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Q577Y2

- GLMU_BRUAB

UniProt

Q577Y2 - GLMU_BRUAB

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Protein
Bifunctional protein GlmU
Gene
glmU, BruAb2_0641
Organism
Brucella abortus biovar 1 (strain 9-941)
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 sitei25 – 251UDP-GlcNAc By similarity
Binding sitei78 – 781UDP-GlcNAc By similarity
Metal bindingi108 – 1081Magnesium By similarity
Binding sitei144 – 1441UDP-GlcNAc; via amide nitrogen By similarity
Binding sitei158 – 1581UDP-GlcNAc By similarity
Binding sitei173 – 1731UDP-GlcNAc By similarity
Metal bindingi230 – 2301Magnesium By similarity
Binding sitei230 – 2301UDP-GlcNAc By similarity
Binding sitei319 – 3191Acetyl-CoA; amide nitrogen By similarity
Binding sitei337 – 3371Acetyl-CoA By similarity
Active sitei349 – 3491Proton acceptor By similarity
Binding sitei352 – 3521Acetyl-CoA By similarity
Binding sitei363 – 3631Acetyl-CoA By similarity
Binding sitei391 – 3911Acetyl-CoA By similarity
Binding sitei409 – 4091Acetyl-CoA; via amide nitrogen By similarity
Binding sitei426 – 4261Acetyl-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
Complete GO annotation...

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

BioCyciBABO262698:GJC2-2856-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:BruAb2_0641
OrganismiBrucella abortus biovar 1 (strain 9-941)
Taxonomic identifieri262698 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000000540: Chromosome II

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 – 454454Bifunctional protein GlmUUniRule annotation
PRO_0000233744Add
BLAST

Interactioni

Subunit structurei

Homotrimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi262698.BruAb2_0641.

Structurei

3D structure databases

ProteinModelPortaliQ577Y2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 232232Pyrophosphorylase By similarity
Add
BLAST
Regioni11 – 144UDP-GlcNAc binding By similarity
Regioni83 – 842UDP-GlcNAc binding By similarity
Regioni233 – 25321Linker By similarity
Add
BLAST
Regioni254 – 454201N-acetyltransferase By similarity
Add
BLAST
Regioni372 – 3732Acetyl-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.
OMAiIGERAYI.
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.

Q577Y2-1 [UniParc]FASTAAdd to Basket

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MTDRTCLSIV LAAGEGTRMK SNLPKVLHRV AGLPLVCHVV NAVRGTGKSD    50
VALVVGRGAE DVRSAVEKIA GPVSAFEQKE RLGTAHAVLA AHEAIARGYD 100
DLLIVFGDTP LIEAQSLLAA RERLAQGADL VVIGFRPASP HGYGRLIEEG 150
GQLVAIIEEK EATDEQKKIG FCNGGLMALR GQHALALLDA VGNDNAKGEY 200
YLTDIVAIAH GKGLNVTAIE VPVDNVIGIN NRAELAEAET IWQNRKRREL 250
MLSGVTLIAP ETVFFSYDTV IEPDVVIEPN VFFGPSVHVA SGALIHSFSH 300
LEGAQVGEKA EIGPFARLRP GADLAEKSKV GNFCEVKNAK VGKGAKINHL 350
AYIGDAVIGA SSNIGAGTIT CNYDGYNKFK TIIGDNAFIG SNSSLVAPVE 400
IGDNAYIASG SVITADVPAD ALALGRARQE TKEGRAKILR EKYAAIKAAK 450
SVSK 454
Length:454
Mass (Da):47,886
Last modified:May 10, 2005 - v1
Checksum:i98D0D7E9AA0EAF2C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017224 Genomic DNA. Translation: AAX76052.1.
RefSeqiYP_223413.1. NC_006933.1.

Genome annotation databases

EnsemblBacteriaiAAX76052; AAX76052; BruAb2_0641.
GeneIDi3342275.
KEGGibmb:BruAb2_0641.
PATRICi17827563. VBIBruAbo15061_2955.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017224 Genomic DNA. Translation: AAX76052.1 .
RefSeqi YP_223413.1. NC_006933.1.

3D structure databases

ProteinModelPortali Q577Y2.
ModBasei Search...

Protein-protein interaction databases

STRINGi 262698.BruAb2_0641.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAX76052 ; AAX76052 ; BruAb2_0641 .
GeneIDi 3342275.
KEGGi bmb:BruAb2_0641.
PATRICi 17827563. VBIBruAbo15061_2955.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00113 ; UER00532 .
UPA00113 ; UER00533 .
UPA00973 .
BioCyci BABO262698:GJC2-2856-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. "Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
    Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
    J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 9-941.

Entry informationi

Entry nameiGLMU_BRUAB
AccessioniPrimary (citable) accession number: Q577Y2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 10, 2005
Last modified: June 11, 2014
This is version 65 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. Brucella abortus strain 9-941
    Brucella abortus (strain 9-941): 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

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