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B8GRB6

- GLMU_THISH

UniProt

B8GRB6 - GLMU_THISH

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Protein
Bifunctional protein GlmU
Gene
glmU, Tgr7_3303
Organism
Thioalkalivibrio sp. (strain HL-EbGR7)
Status
Reviewed - 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 By similarity.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

Binds 1 magnesium ion per subunit By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei24 – 241UDP-GlcNAc By similarity
Binding sitei75 – 751UDP-GlcNAc By similarity
Metal bindingi104 – 1041Magnesium By similarity
Binding sitei140 – 1401UDP-GlcNAc; via amide nitrogen By similarity
Binding sitei155 – 1551UDP-GlcNAc By similarity
Binding sitei170 – 1701UDP-GlcNAc By similarity
Metal bindingi228 – 2281Magnesium By similarity
Binding sitei228 – 2281UDP-GlcNAc By similarity
Binding sitei334 – 3341Acetyl-CoA; amide nitrogen By similarity
Binding sitei352 – 3521Acetyl-CoA By similarity
Active sitei364 – 3641Proton acceptor By similarity
Binding sitei367 – 3671Acetyl-CoA By similarity
Binding sitei378 – 3781Acetyl-CoA By similarity
Binding sitei406 – 4061Acetyl-CoA By similarity
Binding sitei424 – 4241Acetyl-CoA; via amide nitrogen By similarity
Binding sitei441 – 4411Acetyl-CoA By similarity

GO - Molecular functioni

  1. UDP-N-acetylglucosamine diphosphorylase activity Source: UniProtKB-HAMAP
  2. glucosamine-1-phosphate N-acetyltransferase activity Source: UniProtKB-HAMAP
  3. magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. UDP-N-acetylglucosamine biosynthetic process Source: UniProtKB-UniPathway
  2. cell morphogenesis Source: UniProtKB-HAMAP
  3. lipid A biosynthetic process Source: UniProtKB-UniPathway
  4. lipopolysaccharide biosynthetic process Source: InterPro
  5. peptidoglycan biosynthetic process Source: UniProtKB-HAMAP
  6. regulation of cell shape Source: UniProtKB-KW
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

BioCyciTSUL396588:GH5B-3355-MONOMER.
UniPathwayiUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional protein GlmU
Including the following 2 domains:
UDP-N-acetylglucosamine pyrophosphorylase (EC:2.7.7.23)
Alternative name(s):
N-acetylglucosamine-1-phosphate uridyltransferase
Glucosamine-1-phosphate N-acetyltransferase (EC:2.3.1.157)
Gene namesi
Name:glmU
Ordered Locus Names:Tgr7_3303
OrganismiThioalkalivibrio sp. (strain HL-EbGR7)
Taxonomic identifieri396588 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeThioalkalivibrio
ProteomesiUP000002383: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459Bifunctional protein GlmUUniRule annotation
PRO_1000186508Add
BLAST

Interactioni

Subunit structurei

Homotrimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi396588.Tgr7_3303.

Structurei

3D structure databases

ProteinModelPortaliB8GRB6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 230230Pyrophosphorylase By similarity
Add
BLAST
Regioni10 – 134UDP-GlcNAc binding By similarity
Regioni80 – 812UDP-GlcNAc binding By similarity
Regioni102 – 1043UDP-GlcNAc binding By similarity
Regioni231 – 25121Linker By similarity
Add
BLAST
Regioni252 – 459208N-acetyltransferase By similarity
Add
BLAST
Regioni387 – 3882Acetyl-CoA binding By similarity

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1207.
KOiK04042.
OMAiDCVTNQD.
OrthoDBiEOG6Z6FQZ.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU.
InterProiIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 4 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.

B8GRB6-1 [UniParc]FASTAAdd to Basket

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MTTPTSILIL AAGQGTRMRS SLPKVLQPLA GRPLLSHVLD TARSLDPHRL    50
VVVYGHGGDR VREAFPEDDI RWVHQAEQRG TGHAVQVALP ETDADDRVLI 100
LYGDVPLVRG ETVRRLLAQL DEGGDLVILT AALKSPTGYG RILRDDSGRV 150
QRIVEEKDAS DSERRVNEVN TGIMAARASD FTRWLSKVTN DNAQGEFYLT 200
DCVALANTEG RRVEAVVGHE AIELMGVNDK RQLAEQERAY QRREAERLMV 250
QGVTVIDPAR LDVRGEVEAG RDVSLDINVI LQGSVKLGEG AKVGAGCVII 300
DSEIGPGAHI LPHTVIEGAV IGAGASVGPF ARIRPGTHTD SNAKIGNFVE 350
VKNARVGEGS KINHLSYVGD SELGRDVNIG AGTITCNYDG ANKHKTIIGD 400
RAFIGSNTAL VAPLTVGEGA TIGAGTTLNK DAPPGELTVA RAKAITIPGW 450
KRPVKKPKE 459
Length:459
Mass (Da):49,073
Last modified:March 3, 2009 - v1
Checksum:i6D7E892C8B1ED632
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001339 Genomic DNA. Translation: ACL74370.1.
RefSeqiYP_002515357.1. NC_011901.1.

Genome annotation databases

EnsemblBacteriaiACL74370; ACL74370; Tgr7_3303.
GeneIDi7315531.
KEGGitgr:Tgr7_3303.
PATRICi23966096. VBIThiSp19295_3262.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001339 Genomic DNA. Translation: ACL74370.1 .
RefSeqi YP_002515357.1. NC_011901.1.

3D structure databases

ProteinModelPortali B8GRB6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 396588.Tgr7_3303.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACL74370 ; ACL74370 ; Tgr7_3303 .
GeneIDi 7315531.
KEGGi tgr:Tgr7_3303.
PATRICi 23966096. VBIThiSp19295_3262.

Phylogenomic databases

eggNOGi COG1207.
KOi K04042.
OMAi DCVTNQD.
OrthoDBi EOG6Z6FQZ.

Enzyme and pathway databases

UniPathwayi UPA00113 ; UER00532 .
UPA00113 ; UER00533 .
UPA00973 .
BioCyci TSUL396588:GH5B-3355-MONOMER.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
HAMAPi MF_01631. GlmU.
InterProi IPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view ]
Pfami PF00132. Hexapep. 4 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view ]
SUPFAMi SSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsi TIGR01173. glmU. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HL-EbGR7.

Entry informationi

Entry nameiGLMU_THISH
AccessioniPrimary (citable) accession number: B8GRB6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: June 11, 2014
This is version 38 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

External Data

Dasty 3

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