Q45305 (MURB_BACLI) Reviewed, UniProtKB/Swiss-Prot

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

Organism

Bacillus licheniformis

Taxonomic identifier

1402 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	184 AA.
Sequence status	Fragment.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Cell wall formation By similarity. HAMAP MF_00037
Catalytic activity	UDP-N-acetylmuramate + NADP+ = UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + NADPH. HAMAP MF_00037
Cofactor	FAD.
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00037
Subcellular location	Cytoplasm By similarity HAMAP MF_00037.
Sequence similarities	Belongs to the MurB family.

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
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	UDP-N-acetylmuramate dehydrogenase activity Inferred from electronic annotation. Source: EC flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 184	›184	UDP-N-acetylenolpyruvoylglucosamine reductase HAMAP MF_00037		PRO_0000179177
Sites
	Active site	55	1	By similarity
	Active site	106	1	Proton donor By similarity
	Active site	176	1	By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q45305 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 4114D8B29AE21EFD	FASTA	184	20,166
	10 20 30 40 50 60 LEFAAGIPGS VGGAVYMNAG AHGSDISRVL VKALILFEDG TIDWLTNEEM AFSYRTSILQ 70 80 90 100 110 120 NERPGICLEA VLQLEQKERD EIVAQMQKNK DYRKETQPVS NPCAGSIFRN PLPEHAGRLV 130 140 150 160 170 180 DEAGLKGHQI GGAKVSEMHG NFIVNAGGAT AQDVLDLIAF IQKTIKEKYD IDMHTEVEII GEKR

References

[1]	"Conservation of the 168 divIB gene in Bacillus subtilis W23 and B. licheniformis, and evidence for homology to ftsQ of Escherichia coli." Harry E.J., Partridge S.R., Weiss A.S., Wake R.G. Gene 147:85-89(1994) [PubMed: 8088553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 5A2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U01958 Genomic DNA. Translation: AAA57244.1.
PIR	I40220.
3D structure databases
ProteinModelPortal	Q45305.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
HAMAP	MF_00037. MurB. [Tree]
InterPro	IPR016169. CO_DH_flavot_FAD-bd_sub2. IPR016166. FAD-bd_2. IPR003170. MurB. IPR011601. MurB_C. [Graphical view]
Gene3D	G3DSA:3.30.465.10. CO_DH_flavoprot_FAD-bd_sub2. 1 hit. G3DSA:3.90.78.10. MurB_C. 1 hit.
PANTHER	PTHR21071. MurB. 1 hit.
Pfam	PF02873. MurB_C. 1 hit. [Graphical view]
SUPFAM	SSF56176. FAD-binding_2. 1 hit. SSF56194. MurB_C. 1 hit.
TIGRFAMs	TIGR00179. MurB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURB_BACLI

Accession

Primary (citable) accession number: Q45305

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	October 19, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program