UniProtKB - Q97R46 (GLMU_STRPN)
Protein
Bifunctional protein GlmU
Gene
glmU
Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
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 + α-D-glucosamine 1-phosphate = CoA + H+ + N-acetyl-α-D-glucosamine 1-phosphateUniRule annotationEC:2.3.1.157UniRule annotation
- H+ + N-acetyl-α-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-α-D-glucosamineUniRule annotationEC:2.7.7.23UniRule 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
: UDP-N-acetyl-alpha-D-glucosamine biosynthesis Pathwayi
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 annotationProteins known to be involved in the 2 steps of the subpathway in this organism are:
- no protein annotated in this organism
- Bifunctional protein GlmU (glmU)
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 annotationProteins known to be involved in this subpathway in this organism are:
- Bifunctional protein GlmU (glmU)
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 annotationView 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 22 | UDP-GlcNAcUniRule annotation1 Publication | 1 | |
Binding sitei | 72 | UDP-GlcNAcUniRule annotation2 Publications | 1 | |
Metal bindingi | 102 | Magnesium or calcium2 Publications | 1 | |
Binding sitei | 139 | UDP-GlcNAc; via amide nitrogenUniRule annotation2 Publications | 1 | |
Binding sitei | 154 | UDP-GlcNAcUniRule annotation2 Publications | 1 | |
Binding sitei | 169 | UDP-GlcNAcUniRule annotation2 Publications | 1 | |
Metal bindingi | 227 | Magnesium or calcium2 Publications | 1 | |
Binding sitei | 227 | UDP-GlcNAcUniRule annotation1 Publication | 1 | |
Binding sitei | 332 | UDP-GlcNAcUniRule annotation | 1 | |
Binding sitei | 350 | UDP-GlcNAcUniRule annotation | 1 | |
Active sitei | 362 | Proton acceptorUniRule annotation | 1 | |
Binding sitei | 365 | UDP-GlcNAcUniRule annotation | 1 | |
Binding sitei | 376 | UDP-GlcNAcUniRule annotation | 1 | |
Binding sitei | 379 | Acetyl-CoA; via amide nitrogenUniRule annotation | 1 | |
Binding sitei | 404 | Acetyl-CoAUniRule annotation | 1 | |
Binding sitei | 422 | Acetyl-CoA; via amide nitrogenUniRule annotation | 1 | |
Binding sitei | 439 | Acetyl-CoAUniRule annotation | 1 |
GO - Molecular functioni
- glucosamine-1-phosphate N-acetyltransferase activity Source: UniProtKB-UniRule
- magnesium ion binding Source: UniProtKB-UniRule
- UDP-N-acetylglucosamine diphosphorylase activity Source: UniProtKB-UniRule
GO - Biological processi
- cell morphogenesis Source: UniProtKB-UniRule
- cell wall organization Source: UniProtKB-KW
- lipid A biosynthetic process Source: UniProtKB-UniPathway
- lipopolysaccharide biosynthetic process Source: InterPro
- peptidoglycan biosynthetic process Source: UniProtKB-UniRule
- regulation of cell shape Source: UniProtKB-KW
- UDP-N-acetylglucosamine biosynthetic process Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Acyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Transferase |
Biological process | Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | SPNE170187:G1FZB-1017-MONOMER |
BRENDAi | 2.3.1.157, 1960 2.7.7.23, 1960 |
UniPathwayi | UPA00113;UER00532 UPA00113;UER00533 UPA00973 |
Names & Taxonomyi
Protein namesi | Recommended name: Bifunctional protein GlmUUniRule annotationIncluding the following 2 domains: |
Gene namesi | Name:glmUUniRule annotation Ordered Locus Names:SP_0988 |
Organismi | Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) |
Taxonomic identifieri | 170187 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › |
Proteomesi |
|
Subcellular locationi
- Cytoplasm UniRule annotation
GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Chemistry databases
ChEMBLi | CHEMBL1949487 |
DrugBanki | DB03397, Uridine-Diphosphate-N-Acetylglucosamine |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000233850 | 1 – 459 | Bifunctional protein GlmUAdd BLAST | 459 |
Interactioni
Subunit structurei
Homotrimer.
