Reviewed, UniProtKB/Swiss-Prot P08373 (MURB_ECOLI)

Names and origin

Protein names

Recommended name:
    UDP-N-acetylenolpyruvoylglucosamine reductase
    EC=1.1.1.158
Alternative name(s):
    UDP-N-acetylmuramate dehydrogenase

Gene names

Name:	murB
Synonyms:	yijB
Ordered Locus Names:	b3972, JW3940

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	342 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Cell wall formation.
Catalytic activity	UDP-N-acetylmuramate + NADP(+) = UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + NADPH.
Cofactor	FAD.
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis.
Subunit structure	Monomer.
Subcellular location	CytoplasmProbable.
Sequence similarities	Belongs to the murB family. Contains 1 FAD-binding PCMH-type domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: HAMAP
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro UDP-N-acetylmuramate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 342

342

UDP-N-acetylenolpyruvoylglucosamine reductase

PRO_0000179207

Regions

Domain

13 – 183

171

FAD-binding PCMH-type

Sites

Active site

159

1

Active site

229

1

Proton donor

Active site

325

1

Binding site

190

1

Substrate

Experimental info

Sequence conflict

35

1

Y → H in AAA24185. Ref.2

Sequence conflict

138

1

S → C in AAA24185. Ref.2

Sequence conflict

242

1

K → E in AAA24185. Ref.2

Sequence conflict

279

1

I → M in AAA24185. Ref.2

Secondary structure

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342

Helix Strand Turn

Details...

