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A5WHT0

- GLMU_PSYWF

UniProt

A5WHT0 - GLMU_PSYWF

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Protein
Bifunctional protein GlmU
Gene
glmU, PsycPRwf_2281
Organism
Psychrobacter sp. (strain PRwf-1)
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 sitei138 – 1381UDP-GlcNAc; via amide nitrogen By similarity
Binding sitei153 – 1531UDP-GlcNAc By similarity
Binding sitei168 – 1681UDP-GlcNAc By similarity
Metal bindingi226 – 2261Magnesium By similarity
Binding sitei226 – 2261UDP-GlcNAc By similarity
Binding sitei332 – 3321Acetyl-CoA; amide nitrogen By similarity
Binding sitei350 – 3501Acetyl-CoA By similarity
Active sitei362 – 3621Proton acceptor By similarity
Binding sitei365 – 3651Acetyl-CoA By similarity
Binding sitei376 – 3761Acetyl-CoA By similarity
Binding sitei422 – 4221Acetyl-CoA; via amide nitrogen By similarity
Binding sitei439 – 4391Acetyl-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

BioCyciPPRW349106:GHZF-2351-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:PsycPRwf_2281
OrganismiPsychrobacter sp. (strain PRwf-1)
Taxonomic identifieri349106 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
ProteomesiUP000001993: 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 – 455455Bifunctional protein GlmUUniRule annotation
PRO_1000073649Add
BLAST

Interactioni

Subunit structurei

Homotrimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi349106.PsycPRwf_2281.

Structurei

3D structure databases

ProteinModelPortaliA5WHT0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 228228Pyrophosphorylase By similarity
Add
BLAST
Regioni10 – 134UDP-GlcNAc binding By similarity
Regioni80 – 812UDP-GlcNAc binding By similarity
Regioni102 – 1043UDP-GlcNAc binding By similarity
Regioni229 – 24921Linker By similarity
Add
BLAST
Regioni250 – 455206N-acetyltransferase By similarity
Add
BLAST
Regioni385 – 3862Acetyl-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.
HOGENOMiHOG000283476.
KOiK04042.
OMAiDCVTNQD.
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. 4 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.

A5WHT0-1 [UniParc]FASTAAdd to Basket

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MNNTLTTIIL AAGKGTRMQS AKPKVLQILA DKPLLAHVLD TCQSISVDKT    50
IVVYGFGGDQ VQQAMTDYSL TWVEQTEQLG TGHAVKVALD ELPSTGKSLI 100
LYGDVPLVSA ETLSRLKQAN VQGMSMLTLT VDNPFGLGRI KRDEQGNITA 150
IVEQKDASEQ EQAIREINSG IYCVDNALLH QYLPNLSNDN AQQEYYLTDI 200
VKMAVADGIA IAAIEPDYEF EIEGVNNRQQ LAQLERKWQA KLVEDLQVQG 250
VQFADPNRVD IRGEVSVGQD VFVDINVVFK GKVSLGNNVT IEAGCMIKDS 300
QIGDNVHIKP YCVFDDAQVA QGATIGPFAH LRPQTVLEKN TRLGNFVEIK 350
KSRIGEGSKV NHLSYVGDAQ IGAGVNFGAG AITCNYDGVN KHQTIVGDNA 400
FIGTNTSLVA PVTIGQTATI GAGSVITKNV EDNALAIGRG RQVQKDNYQR 450
PEKKK 455
Length:455
Mass (Da):49,296
Last modified:July 10, 2007 - v1
Checksum:i6074BD4D1C91F6F6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000713 Genomic DNA. Translation: ABQ95221.1.
RefSeqiWP_011961493.1. NC_009524.1.
YP_001281171.1. NC_009524.1.

Genome annotation databases

EnsemblBacteriaiABQ95221; ABQ95221; PsycPRwf_2281.
GeneIDi5205575.
KEGGiprw:PsycPRwf_2281.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000713 Genomic DNA. Translation: ABQ95221.1 .
RefSeqi WP_011961493.1. NC_009524.1.
YP_001281171.1. NC_009524.1.

3D structure databases

ProteinModelPortali A5WHT0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 349106.PsycPRwf_2281.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABQ95221 ; ABQ95221 ; PsycPRwf_2281 .
GeneIDi 5205575.
KEGGi prw:PsycPRwf_2281.

Phylogenomic databases

eggNOGi COG1207.
HOGENOMi HOG000283476.
KOi K04042.
OMAi DCVTNQD.
OrthoDBi EOG6Z6FQZ.

Enzyme and pathway databases

UniPathwayi UPA00113 ; UER00532 .
UPA00113 ; UER00533 .
UPA00973 .
BioCyci PPRW349106:GHZF-2351-MONOMER.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
HAMAPi MF_01631. GlmU.
InterProi IPR005882. 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 ]
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.
PROSITEi PS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

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

Entry informationi

Entry nameiGLMU_PSYWF
AccessioniPrimary (citable) accession number: A5WHT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: July 10, 2007
Last modified: September 3, 2014
This is version 54 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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