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O51544 (MURB_BORBU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
UDP-N-acetylenolpyruvoylglucosamine reductase
EC=1.1.1.158
Alternative name(s):
UDP-N-acetylmuramate dehydrogenase
Gene names
Name:murB
Ordered Locus Names:BB_0598
OrganismBorrelia burgdorferi (Lyme disease spirochete)
Taxonomic identifier139 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 302302UDP-N-acetylenolpyruvoylglucosamine reductase HAMAP MF_00037
PRO_0000179181

Regions

Domain28 – 194167FAD-binding PCMH-type

Sites

Active site2231Proton donor By similarity
Active site2951 By similarity

Sequences

Sequence LengthMass (Da)Tools
O51544 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: D0E455CD21E815A1

FASTA30234,182
        10         20         30         40         50         60 
MPKSLNNFLK KINIKPQTKN LANYTTYKIG NISKLFLTPK NIKEAENIFK AAIEEKIKLF 

        70         80         90        100        110        120 
ILGGGSNILV NDEREIDFPI IYTGYLNKIE IHENKIVGEC GADFESLCKI ALDNSLSGLE 

       130        140        150        160        170        180 
FIYGLPGTLG GAVWMNARCF GNEISEILKK ITFIDDKGKT ICKEFKKEDF KYKISPFQNK 

       190        200        210        220        230        240 
NFFILKIELN LKKDNKKIIE EKMNKNKQAR INRGHYLFPS GGSTFKNNKA FLKPSGQIIE 

       250        260        270        280        290        300 
ECKLKGLSIG GATVSKYHGN FIININNATS KDIKSLIEKV KAEVYLKTGL LLEEEVLYIG 


FK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000783 Genomic DNA. Translation: AAC66953.1.
PIRE70174.
RefSeqNP_212732.1. NC_001318.1.

3D structure databases

ProteinModelPortalO51544.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBORT00000008851; EBBORP00000008181; EBBORG00000008850.
GeneID1195445.
GenomeReviewsGene locus BB_0598 in contig AE000783_GR.
KEGGbbu:BB0598.
NMPDRfig|224326.1.peg.982.
PATRIC20557829. VBIBorBur75917_0989.
TIGRBB_0598.

Phylogenomic databases

GeneTreeEBGT00050000007374.
HOGENOMHBG686573.
OMASKKHAGF.
PhylomeDBO51544.
ProtClustDBPRK14650.

Enzyme and pathway databases

BioCycBBUR224326:BB_0598-MONOMER.

Family and domain databases

HAMAPMF_00037. MurB. Divergent sequence.
[Tree]
InterProIPR016169. 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]
Gene3DG3DSA: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.
KOK00075.
PANTHERPTHR21071. MurB. 1 hit.
PfamPF01565. FAD_binding_4. 1 hit.
PF02873. MurB_C. 1 hit.
[Graphical view]
SUPFAMSSF56176. FAD-binding_2. 1 hit.
SSF56194. MurB_C. 1 hit.
TIGRFAMsTIGR00179. MurB. 1 hit.
PROSITEPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMURB_BORBU
AccessionPrimary (citable) accession number: O51544
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: January 25, 2012
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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