Helix

6 – 8

3

Beta strand

16 – 23

8

Helix

26 – 38

13

Beta strand

43 – 48

6

Beta strand

52 – 54

3

Beta strand

58 – 65

8

Beta strand

70 – 75

6

Beta strand

78 – 84

7

Helix

89 – 98

10

Helix

105 – 107

3

Helix

114 – 116

3

Turn

117 – 121

5

Helix

129 – 131

3

Beta strand

133 – 140

8

Helix

141 – 143

3

Beta strand

146 – 150

5

Turn

151 – 155

5

Helix

162 – 164

3

Turn

165 – 170

6

Beta strand

171 – 183

13

Helix

191 – 193

3

Turn

198 – 200

3

Helix

203 – 217

15

Turn

221 – 223

3

Beta strand

224 – 231

8

Helix

238 – 247

10

Beta strand

253 – 255

3

Beta strand

261 – 263

3

Helix

265 – 270

6

Turn

271 – 273

3

Beta strand

282 – 284

3

Beta strand

291 – 294

4

Helix

300 – 318

19

Beta strand

326 – 330

5

Helix

337 – 341

5

Sequences

	Sequence		Length	Mass (Da)
	P08373-1 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: F43CFE29251E45C6	FASTA	342	37,851
	10 20 30 40 50 60 MNHSLKPWNT FGIDHNAQHI VCAEDEQQLL NAWQYATAEG QPVLILGEGS NVLFLEDYRG 70 80 90 100 110 120 TVIINRIKGI EIHDEPDAWY LHVGAGENWH RLVKYTLQEG MPGLENLALI PGCVGSSPIQ 130 140 150 160 170 180 NIGAYGVELQ RVCAYVDSVE LATGKQVRLT AKECRFGYRD SIFKHEYQDR FAIVAVGLRL 190 200 210 220 230 240 PKEWQPVLTY GDLTRLDPTT VTPQQVFNAV CHMRTTKLPD PKVNGNAGSF FKNPVVSAET 250 260 270 280 290 300 AKALLSQFPT APNYPQADGS VKLAAGWLID QCQLKGMQIG GAAVHRQQAL VLINEDNAKS 310 320 330 340 EDVVQLAHHV RQKVGEKFNV WLEPEVRFIG ASGEVSAVET IS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the birA gene encoding the biotin operon repressor and biotin holoenzyme synthetase functions of Escherichia coli." Howard P.K., Shaw J., Otsuka A.J. Gene 35:321-331(1985) [PubMed: 3899863] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: B.
[2]	"Cloning and identification of the Escherichia coli murB DNA sequence, which encodes UDP-N-acetylenolpyruvoylglucosamine reductase." Pucci M.J., Discotto L.F., Dougherty T.J. J. Bacteriol. 174:1690-1693(1992) [PubMed: 1311302] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[3]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Gene organization and primary structure of a ribosomal RNA operon from Escherichia coli." Brosius J., Dull T.J., Sleeter D.D., Noller H.F. J. Mol. Biol. 148:107-127(1981) [PubMed: 7028991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-197.
[7]	"Overexpression, purification, and mechanistic study of UDP-N-acetylenolpyruvylglucosamine reductase." Benson T.E., Marquardt J.L., Marquardt A.C., Etzkorn F.A., Walsh C.T. Biochemistry 32:2024-2030(1993) [PubMed: 8448160] [Abstract] Cited for: CHARACTERIZATION.
[8]	"The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls." Benson T.E., Walsh C.T., Hogle J.M. Structure 4:47-54(1996) [PubMed: 8805513] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[9]	"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." Benson T.E., Walsh C.T., Hogle J.M. Biochemistry 36:806-811(1997) [PubMed: 9020778] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[10]	"Characterization of NADP+ binding to perdeuterated MurB: backbone atom NMR assignments and chemical-shift changes." 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. II J. Mol. Biol. 267:1223-1246(1997) [PubMed: 9150408] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M10123 Genomic DNA. Translation: AAA23519.1.
L14557 Genomic DNA. Translation: AAA24185.1.
U00006 Genomic DNA. Translation: AAC43074.1.
U00096 Genomic DNA. Translation: AAC76950.1.
AP009048 Genomic DNA. Translation: BAE77343.1.
V00348 Genomic DNA. No translation available.

PIR

QQECB8. A24029.

RefSeq

AP_003842.1.
NP_418403.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MBB	X-ray	2.30	A	1-342	[»]
1MBT	X-ray	3.00	A	1-342	[»]
1UXY	X-ray	1.80	A	3-342	[»]
2MBR	X-ray	1.80	A	3-342	[»]
2Q85	X-ray	2.51	A	1-342	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:10277N.

Genome annotation databases

GeneID

948470.

GenomeReviews

Gene locus b3972 in contig U00096_GR.
Gene locus JW3940 in contig AP009048_GR.

KEGG

ecj:JW3940.
eco:b3972.

Organism-specific databases

EchoBASE

EB1190.

EcoGene

EG11205. murB.

CMR

Search...

Phylogenomic databases

HOGENOM

P08373.

Enzyme and pathway databases

BioCyc

EcoCyc:UDPNACETYLMURAMATEDEHYDROG-MON.
MetaCyc:UDPNACETYLMURAMATEDEHYDROG-MON.

Family and domain databases

HAMAP

MF_00037.
[Tree]

InterPro

IPR016169. CO_DHase_flavot_FAD-bd_sub2.
IPR016167. FAD-bd_2_sub1.
IPR003170. MurB.
IPR011601. MurB_C.
IPR006094. Oxid_FAD_bind_N.
[Graphical view]

Gene3D

G3DSA:3.30.465.10. CO_DH_flavoprot_FAD-bd_sub2. 1 hit.
G3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit.
G3DSA:3.90.78.10. MurB_C. 1 hit.

PANTHER

PTHR21071. MurB. 1 hit.

Pfam

PF01565. FAD_binding_4. 1 hit.
PF02873. MurB_C. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00179. murB. 1 hit.

PROSITE

PS51387. FAD_PCMH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

P08373.

Entry information

Entry name

MURB_ECOLI

Accession

Primary (citable) accession number: P08373
Secondary accession number(s): Q2M8R3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	November 25, 2008
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)