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P61431 (MURB_STAAU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismStaphylococcus aureus
Taxonomic identifier1280 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length307 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell wall formation. 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.

Contains 1 FAD-binding PCMH-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 307307UDP-N-acetylenolpyruvoylglucosamine reductase HAMAP MF_00037
PRO_0000179261

Regions

Domain33 – 197165FAD-binding PCMH-type

Sites

Active site1761
Active site2261Proton donor
Active site2961

Secondary structure

1 ................................................... 307
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61431 [UniParc].

Last modified May 24, 2004. Version 1.
Checksum: 8F5C3E89F7EAE0A0

FASTA30733,797
        10         20         30         40         50         60 
MINKDIYQAL QQLIPNEKIK VDEPLKRYTY TKTGGNADFY ITPTKNEEVQ AVVKYAYQNE 

        70         80         90        100        110        120 
IPVTYLGNGS NIIIREGGIR GIVISLLSLD HIEVSDDAII AGSGAAIIDV SRVARDYALT 

       130        140        150        160        170        180 
GLEFACGIPG SIGGAVYMNA GAYGGEVKDC IDYALCVNEQ GSLIKLTTKE LELDYRNSII 

       190        200        210        220        230        240 
QKEHLVVLEA AFTLAPGKMT EIQAKMDDLT ERRESKQPLE YPSCGSVFQR PPGHFAGKLI 

       250        260        270        280        290        300 
QDSNLQGHRI GGVEVSTKHA GFMVNVDNGT ATDYENLIHY VQKTVKEKFG IELNREVRII 


GEHPKES

« Hide

References

[1]"A structural variation for MurB: X-ray crystal structure of Staphylococcus aureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB)."
Benson T.E., Harris M.S., Choi G.H., Cialdella J.I., Herberg J.T., Martin J.P. Jr., Baldwin E.T.
Biochemistry 40:2340-2350(2001) [PubMed: 11327854] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Strain: ISP3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF300988 Genomic DNA. Translation: AAK97215.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HSKX-ray2.30A2-307[»]
ProteinModelPortalP61431.
SMRP61431. Positions 3-305.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12254.

Family and domain databases

HAMAPMF_00037. MurB.
[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.
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_STAAU
AccessionPrimary (citable) accession number: P61431
Secondary accession number(s): Q93G02
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: October 19, 2011
This is version 54 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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