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Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate.UniRule annotation
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine.UniRule annotation

Cofactori

Mg2+1 Publication, Ca2+1 PublicationNote: Binds 1 Mg2+ ion per subunit (PubMed:11124906). Can also use Ca2+ ion to a lesser extent (PubMed:11118459).2 Publications

Pathwayi: UDP-N-acetyl-alpha-D-glucosamine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Bifunctional protein GlmU (glmU)
This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II), the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.

Pathwayi: UDP-N-acetyl-alpha-D-glucosamine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional protein GlmU (glmU)
This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate, the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.

Pathwayi: LPS lipid A biosynthesis

This protein is involved in the pathway LPS lipid A biosynthesis, which is part of Bacterial outer membrane biogenesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway LPS lipid A biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei22 – 221UDP-GlcNAcUniRule annotation1 Publication
Binding sitei72 – 721UDP-GlcNAcUniRule annotation2 Publications
Metal bindingi102 – 1021Magnesium or calcium2 Publications
Binding sitei139 – 1391UDP-GlcNAc; via amide nitrogenUniRule annotation2 Publications
Binding sitei154 – 1541UDP-GlcNAcUniRule annotation2 Publications
Binding sitei169 – 1691UDP-GlcNAcUniRule annotation2 Publications
Metal bindingi227 – 2271Magnesium or calcium2 Publications
Binding sitei227 – 2271UDP-GlcNAcUniRule annotation1 Publication
Binding sitei332 – 3321UDP-GlcNAcUniRule annotation
Binding sitei350 – 3501UDP-GlcNAcUniRule annotation
Active sitei362 – 3621Proton acceptorUniRule annotation
Binding sitei365 – 3651UDP-GlcNAcUniRule annotation
Binding sitei376 – 3761UDP-GlcNAcUniRule annotation
Binding sitei379 – 3791Acetyl-CoA; via amide nitrogenUniRule annotation
Binding sitei404 – 4041Acetyl-CoAUniRule annotation
Binding sitei422 – 4221Acetyl-CoA; via amide nitrogenUniRule annotation
Binding sitei439 – 4391Acetyl-CoAUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciSPNE170187:GHGN-992-MONOMER.
BRENDAi2.3.1.157. 1960.
2.7.7.23. 1960.
UniPathwayiUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional protein GlmUUniRule annotation
Including the following 2 domains:
UDP-N-acetylglucosamine pyrophosphorylaseUniRule annotation (EC:2.7.7.23UniRule annotation)
Alternative name(s):
N-acetylglucosamine-1-phosphate uridyltransferaseUniRule annotation
Glucosamine-1-phosphate N-acetyltransferaseUniRule annotation (EC:2.3.1.157UniRule annotation)
Gene namesi
Name:glmUUniRule annotation
Ordered Locus Names:SP_0988
OrganismiStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Taxonomic identifieri170187 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000000585 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1949487.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459Bifunctional protein GlmUPRO_0000233850Add
BLAST

Interactioni

Subunit structurei

Homotrimer.UniRule annotation2 Publications

Protein-protein interaction databases

STRINGi170187.SpneT_02001435.

Chemistry

BindingDBiQ97R46.

Structurei

Secondary structure

1
459
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Helixi14 – 163Combined sources
Helixi22 – 243Combined sources
Beta strandi25 – 273Combined sources
Helixi32 – 4110Combined sources
Beta strandi46 – 527Combined sources
Helixi56 – 616Combined sources
Beta strandi62 – 7110Combined sources
Helixi78 – 836Combined sources
Helixi86 – 894Combined sources
Beta strandi94 – 1007Combined sources
Helixi108 – 12013Combined sources
Beta strandi124 – 1318Combined sources
Beta strandi140 – 1434Combined sources
Beta strandi149 – 1535Combined sources
Turni155 – 1573Combined sources
Helixi162 – 1643Combined sources
Beta strandi167 – 17610Combined sources
Helixi177 – 1848Combined sources
Beta strandi192 – 1943Combined sources
Helixi200 – 2089Combined sources
Beta strandi212 – 2165Combined sources
Helixi220 – 2234Combined sources
Helixi229 – 24921Combined sources
Beta strandi253 – 2553Combined sources
Helixi257 – 2593Combined sources
Beta strandi279 – 2835Combined sources
Beta strandi297 – 3004Combined sources
Beta strandi313 – 3164Combined sources
Beta strandi333 – 3375Combined sources
Beta strandi342 – 35110Combined sources
Beta strandi359 – 37113Combined sources
Beta strandi382 – 3843Combined sources
Beta strandi386 – 3894Combined sources
Beta strandi394 – 3963Combined sources
Beta strandi407 – 4115Combined sources
Helixi448 – 4514Combined sources
Helixi456 – 4583Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G95X-ray2.33A1-459[»]
1G97X-ray1.96A1-459[»]
1HM0X-ray2.30A/B2-459[»]
1HM8X-ray2.50A/B2-459[»]
1HM9X-ray1.75A/B2-459[»]
ProteinModelPortaliQ97R46.
SMRiQ97R46. Positions 2-447.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ97R46.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 229229PyrophosphorylaseUniRule annotationAdd
BLAST
Regioni8 – 114UDP-GlcNAc bindingUniRule annotation2 Publications
Regioni77 – 782UDP-GlcNAc bindingUniRule annotation2 Publications
Regioni101 – 1022UDP-GlcNAc binding2 Publications
Regioni230 – 25021LinkerUniRule annotationAdd
BLAST
Regioni251 – 459209N-acetyltransferaseUniRule annotationAdd
BLAST
Regioni385 – 3862Acetyl-CoA bindingUniRule annotation1 Publication