UniRule annotation2 PublicationsProtein-protein interaction databases
STRINGi | 170187.SP_0988 |
Chemistry databases
BindingDBi | Q97R46 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q97R46 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q97R46 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 229 | PyrophosphorylaseUniRule annotationAdd BLAST | 229 | |
Regioni | 8 – 11 | UDP-GlcNAc bindingUniRule annotation2 Publications | 4 | |
Regioni | 77 – 78 | UDP-GlcNAc bindingUniRule annotation2 Publications | 2 | |
Regioni | 101 – 102 | UDP-GlcNAc binding2 Publications | 2 | |
Regioni | 230 – 250 | LinkerUniRule annotationAdd BLAST | 21 | |
Regioni | 251 – 459 | N-acetyltransferaseUniRule annotationAdd BLAST | 209 | |
Regioni | 385 – 386 | Acetyl-CoA bindingUniRule annotation1 Publication | 2 |
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
RepeatPhylogenomic databases
eggNOGi | COG1207, Bacteria |
OMAi | TAIVEHK |
Family and domain databases
CDDi | cd03353, LbH_GlmU_C, 1 hit |
Gene3Di | 3.90.550.10, 1 hit |
HAMAPi | MF_01631, GlmU, 1 hit |
InterProi | View protein in InterPro IPR005882, Bifunctional_GlmU IPR038009, GlmU_C_LbH IPR001451, Hexapep IPR018357, Hexapep_transf_CS IPR005835, NTP_transferase_dom IPR029044, Nucleotide-diphossugar_trans IPR011004, Trimer_LpxA-like_sf |
Pfami | View protein in Pfam PF00132, Hexapep, 2 hits PF14602, Hexapep_2, 1 hit PF00483, NTP_transferase, 1 hit |
SUPFAMi | SSF51161, SSF51161, 1 hit SSF53448, SSF53448, 1 hit |
TIGRFAMsi | TIGR01173, glmU, 1 hit |
PROSITEi | View protein in PROSITE PS00101, HEXAPEP_TRANSFERASES, 1 hit |
i Sequence
Sequence statusi: Complete.
Q97R46-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE005672 Genomic DNA Translation: AAK75107.1 |
PIRi | B95114 |
RefSeqi | WP_000064406.1, NZ_AKVY01000001.1 |
Genome annotation databases
EnsemblBacteriai | AAK75107; AAK75107; SP_0988 |
KEGGi | spn:SP_0988 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE005672 Genomic DNA Translation: AAK75107.1 |
PIRi | B95114 |
RefSeqi | WP_000064406.1, NZ_AKVY01000001.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1G95 | X-ray | 2.33 | A | 1-459 | [»] | |
1G97 | X-ray | 1.96 | A | 1-459 | [»] | |
1HM0 | X-ray | 2.30 | A/B | 2-459 | [»] | |
1HM8 | X-ray | 2.50 | A/B | 2-459 | [»] | |
1HM9 | X-ray | 1.75 | A/B | 2-459 | [»] | |
SMRi | Q97R46 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 170187.SP_0988 |
Chemistry databases
BindingDBi | Q97R46 |
ChEMBLi | CHEMBL1949487 |
DrugBanki | DB03397, Uridine-Diphosphate-N-Acetylglucosamine |
Genome annotation databases
EnsemblBacteriai | AAK75107; AAK75107; SP_0988 |
KEGGi | spn:SP_0988 |
Phylogenomic databases
eggNOGi | COG1207, Bacteria |
OMAi | TAIVEHK |
Enzyme and pathway databases
UniPathwayi | UPA00113;UER00532 UPA00113;UER00533 UPA00973 |
BioCyci | SPNE170187:G1FZB-1017-MONOMER |
BRENDAi | 2.3.1.157, 1960 2.7.7.23, 1960 |
Miscellaneous databases
EvolutionaryTracei | Q97R46 |
PROi | PR:Q97R46 |
Family and domain databases
CDDi | cd03353, LbH_GlmU_C, 1 hit |
Gene3Di | 3.90.550.10, 1 hit |
HAMAPi | MF_01631, GlmU, 1 hit |
InterProi | View protein in InterPro IPR005882, Bifunctional_GlmU IPR038009, GlmU_C_LbH IPR001451, Hexapep IPR018357, Hexapep_transf_CS IPR005835, NTP_transferase_dom IPR029044, Nucleotide-diphossugar_trans IPR011004, Trimer_LpxA-like_sf |
Pfami | View protein in Pfam PF00132, Hexapep, 2 hits PF14602, Hexapep_2, 1 hit PF00483, NTP_transferase, 1 hit |
SUPFAMi | SSF51161, SSF51161, 1 hit SSF53448, SSF53448, 1 hit |
TIGRFAMsi | TIGR01173, glmU, 1 hit |
PROSITEi | View protein in PROSITE PS00101, HEXAPEP_TRANSFERASES, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | GLMU_STRPN | |
Accessioni | Q97R46Primary (citable) accession number: Q97R46 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 2, 2006 |
Last sequence update: | October 1, 2001 | |
Last modified: | December 2, 2020 | |
This is version 129 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- 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