Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B1MKE4 (B1MKE4_MYCA9) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_01631 SAAS SAAS005882

Catalytic activity

Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. HAMAP-Rule MF_01631 SAAS SAAS005882

UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine. HAMAP-Rule MF_01631 SAAS SAAS005882

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01631 SAAS SAAS005882

Pathway

Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. HAMAP-Rule MF_01631 SAAS SAAS005882

Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. HAMAP-Rule MF_01631 SAAS SAAS005882

Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. HAMAP-Rule MF_01631 SAAS SAAS005882

Subunit structure

Homotrimer By similarity. HAMAP-Rule MF_01631 SAAS SAAS005882

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01631 SAAS SAAS005882.

Sequence similarities

In the C-terminal section; belongs to the transferase hexapeptide repeat family. HAMAP-Rule MF_01631

In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family. HAMAP-Rule MF_01631

Ontologies

Keywords
   Biological processCell shape
Cell wall biogenesis/degradation HAMAP-Rule MF_01631 SAAS SAAS005882
Peptidoglycan synthesis HAMAP-Rule MF_01631 SAAS SAAS005882
   Cellular componentCytoplasm HAMAP-Rule MF_01631 SAAS SAAS005882
   DomainRepeat HAMAP-Rule MF_01631 SAAS SAAS005882
   LigandMagnesium HAMAP-Rule MF_01631 SAAS SAAS005882
Metal-binding HAMAP-Rule MF_01631 SAAS SAAS005882
   Molecular functionAcyltransferase HAMAP-Rule MF_01631 SAAS SAAS005882
Nucleotidyltransferase HAMAP-Rule MF_01631 SAAS SAAS005882
Transferase
   Technical termComplete proteome
Multifunctional enzyme HAMAP-Rule MF_01631 SAAS SAAS005882
Gene Ontology (GO)
   Biological_processUDP-N-acetylglucosamine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

cell morphogenesis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

lipid A biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

lipopolysaccharide biosynthetic process

Inferred from electronic annotation. Source: InterPro

peptidoglycan biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionUDP-N-acetylglucosamine diphosphorylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glucosamine-1-phosphate N-acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region1 – 242242Pyrophosphorylase By similarity HAMAP-Rule MF_01631
Region13 – 164UDP-GlcNAc binding By similarity HAMAP-Rule MF_01631
Region89 – 902UDP-GlcNAc binding By similarity HAMAP-Rule MF_01631
Region113 – 1153UDP-GlcNAc binding By similarity HAMAP-Rule MF_01631
Region243 – 26321Linker By similarity HAMAP-Rule MF_01631
Region264 – 482219N-acetyltransferase By similarity HAMAP-Rule MF_01631
Region398 – 3992Acetyl-CoA binding By similarity HAMAP-Rule MF_01631

Sites

Active site3751Proton acceptor By similarity HAMAP-Rule MF_01631
Metal binding1151Magnesium By similarity HAMAP-Rule MF_01631
Metal binding2401Magnesium By similarity HAMAP-Rule MF_01631
Binding site271UDP-GlcNAc By similarity HAMAP-Rule MF_01631
Binding site841UDP-GlcNAc By similarity HAMAP-Rule MF_01631
Binding site1521UDP-GlcNAc; via amide nitrogen By similarity HAMAP-Rule MF_01631
Binding site1671UDP-GlcNAc By similarity HAMAP-Rule MF_01631
Binding site1821UDP-GlcNAc By similarity HAMAP-Rule MF_01631
Binding site2401UDP-GlcNAc By similarity HAMAP-Rule MF_01631
Binding site3451Acetyl-CoA; amide nitrogen By similarity HAMAP-Rule MF_01631
Binding site3631Acetyl-CoA By similarity HAMAP-Rule MF_01631
Binding site3781Acetyl-CoA By similarity HAMAP-Rule MF_01631
Binding site3891Acetyl-CoA By similarity HAMAP-Rule MF_01631
Binding site4171Acetyl-CoA By similarity HAMAP-Rule MF_01631
Binding site4351Acetyl-CoA; via amide nitrogen By similarity HAMAP-Rule MF_01631

Sequences

Sequence LengthMass (Da)Tools
B1MKE4 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: DCDD8EB6FB512C09

FASTA48250,002
        10         20         30         40         50         60 
MPGNTAGTAV IVLAAGAGTR MCSDIPKVLH TLGGRSMLAH AVYAAASVNP EHLVIVLGHE 

        70         80         90        100        110        120 
RERIATAVDI LAESLGRRIE IAVQEQQLGT GHAVACGLQA LPAGFAGTVV VTSGDIPLLD 

       130        140        150        160        170        180 
GGTLAGLIGS HTSEPAAATL LTTTLTDPTG YGRILRTQDR EVIAIVEQTD ATESQRAIGE 

       190        200        210        220        230        240 
VNAGVYAFDI EPLHAALSRL RSNNAQHELY LTDAVSIIRE SGKVVHANHV DDSALVAGVN 

       250        260        270        280        290        300 
DRVQLSELGA ELNRRIIRHH QRNGVTIIDP SSTWIDVDVH IGQDATIAPG TQLHSATVIG 

       310        320        330        340        350        360 
GHCHIGPDTT LIDVTVGDSA TVIRTHGQGS TIGARSVIGP FTYLRPGTVT GESAKLGAFV 

       370        380        390        400        410        420 
EVKNSTVGRG TKVPHLTYVG DADIGEHSNI GASSVFVNYD GETKRRTVIG SHVKTGSDTM 

       430        440        450        460        470        480 
FVAPVTVGDG AYTGAGTVIR EDVPPGALAV SAGRQRNIEG WVAQKRPGSD AAKAAEEASK 


GS 

« Hide

References

[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 (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19977 / DSM 44196.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU458896 Genomic DNA. Translation: CAM61236.1.
RefSeqYP_001701890.1. NC_010397.1.

3D structure databases

ProteinModelPortalB1MKE4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561007.MAB_1148c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM61236; CAM61236; MAB_1148c.
GeneID5963672.
KEGGmab:MAB_1148c.
PATRIC17973977. VBIMycAbs55940_1185.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1207.
HOGENOMHOG000283476.
KOK04042.
OMANKHKTII.
OrthoDBEOG6Z6FQZ.
ProtClustDBPRK14352.

Enzyme and pathway databases

BioCycMABS561007:GJTG-1150-MONOMER.
UniPathwayUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Family and domain databases

HAMAPMF_01631. GlmU.
InterProIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep_transf.
IPR025877. MobA-like_NTP_Trfase_dom.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamPF00132. Hexapep. 3 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMSSF51161. SSF51161. 1 hit.
TIGRFAMsTIGR01173. glmU. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB1MKE4_MYCA9
AccessionPrimary (citable) accession number: B1MKE4
Entry history
Integrated into UniProtKB/TrEMBL: April 29, 2008
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)