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Q7V8F2 (GLMU_PROMM) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 73. 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:
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
Ordered Locus Names:PMT_0400
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length446 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-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain By similarity. HAMAP-Rule MF_01631

Catalytic activity

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

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

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule 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-Rule 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-Rule MF_01631

Subunit structure

Homotrimer By similarity. HAMAP-Rule MF_01631

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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 – 446446Bifunctional protein GlmU HAMAP-Rule MF_01631
PRO_0000233816

Regions

Region1 – 226226Pyrophosphorylase By similarity
Region7 – 104UDP-GlcNAc binding By similarity
Region78 – 792UDP-GlcNAc binding By similarity
Region227 – 24721Linker By similarity
Region248 – 446199N-acetyltransferase By similarity
Region382 – 3832Acetyl-CoA binding By similarity

Sites

Active site3591Proton acceptor By similarity
Metal binding1031Magnesium By similarity
Metal binding2241Magnesium By similarity
Binding site211UDP-GlcNAc By similarity
Binding site731UDP-GlcNAc By similarity
Binding site1401UDP-GlcNAc; via amide nitrogen By similarity
Binding site1551UDP-GlcNAc By similarity
Binding site1701UDP-GlcNAc By similarity
Binding site2241UDP-GlcNAc By similarity
Binding site3291Acetyl-CoA; amide nitrogen By similarity
Binding site3471Acetyl-CoA By similarity
Binding site3621Acetyl-CoA By similarity
Binding site3731Acetyl-CoA By similarity
Binding site4191Acetyl-CoA; via amide nitrogen By similarity
Binding site4361Acetyl-CoA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7V8F2 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: C53372DB8F81E797

FASTA44647,744
        10         20         30         40         50         60 
MLAVAILAAG KGTRMKSCLP KVLQPLAGST LVERVLTSCS GLQPQRRLLI VGHQAQEVQQ 

        70         80         90        100        110        120 
QLTDWQGLEF VVQQPQNGTG HAVQQVLPVL EGFDGELLVL NGDVPLLRPS TIEHLVNEHR 

       130        140        150        160        170        180 
SSGADVTLLT ARLADPTGYG RVFSDQQGRV SSIVEHRDCS DEQRHNNLTN AGIYCFNWKK 

       190        200        210        220        230        240 
LAAVLPQLCS DNDQGELYLT DTVALLPIAM HVEVADPDEV NGINDRCQLA NCEALLQERL 

       250        260        270        280        290        300 
RNYWMKEGVT FTDPASCTLS EDCQFGRDVV IEPQTHLRGC CNIGDGCQLG PGSLIENAEL 

       310        320        330        340        350        360 
GHGVSVLHSV VCDAKVGNEV AIGPFSHLRP GAGIADQCRI GNFVEIKKSQ IGEGSKVNHL 

       370        380        390        400        410        420 
SYIGDAQLGR HVNVGAGTIT ANYDGVRKHL TVVGDNSKTG ANSVLVAPIV LGSDVTVGAG 

       430        440 
STLTKDVPNG ALALGRSKQL IKNGWQ 

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References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9313.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548175 Genomic DNA. Translation: CAE20575.1.
RefSeqNP_894233.1. NC_005071.1.

3D structure databases

ProteinModelPortalQ7V8F2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING74547.PMT0400.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE20575; CAE20575; PMT_0400.
GeneID1729380.
KEGGpmt:PMT0400.
PATRIC23008645. VBIProMar135351_0480.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
KOK04042.
OMADCVTNQD.
OrthoDBEOG6Z6FQZ.

Enzyme and pathway databases

UniPathwayUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
HAMAPMF_01631. GlmU.
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamPF00132. Hexapep. 4 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsTIGR01173. glmU. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLMU_PROMM
AccessionPrimary (citable) accession number: Q7V8F2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: October 1, 2003
Last modified: June 11, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways