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Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Thioalkalivibrio sulfidiphilus (strain HL-EbGR7)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

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 sitei24UDP-GlcNAcUniRule annotation1
Binding sitei75UDP-GlcNAcUniRule annotation1
Metal bindingi104MagnesiumUniRule annotation1
Binding sitei140UDP-GlcNAc; via amide nitrogenUniRule annotation1
Binding sitei155UDP-GlcNAcUniRule annotation1
Binding sitei170UDP-GlcNAcUniRule annotation1
Metal bindingi228MagnesiumUniRule annotation1
Binding sitei228UDP-GlcNAcUniRule annotation1
Binding sitei334UDP-GlcNAcUniRule annotation1
Binding sitei352UDP-GlcNAcUniRule annotation1
Active sitei364Proton acceptorUniRule annotation1
Binding sitei367UDP-GlcNAcUniRule annotation1
Binding sitei378UDP-GlcNAcUniRule annotation1
Binding sitei381Acetyl-CoA; via amide nitrogenUniRule annotation1
Binding sitei406Acetyl-CoAUniRule annotation1
Binding sitei424Acetyl-CoA; via amide nitrogenUniRule annotation1
Binding sitei441Acetyl-CoAUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Transferase
Biological processCell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyciTSUL396588:G1GUK-3353-MONOMER
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:Tgr7_3303
OrganismiThioalkalivibrio sulfidiphilus (strain HL-EbGR7)
Taxonomic identifieri396588 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeThioalkalivibrio
Proteomesi
  • UP000002383 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001865081 – 459Bifunctional protein GlmUAdd BLAST459

Proteomic databases

PRIDEiB8GRB6

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Protein-protein interaction databases

STRINGi396588.Tgr7_3303

Structurei

3D structure databases

ProteinModelPortaliB8GRB6
SMRiB8GRB6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 230PyrophosphorylaseUniRule annotationAdd BLAST230
Regioni10 – 13UDP-GlcNAc bindingUniRule annotation4
Regioni80 – 81UDP-GlcNAc bindingUniRule annotation2
Regioni102 – 104UDP-GlcNAc bindingUniRule annotation3
Regioni231 – 251LinkerUniRule annotationAdd BLAST21
Regioni252 – 459N-acetyltransferaseUniRule annotationAdd BLAST208
Regioni387 – 388Acetyl-CoA bindingUniRule annotation2

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CAJ Bacteria
COG1207 LUCA
KOiK04042
OMAiIEPQTHL
OrthoDBiPOG091H02I2

Family and domain databases

CDDicd03353 LbH_GlmU_C, 1 hit
Gene3Di3.90.550.10, 1 hit
HAMAPiMF_01631 GlmU, 1 hit
InterProiView protein in InterPro
IPR005882 Bifunctional_GlmU
IPR038009 GlmU_C_LbH
IPR001451 Hexapep
IPR025877 MobA-like_NTP_Trfase
IPR029044 Nucleotide-diphossugar_trans
IPR011004 Trimer_LpxA-like_sf
PfamiView protein in Pfam
PF00132 Hexapep, 3 hits
PF14602 Hexapep_2, 1 hit
PF12804 NTP_transf_3, 1 hit
SUPFAMiSSF51161 SSF51161, 1 hit
SSF53448 SSF53448, 1 hit
TIGRFAMsiTIGR01173 glmU, 1 hit

Sequencei

Sequence statusi: Complete.

B8GRB6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTPTSILIL AAGQGTRMRS SLPKVLQPLA GRPLLSHVLD TARSLDPHRL
60 70 80 90 100
VVVYGHGGDR VREAFPEDDI RWVHQAEQRG TGHAVQVALP ETDADDRVLI
110 120 130 140 150
LYGDVPLVRG ETVRRLLAQL DEGGDLVILT AALKSPTGYG RILRDDSGRV
160 170 180 190 200
QRIVEEKDAS DSERRVNEVN TGIMAARASD FTRWLSKVTN DNAQGEFYLT
210 220 230 240 250
DCVALANTEG RRVEAVVGHE AIELMGVNDK RQLAEQERAY QRREAERLMV
260 270 280 290 300
QGVTVIDPAR LDVRGEVEAG RDVSLDINVI LQGSVKLGEG AKVGAGCVII
310 320 330 340 350
DSEIGPGAHI LPHTVIEGAV IGAGASVGPF ARIRPGTHTD SNAKIGNFVE
360 370 380 390 400
VKNARVGEGS KINHLSYVGD SELGRDVNIG AGTITCNYDG ANKHKTIIGD
410 420 430 440 450
RAFIGSNTAL VAPLTVGEGA TIGAGTTLNK DAPPGELTVA RAKAITIPGW

KRPVKKPKE
Length:459
Mass (Da):49,073
Last modified:March 3, 2009 - v1
Checksum:i6D7E892C8B1ED632
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001339 Genomic DNA Translation: ACL74370.1
RefSeqiWP_012639832.1, NC_011901.1

Genome annotation databases

EnsemblBacteriaiACL74370; ACL74370; Tgr7_3303
KEGGitgr:Tgr7_3303

Similar proteinsi

Entry informationi

Entry nameiGLMU_THISH
AccessioniPrimary (citable) accession number: B8GRB6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: May 23, 2018
This is version 57 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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