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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)DescriptionActionsGraphical viewLength
Binding sitei22UDP-GlcNAcUniRule annotation1 Publication1
Binding sitei72UDP-GlcNAcUniRule annotation2 Publications1
Metal bindingi102Magnesium or calcium2 Publications1
Binding sitei139UDP-GlcNAc; via amide nitrogenUniRule annotation2 Publications1
Binding sitei154UDP-GlcNAcUniRule annotation2 Publications1
Binding sitei169UDP-GlcNAcUniRule annotation2 Publications1
Metal bindingi227Magnesium or calcium2 Publications1
Binding sitei227UDP-GlcNAcUniRule annotation1 Publication1
Binding sitei332UDP-GlcNAcUniRule annotation1
Binding sitei350UDP-GlcNAcUniRule annotation1
Active sitei362Proton acceptorUniRule annotation1
Binding sitei365UDP-GlcNAcUniRule annotation1
Binding sitei376UDP-GlcNAcUniRule annotation1
Binding sitei379Acetyl-CoA; via amide nitrogenUniRule annotation1
Binding sitei404Acetyl-CoAUniRule annotation1
Binding sitei422Acetyl-CoA; via amide nitrogenUniRule annotation1
Binding sitei439Acetyl-CoAUniRule annotation1

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

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 databases

ChEMBLiCHEMBL1949487.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002338501 – 459Bifunctional protein GlmUAdd BLAST459

Interactioni

Subunit structurei

Homotrimer.UniRule annotation2 Publications

Protein-protein interaction databases

STRINGi170187.SpneT_02001435.

Chemistry databases

BindingDBiQ97R46.

Structurei

Secondary structure

1459
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Helixi14 – 16Combined sources3
Helixi22 – 24Combined sources3
Beta strandi25 – 27Combined sources3
Helixi32 – 41Combined sources10
Beta strandi46 – 52Combined sources7
Helixi56 – 61Combined sources6
Beta strandi62 – 71Combined sources10
Helixi78 – 83Combined sources6
Helixi86 – 89Combined sources4
Beta strandi94 – 100Combined sources7
Helixi108 – 120Combined sources13
Beta strandi124 – 131Combined sources8
Beta strandi140 – 143Combined sources4
Beta strandi149 – 153Combined sources5
Turni155 – 157Combined sources3
Helixi162 – 164Combined sources3
Beta strandi167 – 176Combined sources10
Helixi177 – 184Combined sources8
Beta strandi192 – 194Combined sources3
Helixi200 – 208Combined sources9
Beta strandi212 – 216Combined sources5
Helixi220 – 223Combined sources4
Helixi229 – 249Combined sources21
Beta strandi253 – 255Combined sources3
Helixi257 – 259Combined sources3
Beta strandi279 – 283Combined sources5
Beta strandi297 – 300Combined sources4
Beta strandi313 – 316Combined sources4
Beta strandi333 – 337Combined sources5
Beta strandi342 – 351Combined sources10
Beta strandi359 – 371Combined sources13
Beta strandi382 – 384Combined sources3
Beta strandi386 – 389Combined sources4
Beta strandi394 – 396Combined sources3
Beta strandi407 – 411Combined sources5
Helixi448 – 451Combined sources4
Helixi456 – 458Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ97R46.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 229PyrophosphorylaseUniRule annotationAdd BLAST229
Regioni8 – 11UDP-GlcNAc bindingUniRule annotation2 Publications4
Regioni77 – 78UDP-GlcNAc bindingUniRule annotation2 Publications2
Regioni101 – 102UDP-GlcNAc binding2 Publications2
Regioni230 – 250LinkerUniRule annotationAdd BLAST21
Regioni251 – 459N-acetyltransferaseUniRule annotationAdd BLAST209
Regioni385 – 386Acetyl-CoA bindingUniRule annotation1 Publication2

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.
OMAiFAHARPK.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU. 1 hit.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi170187.SpneT_02001435.

Chemistry databases

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.
OMAiFAHARPK.

Enzyme and pathway databases

UniPathwayiUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.
BRENDAi2.3.1.157. 1960.
2.7.7.23. 1960.

Miscellaneous databases

EvolutionaryTraceiQ97R46.
PROiQ97R46.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU. 1 hit.
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...

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: November 2, 2016
This is version 109 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.