Q7WGH4 (MURB_BORBR) 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
Ordered Locus Names:	BB3945

Organism

Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]

Taxonomic identifier

257310 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	353 AA.
Sequence status	Complete.
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 By similarity. HAMAP MF_00037
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00037
Subcellular location	Cytoplasm By similarity HAMAP 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	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 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 – 353	353	UDP-N-acetylenolpyruvoylglucosamine reductase HAMAP MF_00037		PRO_0000179180
Regions
	Domain	31 – 201	171	FAD-binding PCMH-type
Sites
	Active site	177	1	By similarity
	Active site	250	1	Proton donor By similarity
	Active site	346	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7WGH4 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: FCC2DC94254236C7	FASTA	353	37,591
	10 20 30 40 50 60 MSMSTVPARI EPVAPLAPQA QDLRCFNTLG LASHAPAFVA LTEPSQLPAL SALAPRFRQL 70 80 90 100 110 120 VVLGGGSNVV LPASIDGLVA QVRLPGVRLV GQCADAWVVE AAAGENWHGF VTVCVDNGWD 130 140 150 160 170 180 GLENLALIPG TVGAAPVQNI GAYGVELADR FHSLTAWDVK GGRWVEMGAA ECRFAYRDSF 190 200 210 220 230 240 FKHQEPGAWV IGSVRFALPR PWQPVLDYPD LQRHAALDGA APTARAVYDA VCAIRRAKLP 250 260 270 280 290 300 DPAVVGNAGS FFKNPLVDAG TRQALLGRFP GLVSYPQPDG RYKLAAGWLI DQCGWKGRQL 310 320 330 340 350 GAAGVHDRQA LVLVNRGGAQ AHDIMALAAA IQGDVERRYG VRLEPEPVVV PAR

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-588 / NCTC 13252 / RB50.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640449 Genomic DNA. Translation: CAE34308.1.
RefSeq	NP_890479.1. NC_002927.3.
3D structure databases
ProteinModelPortal	Q7WGH4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2660802.
GenomeReviews	Gene locus BB3945 in contig BX470250_GR.
KEGG	bbr:BB3945.
NMPDR	fig|257310.1.peg.3926.
PATRIC	21141295. VBIBorBro124907_4005.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG686573.
OMA	LAYEITS.
PhylomeDB	Q7WGH4.
ProtClustDB	PRK00046.
Enzyme and pathway databases
BioCyc	BBRO257310:BB3945-MONOMER.
Family and domain databases
HAMAP	MF_00037. MurB. [Tree]
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]
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.
KO	K00075.
PANTHER	PTHR21071. MurB. 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...

Entry information

Entry name

MURB_BORBR

Accession

Primary (citable) accession number: Q7WGH4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program