Q6HBI9 (MURB2_BACHK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UDP-N-acetylenolpyruvoylglucosamine reductase 2
EC=1.1.1.158

Alternative name(s):
UDP-N-acetylmuramate dehydrogenase 2

Gene names

Name:	murB2
Ordered Locus Names:	BT9727_4778

Organism

Bacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP]

Taxonomic identifier

281309 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	305 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 – 305	305	UDP-N-acetylenolpyruvoylglucosamine reductase 2 HAMAP MF_00037		PRO_0000224661
Regions
	Domain	33 – 197	165	FAD-binding PCMH-type
Sites
	Active site	176	1	By similarity
	Active site	226	1	Proton donor By similarity
	Active site	296	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6HBI9 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 5A085B50166644FA	FASTA	305	33,560
	10 20 30 40 50 60 MNMQEVYEYL STVLPEGHVK QDEMLKNHTH IKVGGKADVF VAPTNYDEIQ EVIKYANKYN 70 80 90 100 110 120 IPVTFLGNGS NVIIKDGGIR GITVSLIHIT GVTVTGTTIV AQCGAAIIDV SRIALDHNLT 130 140 150 160 170 180 GLEFACGIPG SVGGALYMNA GAYGGEISFV LTEAVVMTGD GELRTLTKEA FEFGYRKSVF 190 200 210 220 230 240 ANNHYIILEA RFELEEGLYE EIKAKMDDLT FKRESKQPLE YPSCGSVFKR PPNNFAGKLI 250 260 270 280 290 300 QESGLQGKRI GGVEVSLKHA GFMVNVDNGT AQDYIDLIHF VQKTVEEKFG VKLEREVRII GEDKE

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 97-27.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017355 Genomic DNA. Translation: AAT63301.1.
RefSeq	YP_039087.1. NC_005957.1.
3D structure databases
ProteinModelPortal	Q6HBI9.
SMR	Q6HBI9. Positions 4-302.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000072059; EBBACP00000070145; EBBACG00000072050.
GeneID	2853612.
GenomeReviews	Gene locus BT9727_4778 in contig AE017355_GR.
KEGG	btk:BT9727_4778.
NMPDR	fig|281309.1.peg.4727.
PATRIC	18990772. VBIBacThu119411_5084.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000001391.
HOGENOM	HBG686573.
OMA	SKKHAGF.
ProtClustDB	PRK12436.
Enzyme and pathway databases
BioCyc	BTHU281309:BT9727_4778-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

MURB2_BACHK

Accession

Primary (citable) accession number: Q6HBI9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	July 19, 2004
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program