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B8GRB6

- GLMU_THISH

UniProt

B8GRB6 - GLMU_THISH

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Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Thioalkalivibrio sulfidiphilus (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.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 Mg(2+) ion per subunit.UniRule annotation

Pathwayi

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. cell morphogenesis Source: UniProtKB-HAMAP
  2. cell wall organization Source: UniProtKB-KW
  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
  7. UDP-N-acetylglucosamine biosynthetic process Source: UniProtKB-UniPathway
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 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
ProteomesiUP000002383: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459Bifunctional protein GlmUPRO_1000186508Add
BLAST

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Protein-protein interaction databases

STRINGi396588.Tgr7_3303.

Structurei

3D structure databases

ProteinModelPortaliB8GRB6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 230230PyrophosphorylaseUniRule annotationAdd
BLAST
Regioni10 – 134UDP-GlcNAc bindingUniRule annotation
Regioni80 – 812UDP-GlcNAc bindingUniRule annotation
Regioni102 – 1043UDP-GlcNAc bindingUniRule annotation
Regioni231 – 25121LinkerUniRule annotationAdd
BLAST
Regioni252 – 459208N-acetyltransferaseUniRule annotationAdd
BLAST
Regioni387 – 3882Acetyl-CoA bindingUniRule annotation

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

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

« 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.
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 41 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

External Data

Dasty 3