.
Medline ID97294652
PubMed ID9150408
JournalJ Mol Biol
Year1997
Volume267
Pages1223-46
AuthorsConstantine KL, Mueller L, Goldfarb V, Wittekind M, Metzler WJ, Yanchunas J Jr, Robertson JG, Malley MF, Friedrichs MS, Farmer BT 2nd
TitleCharacterization of NADP+ binding to perdeuterated MurB: backbone atom NMR assignments and chemical-shift changes.
Related UniProtKBP08373


createdupdated
2004-03-252009-02-26


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