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Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258)
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 sitei27UDP-GlcNAcUniRule annotation1
Binding sitei82UDP-GlcNAcUniRule annotation1
Metal bindingi112MagnesiumUniRule annotation1
Binding sitei149UDP-GlcNAc; via amide nitrogenUniRule annotation1
Binding sitei164UDP-GlcNAcUniRule annotation1
Binding sitei179UDP-GlcNAcUniRule annotation1
Metal bindingi235MagnesiumUniRule annotation1
Binding sitei235UDP-GlcNAcUniRule annotation1
Binding sitei341UDP-GlcNAcUniRule annotation1
Binding sitei359UDP-GlcNAcUniRule annotation1
Active sitei371Proton acceptorUniRule annotation1
Binding sitei374UDP-GlcNAcUniRule annotation1
Binding sitei385UDP-GlcNAcUniRule annotation1
Binding sitei388Acetyl-CoA; via amide nitrogenUniRule annotation1
Binding sitei413Acetyl-CoAUniRule annotation1
Binding sitei431Acetyl-CoA; via amide nitrogenUniRule annotation1
Binding sitei448Acetyl-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:A2cp1_4101
OrganismiAnaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258)
Taxonomic identifieri455488 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeAnaeromyxobacteraceaeAnaeromyxobacter
Proteomesi
  • UP000007089 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_10001863921 – 488Bifunctional protein GlmUAdd BLAST488

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB8J9N1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 237PyrophosphorylaseUniRule annotationAdd BLAST237
Regioni13 – 16UDP-GlcNAc bindingUniRule annotation4
Regioni87 – 88UDP-GlcNAc bindingUniRule annotation2
Regioni110 – 112UDP-GlcNAc bindingUniRule annotation3
Regioni238 – 258LinkerUniRule annotationAdd BLAST21
Regioni259 – 488N-acetyltransferaseUniRule annotationAdd BLAST230
Regioni394 – 395Acetyl-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

HOGENOMiHOG000283476.
KOiK04042.
OMAiFAHARPK.
OrthoDBiPOG091H02I2.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU. 1 hit.
InterProiIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep.
IPR018357. Hexapep_transf_CS.
IPR025877. MobA-like_NTP_Trfase.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 2 hits.
PF14602. Hexapep_2. 1 hit.
PF12804. NTP_transf_3. 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.

B8J9N1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRTRTPLAA IVLAAGKGTR MKSNKAKVLH EVAGRPLAYY PVKRALELGA
60 70 80 90 100
SPVVVVVGHQ AEAVEAALSA ALPEAPLRFA VQEQQLGTAH AVLAAKRALR
110 120 130 140 150
GYRGPVLILS GDTPLLRAET LEAVVSAGRR ARAAVSLATM TLEVPRGYGR
160 170 180 190 200
VVRDARGRPA RIVEEKDATE AERAVREVNA GLYCVDAELL WKKLAKVGTA
210 220 230 240 250
NAQREFYLTD LVPMAAQAGG VAGVEVPAEE ASGVNDRVEL SRANRVMVGR
260 270 280 290 300
LAEAFMRAGV TIEDPARFDC DEGVEIGADA VIEPNVRLRG RTRVGARTRV
310 320 330 340 350
GVGAVITDGV LADGVTVNPY TVISEAQVAE GAILGPFSRL RPGADIGPEA
360 370 380 390 400
HVGNFVEVKK SRLGKGAKAN HLAYLGDAEI GAGANIGAGT ITCNYDGERK
410 420 430 440 450
NPTRIGEGAF IGSDSILVAP IEIGAGAYVA AGSTLTDPVP AGALALGRAR
460 470 480
QVTKEGWVAQ RQAEKQMKGT ATGPASARKG RPAARRAS
Length:488
Mass (Da):50,902
Last modified:March 3, 2009 - v1
Checksum:i889645503870632F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001359 Genomic DNA. Translation: ACL67419.1.
RefSeqiWP_015935139.1. NC_011891.1.

Genome annotation databases

EnsemblBacteriaiACL67419; ACL67419; A2cp1_4101.
KEGGiacp:A2cp1_4101.
PATRICi20915156. VBIAnaDeh28364_4136.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001359 Genomic DNA. Translation: ACL67419.1.
RefSeqiWP_015935139.1. NC_011891.1.

3D structure databases

ProteinModelPortaliB8J9N1.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACL67419; ACL67419; A2cp1_4101.
KEGGiacp:A2cp1_4101.
PATRICi20915156. VBIAnaDeh28364_4136.

Phylogenomic databases

HOGENOMiHOG000283476.
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.
IPR018357. Hexapep_transf_CS.
IPR025877. MobA-like_NTP_Trfase.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 2 hits.
PF14602. Hexapep_2. 1 hit.
PF12804. NTP_transf_3. 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_ANAD2
AccessioniPrimary (citable) accession number: B8J9N1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: November 2, 2016
This is version 51 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

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.