Skip Header

Contribute Send feedback
Read comments (?) or add your own

P14192 (GLMU_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional protein GlmU

Including the following 2 domains:

  1. UDP-N-acetylglucosamine pyrophosphorylase
    EC=2.7.7.23
    Alternative name(s):
    N-acetylglucosamine-1-phosphate uridyltransferase
  2. Glucosamine-1-phosphate N-acetyltransferase
    EC=2.3.1.157
Gene names
Name:glmU
Synonyms:gcaD, tms, tms-26
Ordered Locus Names:BSU00500
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-GlcNAc. Responsible for the acetylation of Glc-N-1-P to give GlcNAc-1-P and for the uridyl transfer from UTP to GlcNAc-1-P which produces UDP-GlcNAc By similarity. HAMAP MF_01631

Catalytic activity

Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. HAMAP MF_01631

UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-D-glucosamine. HAMAP MF_01631

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01631

Pathway

Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. HAMAP MF_01631

Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.

Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. HAMAP MF_01631

Subcellular location

Cytoplasm By similarity HAMAP MF_01631.

Sequence similarities

In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.

In the C-terminal section; belongs to the transferase hexapeptide repeat family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456Bifunctional protein GlmU HAMAP MF_01631
PRO_0000068706

Regions

Region1 – 230230Pyrophosphorylase By similarity
Region9 – 124Substrate binding By similarity
Region78 – 792Substrate binding By similarity
Region231 – 25121Linker By similarity
Region252 – 456205N-acetyltransferase By similarity

Sites

Active site3631Proton acceptor By similarity
Metal binding1031Magnesium By similarity
Metal binding2281Magnesium By similarity
Binding site731Substrate By similarity
Binding site1401Substrate; via amide nitrogen By similarity
Binding site1551Substrate By similarity
Binding site1701Substrate By similarity
Binding site3871Acetyl-CoA By similarity
Binding site4231Acetyl-CoA; via amide nitrogen By similarity
Binding site4401Acetyl-CoA By similarity

Experimental info

Sequence conflict191S → L Ref.4
Sequence conflict71 – 722RV → AL in BAA05285. Ref.2
Sequence conflict71 – 722RV → AL in CAB11826. Ref.2
Sequence conflict1261R → A in BAA05285. Ref.2
Sequence conflict1261R → A in CAB11826. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P14192 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 6D65E0A05D5E9261

FASTA45649,610
        10         20         30         40         50         60 
MDKRFAVVLA AGQGTRMKSK LYKVLHPVCG KPMVEHVVDE ALKLSLSKLV TIVGHGAEEV 

        70         80         90        100        110        120 
KKQLGDKSEY RVQAKQLGTA HAVKQAQPFL ADEKGVTIVI CGDTPLLTAE TMEQMLKEHT 

       130        140        150        160        170        180 
QREAKRTILT AVAEDPTGYG RIIRSENGAV QKIVEHKDAS EEERLVTEIN TGTYCFDNEA 

       190        200        210        220        230        240 
LFRAIDQVSN DNAQGEYYLP DVIEILKNEG ETVAAYQTGN FQETLGVNDR VALSQAEQFM 

       250        260        270        280        290        300 
KERINKRHMQ NGVTLIDPMN TYISPDAVIG SDTVIYPGTV IKGEVQIGED TIIGPHTEIM 

       310        320        330        340        350        360 
NSAIGSRTVI KQSVVNHSKV GNDVNIGPFA HIRPDSVIGN EVKIGNFVEI KKTQFGDRSK 

       370        380        390        400        410        420 
ASHLSYVGDA EVGTDVNLGC GSITVNYDGK NKYLTKIEDG AFIGCNSNLV APVTVGEGAY 

       430        440        450 
VAAGSTVTED VPGKALAIAR ARQVNKDDYV KNIHKK

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of the tms and prs genes of Bacillus subtilis."
Nilsson D., Hove-Jensen B., Arnvig K.
Mol. Gen. Genet. 218:565-571(1989) [PubMed: 2555671] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin."
Ogasawara N., Nakai S., Yoshikawa H.
DNA Res. 1:1-14(1994) [PubMed: 7584024] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"Nucleotide sequences that signal the initiation of transcription and translation in Bacillus subtilis."
Moran C.P. Jr., Lang N., LeGrice S.F.J., Lee G., Stephens M., Sonenshein A.L., Pero J., Losick R.
Mol. Gen. Genet. 186:339-346(1982) [PubMed: 6181373] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
Strain: 168.
[5]"spoVG sequence of Bacillus megaterium and Bacillus subtilis."
Hudspeth D.S.S., Vary P.S.
Biochim. Biophys. Acta 1130:229-231(1992) [PubMed: 1373326] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
Strain: 168.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X16518 Genomic DNA. Translation: CAA34522.1.
D26185 Genomic DNA. Translation: BAA05285.1.
AL009126 Genomic DNA. Translation: CAB11826.1.
J01550 Genomic DNA. Translation: AAA22854.1.
X62378 Genomic DNA. Translation: CAA44243.1.
PIRS66080.
RefSeqNP_387931.1. NC_000964.3.

3D structure databases

ProteinModelPortalP14192.
SMRP14192. Positions 4-455.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000003539; EBBACP00000003539; EBBACG00000003532.
GeneID936139.
GenomeReviewsGene locus BSU00500 in contig AL009126_GR.
KEGGbsu:BSU00500.
PATRIC18971571. VBIBacSub10457_0051.

Organism-specific databases

GenoListBSU00500. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000000560.
HOGENOMHBG688195.
PhylomeDBP14192.
ProtClustDBPRK14354.

Enzyme and pathway databases

BioCycBSUB:BSU00500-MONOMER.

Family and domain databases

HAMAPMF_01631. GlmU.
[Tree]
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR005835. NTP_transferase.
IPR011004. Trimer_LpxA-like.
[Graphical view]
KOK04042.
PANTHERPTHR22572:SF17. PTHR22572:SF17. 1 hit.
PfamPF00132. Hexapep. 3 hits.
PF00483. NTP_transferase. 1 hit.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR01173. GlmU. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMU_BACSU
AccessionPrimary (citable) accession number: P14192
Secondary accession number(s): Q45684
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: January 25, 2012
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents