P08373 (MURB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UDP-N-acetylenolpyruvoylglucosamine reductase
EC=1.3.1.98

Alternative name(s):
UDP-N-acetylmuramate dehydrogenase

Gene names

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

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	342 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cell wall formation. HAMAP-Rule MF_00037
Catalytic activity	UDP-N-acetyl-alpha-D-muramate + NADP+ = UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH. HAMAP-Rule MF_00037
Cofactor	FAD.
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00037
Subunit structure	Monomer.
Subcellular location	Cytoplasm Probable HAMAP-Rule MF_00037.
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 Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cell wall organization Inferred from mutant phenotype PubMed 16436710. Source: EcoliWiki peptidoglycan biosynthetic process Inferred from mutant phenotype PubMed 16436710. Source: EcoliWiki regulation of cell shape Inferred from mutant phenotype PubMed 16436710. Source: EcoliWiki
Cellular_component	cytoplasm Inferred from direct assay PubMed 16436710. Source: EcoliWiki
Molecular_function	UDP-N-acetylmuramate dehydrogenase activity Inferred from direct assay PubMed 7727397. Source: EcoCyc flavin adenine dinucleotide binding Inferred from direct assay Ref.7. Source: EcoliWiki
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 HAMAP-Rule MF_00037

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 – 25

10

Helix

26 – 38

13

Beta strand

43 – 48

6

Beta strand

52 – 54

3

Beta strand

58 – 65

8

Beta strand

70 – 74

5

Beta strand

76 – 84

9

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

Turn

141 – 143

3

Beta strand

146 – 150

5

Helix

152 – 154

3

Helix

162 – 164

3

Turn

165 – 170

6

Beta strand

171 – 183

13

Helix

191 – 195

5

Turn

198 – 200

3

Helix

203 – 217

15

Turn

221 – 223

3

Beta strand

226 – 231

6

Helix

238 – 247

10

Beta strand

253 – 255

3

Beta strand

261 – 263

3

Helix

265 – 271

7

Beta strand

282 – 284

3

Beta strand

286 – 288

3

Beta strand

291 – 294

4

Helix

300 – 318

19

Beta strand

326 – 330

5

Beta strand

333 – 335

3

Helix

337 – 341

5

Sequences

	Sequence		Length	Mass (Da)
	P08373 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

NP_418403.1. NC_000913.2.
YP_491484.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P08373.

SMR

P08373. Positions 3-342.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10277N.

IntAct

P08373. 10 interactions.

MINT

MINT-1275566.

STRING

511145.b3972.

Proteomic databases

PaxDb

P08373.

PRIDE

P08373.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76950; AAC76950; b3972.
BAE77343; BAE77343; BAE77343.

GeneID

12933988.
948470.

KEGG

ecj:Y75_p3220.
eco:b3972.

PATRIC

32123465. VBIEscCol129921_4089.

Organism-specific databases

EchoBASE

EB1190.

EcoGene

EG11205. murB.

Phylogenomic databases

eggNOG

COG0812.

HOGENOM

HOG000284356.

KO

K00075.

OMA

RDSVFKH.

ProtClustDB

PRK00046.

Enzyme and pathway databases

BioCyc

EcoCyc:UDPNACETYLMURAMATEDEHYDROG-MONOMER.
ECOL316407:JW3940-MONOMER.
MetaCyc:UDPNACETYLMURAMATEDEHYDROG-MONOMER.

SABIO-RK

P08373.

UniPathway

UPA00219.

Gene expression databases

Genevestigator

P08373.

Family and domain databases

Gene3D

3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.78.10. 1 hit.

HAMAP

MF_00037. MurB.

InterPro

IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR003170. MurB.
IPR011601. MurB_C.
IPR006094. Oxid_FAD_bind_N.
[Graphical view]

PANTHER

PTHR21071. PTHR21071. 1 hit.

Pfam

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

SUPFAM

SSF56176. FAD-binding_2. 1 hit.
SSF56194. MurB_C. 1 hit.

TIGRFAMs

TIGR00179. murB. 1 hit.

PROSITE

PS51387. FAD_PCMH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P08373.

ChEMBL

CHEMBL5526.

EvolutionaryTrace

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:	May 1, 2013
This is version 143 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program