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Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Mycobacterium abscessus (strain ATCC 19977 / DSM 44196)
Status
Unreviewed-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 annotationSAAS annotation

Catalytic activityi

Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate.UniRule annotationSAAS annotation
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine.UniRule annotationSAAS annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotationSAAS annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotationSAAS annotation
  • Mg2+Note: Binds 1 Mg2+ ion per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei27 – 271UDP-GlcNAcUniRule annotation
Binding sitei84 – 841UDP-GlcNAcUniRule annotation
Metal bindingi115 – 1151MagnesiumUniRule annotation
Binding sitei152 – 1521UDP-GlcNAc; via amide nitrogenUniRule annotation
Binding sitei167 – 1671UDP-GlcNAcUniRule annotation
Binding sitei182 – 1821UDP-GlcNAcUniRule annotation
Metal bindingi240 – 2401MagnesiumUniRule annotation
Binding sitei240 – 2401UDP-GlcNAcUniRule annotation
Binding sitei345 – 3451Acetyl-CoA; amide nitrogenUniRule annotation
Binding sitei363 – 3631Acetyl-CoAUniRule annotation
Active sitei375 – 3751Proton acceptorUniRule annotation
Binding sitei378 – 3781Acetyl-CoAUniRule annotation
Binding sitei389 – 3891Acetyl-CoAUniRule annotation
Binding sitei417 – 4171Acetyl-CoAUniRule annotation
Binding sitei435 – 4351Acetyl-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

AcyltransferaseUniRule annotationSAAS annotation, NucleotidyltransferaseUniRule annotationSAAS annotation, Transferase

Keywords - Biological processi

Cell shape, Cell wall biogenesis/degradationUniRule annotationSAAS annotation, Peptidoglycan synthesisUniRule annotationSAAS annotation

Keywords - Ligandi

MagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciMABS36809-WGS:GSQO-1150-MONOMER.
MABS561007:GJTG-1150-MONOMER.
UniPathwayiUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional protein GlmUUniRule annotationSAAS annotation
Gene namesi
Name:glmUUniRule annotation
Ordered Locus Names:MAB_1148cImported
OrganismiMycobacterium abscessus (strain ATCC 19977 / DSM 44196)Imported
Taxonomic identifieri561007 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium abscessus
ProteomesiUP000007137 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Interactioni

Subunit structurei

Homotrimer.UniRule annotationSAAS annotation

Protein-protein interaction databases

STRINGi561007.MAB_1148c.

Structurei

3D structure databases

ProteinModelPortaliB1MKE4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 242242PyrophosphorylaseUniRule annotationAdd
BLAST
Regioni13 – 164UDP-GlcNAc bindingUniRule annotation
Regioni89 – 902UDP-GlcNAc bindingUniRule annotation
Regioni113 – 1153UDP-GlcNAc bindingUniRule annotation
Regioni243 – 26321LinkerUniRule annotationAdd
BLAST
Regioni264 – 482219N-acetyltransferaseUniRule annotationAdd
BLAST
Regioni398 – 3992Acetyl-CoA bindingUniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

RepeatUniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiCOG1207.
HOGENOMiHOG000283476.
OMAiFAHARPK.
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. 3 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.

B1MKE4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGNTAGTAV IVLAAGAGTR MCSDIPKVLH TLGGRSMLAH AVYAAASVNP
60 70 80 90 100
EHLVIVLGHE RERIATAVDI LAESLGRRIE IAVQEQQLGT GHAVACGLQA
110 120 130 140 150
LPAGFAGTVV VTSGDIPLLD GGTLAGLIGS HTSEPAAATL LTTTLTDPTG
160 170 180 190 200
YGRILRTQDR EVIAIVEQTD ATESQRAIGE VNAGVYAFDI EPLHAALSRL
210 220 230 240 250
RSNNAQHELY LTDAVSIIRE SGKVVHANHV DDSALVAGVN DRVQLSELGA
260 270 280 290 300
ELNRRIIRHH QRNGVTIIDP SSTWIDVDVH IGQDATIAPG TQLHSATVIG
310 320 330 340 350
GHCHIGPDTT LIDVTVGDSA TVIRTHGQGS TIGARSVIGP FTYLRPGTVT
360 370 380 390 400
GESAKLGAFV EVKNSTVGRG TKVPHLTYVG DADIGEHSNI GASSVFVNYD
410 420 430 440 450
GETKRRTVIG SHVKTGSDTM FVAPVTVGDG AYTGAGTVIR EDVPPGALAV
460 470 480
SAGRQRNIEG WVAQKRPGSD AAKAAEEASK GS
Length:482
Mass (Da):50,002
Last modified:April 28, 2008 - v1
Checksum:iDCDD8EB6FB512C09
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU458896 Genomic DNA. Translation: CAM61236.1.

Genome annotation databases

EnsemblBacteriaiCAM61236; CAM61236; MAB_1148c.
PATRICi17973977. VBIMycAbs55940_1185.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU458896 Genomic DNA. Translation: CAM61236.1.

3D structure databases

ProteinModelPortaliB1MKE4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi561007.MAB_1148c.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAM61236; CAM61236; MAB_1148c.
PATRICi17973977. VBIMycAbs55940_1185.

Phylogenomic databases

eggNOGiCOG1207.
HOGENOMiHOG000283476.
OMAiFAHARPK.
OrthoDBiEOG6Z6FQZ.

Enzyme and pathway databases

UniPathwayiUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.
BioCyciMABS36809-WGS:GSQO-1150-MONOMER.
MABS561007:GJTG-1150-MONOMER.

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. 3 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR01173. glmU. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Acquisition of foreign virulence genes by the cystic fibrosis pathogen Mycobacterium abscessus."
    Genoscope
    Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L., Gaillard J.L.
    Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 19977 / DSM 44196Imported.

Entry informationi

Entry nameiB1MKE4_MYCA9
AccessioniPrimary (citable) accession number: B1MKE4
Entry historyi
Integrated into UniProtKB/TrEMBL: April 28, 2008
Last sequence update: April 28, 2008
Last modified: March 31, 2015
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzymeUniRule annotationSAAS annotation, Reference proteomeImported

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.