Sequence similaritiesi

In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.UniRule annotationCurated
In the C-terminal section; belongs to the transferase hexapeptide repeat family.UniRule annotationCurated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CAJ. Bacteria.
COG1207. LUCA.
HOGENOMiHOG000283476.
KOiK04042.
OMAiSITANYD.
OrthoDBiEOG6Z6FQZ.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU.
InterProiIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep.
IPR018357. Hexapep_transf_CS.
IPR005835. NTP_transferase_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 2 hits.
PF14602. Hexapep_2. 1 hit.
PF00483. NTP_transferase. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR01173. glmU. 1 hit.
PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q97R46-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNFAIILAA GKGTRMKSDL PKVLHKVAGI SMLEHVFRSV GAIQPEKTVT
60 70 80 90 100
VVGHKAELVE EVLAGQTEFV TQSEQLGTGH AVMMTEPILE GLSGHTLVIA
110 120 130 140 150
GDTPLITGES LKNLIDFHIN HKNVATILTA ETDNPFGYGR IVRNDNAEVL
160 170 180 190 200
RIVEQKDATD FEKQIKEINT GTYVFDNERL FEALKNINTN NAQGEYYITD
210 220 230 240 250
VIGIFRETGE KVGAYTLKDF DESLGVNDRV ALATAESVMR RRINHKHMVN
260 270 280 290 300
GVSFVNPEAT YIDIDVEIAS EVQIEANVTL KGQTKIGAET VLTNGTYVVD
310 320 330 340 350
STIGAGAVIT NSMIEESSVA DGVIVGPYAH IRPNSSLGAQ VHIGNFVEVK
360 370 380 390 400
GSSIGENTKA GHLTYIGNCE VGSNVNFGAG TITVNYDGKN KYKTVIGNNV
410 420 430 440 450
FVGSNSTIIA PVELGDNSLV GAGSTITKDV PADAIAIGRG RQINKDEYAT

RLPHHPKNQ
Length:459
Mass (Da):49,345
Last modified:October 1, 2001 - v1
Checksum:iF4EFE18D768DC4A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005672 Genomic DNA. Translation: AAK75107.1.
PIRiB95114.
RefSeqiWP_000064406.1. NZ_AKVY01000001.1.

Genome annotation databases

EnsemblBacteriaiAAK75107; AAK75107; SP_0988.
KEGGispn:SP_0988.
PATRICi19706381. VBIStrPne105772_1036.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005672 Genomic DNA. Translation: AAK75107.1.
PIRiB95114.
RefSeqiWP_000064406.1. NZ_AKVY01000001.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G95X-ray2.33A1-459[»]
1G97X-ray1.96A1-459[»]
1HM0X-ray2.30A/B2-459[»]
1HM8X-ray2.50A/B2-459[»]
1HM9X-ray1.75A/B2-459[»]
ProteinModelPortaliQ97R46.
SMRiQ97R46. Positions 2-447.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi170187.SpneT_02001435.

Chemistry

BindingDBiQ97R46.
ChEMBLiCHEMBL1949487.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK75107; AAK75107; SP_0988.
KEGGispn:SP_0988.
PATRICi19706381. VBIStrPne105772_1036.

Phylogenomic databases

eggNOGiENOG4105CAJ. Bacteria.
COG1207. LUCA.
HOGENOMiHOG000283476.
KOiK04042.
OMAiSITANYD.
OrthoDBiEOG6Z6FQZ.

Enzyme and pathway databases

UniPathwayiUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.
BioCyciSPNE170187:GHGN-992-MONOMER.
BRENDAi2.3.1.157. 1960.
2.7.7.23. 1960.

Miscellaneous databases

EvolutionaryTraceiQ97R46.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU.
InterProiIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep.
IPR018357. Hexapep_transf_CS.
IPR005835. NTP_transferase_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 2 hits.
PF14602. Hexapep_2. 1 hit.
PF00483. NTP_transferase. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR01173. glmU. 1 hit.
PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-334 / TIGR4.
  2. "Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture."
    Sulzenbacher G., Gal L., Peneff C., Fassy F., Bourne Y.
    J. Biol. Chem. 276:11844-11851(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF NATIVE PROTEIN AND IN COMPLEX WITH ACETYL-COA; CALIUM ION AND UDP-GLCNAC, SUBUNIT, COFACTOR.
    Strain: R800.
  3. "Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 2.33 A resolution and in complex with UDP-N-acetylglucosamine and Mg(2+) at 1.96 A resolution."
    Kostrewa D., D'Arcy A., Takacs B., Kamber M.
    J. Mol. Biol. 305:279-289(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF NATIVE PROTEIN AND IN COMPLEX WITH WITH BOTH UDP-GLCNAC AND MAGNESIUM, SUBUNIT, COFACTOR.

Entry informationi

Entry nameiGLMU_STRPN
AccessioniPrimary (citable) accession number: Q97R46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: October 1, 2001
Last modified: February 17, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.