Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Prochlorococcus marinus (strain MIT 9313)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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 sitei21UDP-GlcNAcUniRule annotation1
Binding sitei73UDP-GlcNAcUniRule annotation1
Metal bindingi103MagnesiumUniRule annotation1
Binding sitei140UDP-GlcNAc; via amide nitrogenUniRule annotation1
Binding sitei155UDP-GlcNAcUniRule annotation1
Binding sitei170UDP-GlcNAcUniRule annotation1
Metal bindingi224MagnesiumUniRule annotation1
Binding sitei224UDP-GlcNAcUniRule annotation1
Binding sitei329UDP-GlcNAcUniRule annotation1
Binding sitei347UDP-GlcNAcUniRule annotation1
Active sitei359Proton acceptorUniRule annotation1
Binding sitei362UDP-GlcNAcUniRule annotation1
Binding sitei373UDP-GlcNAcUniRule annotation1
Binding sitei376Acetyl-CoA; via amide nitrogenUniRule annotation1
Binding sitei419Acetyl-CoA; via amide nitrogenUniRule annotation1
Binding sitei436Acetyl-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

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:PMT_0400
OrganismiProchlorococcus marinus (strain MIT 9313)
Taxonomic identifieri74547 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesProchloraceaeProchlorococcus
Proteomesi
  • UP000001423 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002338161 – 446Bifunctional protein GlmUAdd BLAST446

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Protein-protein interaction databases

STRINGi74547.PMT0400.

Structurei

3D structure databases

ProteinModelPortaliQ7V8F2.
SMRiQ7V8F2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 226PyrophosphorylaseUniRule annotationAdd BLAST226
Regioni7 – 10UDP-GlcNAc bindingUniRule annotation4
Regioni78 – 79UDP-GlcNAc bindingUniRule annotation2
Regioni227 – 247LinkerUniRule annotationAdd BLAST21
Regioni248 – 446N-acetyltransferaseUniRule annotationAdd BLAST199
Regioni382 – 383Acetyl-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.
OMAiFAHARPK.
OrthoDBiPOG091H02I2.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU. 1 hit.
InterProiIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep.
IPR025877. MobA-like_NTP_Trfase.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 3 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR01173. glmU. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7V8F2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLAVAILAAG KGTRMKSCLP KVLQPLAGST LVERVLTSCS GLQPQRRLLI
60 70 80 90 100
VGHQAQEVQQ QLTDWQGLEF VVQQPQNGTG HAVQQVLPVL EGFDGELLVL
110 120 130 140 150
NGDVPLLRPS TIEHLVNEHR SSGADVTLLT ARLADPTGYG RVFSDQQGRV
160 170 180 190 200
SSIVEHRDCS DEQRHNNLTN AGIYCFNWKK LAAVLPQLCS DNDQGELYLT
210 220 230 240 250
DTVALLPIAM HVEVADPDEV NGINDRCQLA NCEALLQERL RNYWMKEGVT
260 270 280 290 300
FTDPASCTLS EDCQFGRDVV IEPQTHLRGC CNIGDGCQLG PGSLIENAEL
310 320 330 340 350
GHGVSVLHSV VCDAKVGNEV AIGPFSHLRP GAGIADQCRI GNFVEIKKSQ
360 370 380 390 400
IGEGSKVNHL SYIGDAQLGR HVNVGAGTIT ANYDGVRKHL TVVGDNSKTG
410 420 430 440
ANSVLVAPIV LGSDVTVGAG STLTKDVPNG ALALGRSKQL IKNGWQ
Length:446
Mass (Da):47,744
Last modified:October 1, 2003 - v1
Checksum:iC53372DB8F81E797
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX548175 Genomic DNA. Translation: CAE20575.1.
RefSeqiWP_011129779.1. NC_005071.1.

Genome annotation databases

EnsemblBacteriaiCAE20575; CAE20575; PMT_0400.
KEGGipmt:PMT_0400.
PATRICi23008645. VBIProMar135351_0480.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX548175 Genomic DNA. Translation: CAE20575.1.
RefSeqiWP_011129779.1. NC_005071.1.

3D structure databases

ProteinModelPortaliQ7V8F2.
SMRiQ7V8F2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi74547.PMT0400.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE20575; CAE20575; PMT_0400.
KEGGipmt:PMT_0400.
PATRICi23008645. VBIProMar135351_0480.

Phylogenomic databases

eggNOGiENOG4105CAJ. Bacteria.
COG1207. LUCA.
KOiK04042.
OMAiFAHARPK.
OrthoDBiPOG091H02I2.

Enzyme and pathway databases

UniPathwayiUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU. 1 hit.
InterProiIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep.
IPR025877. MobA-like_NTP_Trfase.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 3 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR01173. glmU. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGLMU_PROMM
AccessioniPrimary (citable) accession number: Q7V8F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: October 1, 2003
Last modified: November 30, 2016
This is version 88 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

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.