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Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei25 – 251UDP-GlcNAcUniRule annotation
Binding sitei76 – 761UDP-GlcNAcUniRule annotation
Metal bindingi105 – 1051MagnesiumUniRule annotation
Binding sitei140 – 1401UDP-GlcNAc; via amide nitrogenUniRule annotation
Binding sitei154 – 1541UDP-GlcNAcUniRule annotation
Metal bindingi227 – 2271MagnesiumUniRule annotation
Binding sitei227 – 2271UDP-GlcNAcUniRule annotation
Binding sitei333 – 3331Acetyl-CoA; amide nitrogenUniRule annotation
Binding sitei351 – 3511Acetyl-CoAUniRule annotation
Active sitei363 – 3631Proton acceptorUniRule annotation
Binding sitei366 – 3661Acetyl-CoAUniRule annotation
Binding sitei377 – 3771Acetyl-CoAUniRule annotation
Binding sitei405 – 4051Acetyl-CoAUniRule annotation
Binding sitei423 – 4231Acetyl-CoA; via amide nitrogenUniRule 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

BioCyciBAPH107806:GBZJ-27-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:BU027
OrganismiBuchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)
Taxonomic identifieri107806 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
ProteomesiUP000001806: Chromosome

Subcellular locationi

Cytoplasm 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 GlmUPRO_0000068698Add
BLAST

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP57139.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 229229PyrophosphorylaseUniRule annotationAdd
BLAST
Regioni11 – 144UDP-GlcNAc bindingUniRule annotation
Regioni81 – 822UDP-GlcNAc bindingUniRule annotation
Regioni103 – 1053UDP-GlcNAc bindingUniRule annotation
Regioni230 – 25021LinkerUniRule annotationAdd
BLAST
Regioni251 – 459209N-acetyltransferaseUniRule annotationAdd
BLAST
Regioni386 – 3872Acetyl-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.
HOGENOMiHOG000283476.
KOiK04042.
OMAiFAHARPK.
OrthoDBiEOG6Z6FQZ.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU.
InterProiIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR025877. MobA-like_NTP_Trfase_dom.
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.
PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P57139-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLTQEIIIVI LAAGKGTRMK SNHPKVLHFL GGKTILEHVI ETAQSIKPKK
60 70 80 90 100
IILVYSDQKK PVLSNIYNIP IQWIIQKKPQ GTGHAILLAI KKISDNTEIL
110 120 130 140 150
VLYGDVPFIS PVSIKKLQKS KKQSKISLLT AKVKNPNGYG RILRKKGKVI
160 170 180 190 200
SIIEDQDASN EQKNIKEIYS GIFIAQSKDL TRWLKKIDKK NEKQEFYATD
210 220 230 240 250
IIALAHLEGS FIKTIEPLNY EEILGINNKL QLSNLEKIFQ KKQINKLLIN
260 270 280 290 300
GVTIKDPSHF IFRGTLQHGQ NVEIDTGVIL ENNVILGDDV KIGPGCIIRN
310 320 330 340 350
SSIDSNTNIQ AYTIIENSKI GKGCIIGPFA HLRSNTLLDR NVHIGNFVET
360 370 380 390 400
KDTFIKNESK VKHLSYLGNS EIGSKVNIGA GSITCNYDGA NKFKTIIGDN
410 420 430 440 450
VLVGSNTQLI APIKIAKNTT IAAGTTVTKD VNTPCLVYNT KEQKYKKNWM

RSKKIIKKN
Length:459
Mass (Da):51,182
Last modified:December 1, 2000 - v1
Checksum:iC26CAFBD3852AAF4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000003 Genomic DNA. Translation: BAB12754.1.
RefSeqiNP_239868.1. NC_002528.1.

Genome annotation databases

EnsemblBacteriaiBAB12754; BAB12754; BAB12754.
GeneIDi1109535.
KEGGibuc:BU027.
PATRICi21243558. VBIBucAph127364_0039.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000003 Genomic DNA. Translation: BAB12754.1.
RefSeqiNP_239868.1. NC_002528.1.

3D structure databases

ProteinModelPortaliP57139.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB12754; BAB12754; BAB12754.
GeneIDi1109535.
KEGGibuc:BU027.
PATRICi21243558. VBIBucAph127364_0039.

Phylogenomic databases

eggNOGiCOG1207.
HOGENOMiHOG000283476.
KOiK04042.
OMAiFAHARPK.
OrthoDBiEOG6Z6FQZ.

Enzyme and pathway databases

UniPathwayiUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.
BioCyciBAPH107806:GBZJ-27-MONOMER.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU.
InterProiIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR025877. MobA-like_NTP_Trfase_dom.
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.
PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."
    Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.
    Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: APS.

Entry informationi

Entry nameiGLMU_BUCAI
AccessioniPrimary (citable) accession number: P57139
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: January 7, 2015
This is version 96 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. Buchnera aphidicola (subsp. Acyrthosiphon pisum)
    Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.