CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004210
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Bifunctional protein GlmU 
Protein Synonyms/Alias
 UDP-N-acetylglucosamine pyrophosphorylase; N-acetylglucosamine-1-phosphate uridyltransferase; Glucosamine-1-phosphate N-acetyltransferase 
Gene Name
 glmU 
Gene Synonyms/Alias
 gcaD; tms; tms-26; BSU00500 
Created Date
 July 27, 2013 
Organism
 Bacillus subtilis (strain 168) 
NCBI Taxa ID
 224308 
Lysine Modification
Position
Peptide
Type
References
241SQAEQFMKERINKRHacetylation[1]
Reference
 [1] The acetylproteome of Gram-positive model bacterium Bacillus subtilis.
 Kim D, Yu BJ, Kim JA, Lee YJ, Choi SG, Kang S, Pan JG.
 Proteomics. 2013 May;13(10-11):1726-36. [PMID: 23468065
Functional Description
 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). 
Sequence Annotation
 REGION 1 230 Pyrophosphorylase (By similarity).
 REGION 9 12 UDP-GlcNAc binding (By similarity).
 REGION 78 79 UDP-GlcNAc binding (By similarity).
 REGION 231 251 Linker (By similarity).
 REGION 252 456 N-acetyltransferase (By similarity).
 REGION 386 387 Acetyl-CoA binding (By similarity).
 ACT_SITE 363 363 Proton acceptor (By similarity).
 METAL 103 103 Magnesium (By similarity).
 METAL 228 228 Magnesium (By similarity).
 BINDING 23 23 UDP-GlcNAc (By similarity).
 BINDING 73 73 UDP-GlcNAc (By similarity).
 BINDING 140 140 UDP-GlcNAc; via amide nitrogen (By
 BINDING 155 155 UDP-GlcNAc (By similarity).
 BINDING 170 170 UDP-GlcNAc (By similarity).
 BINDING 228 228 UDP-GlcNAc (By similarity).
 BINDING 333 333 Acetyl-CoA; amide nitrogen (By
 BINDING 351 351 Acetyl-CoA (By similarity).
 BINDING 366 366 Acetyl-CoA (By similarity).
 BINDING 377 377 Acetyl-CoA (By similarity).
 BINDING 423 423 Acetyl-CoA; via amide nitrogen (By
 BINDING 440 440 Acetyl-CoA (By similarity).  
Keyword
 Acyltransferase; Cell shape; Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; Magnesium; Metal-binding; Multifunctional enzyme; Nucleotidyltransferase; Peptidoglycan synthesis; Reference proteome; Repeat; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 456 AA 
Protein Sequence
MDKRFAVVLA AGQGTRMKSK LYKVLHPVCG KPMVEHVVDE ALKLSLSKLV TIVGHGAEEV 60
KKQLGDKSEY RVQAKQLGTA HAVKQAQPFL ADEKGVTIVI CGDTPLLTAE TMEQMLKEHT 120
QREAKRTILT AVAEDPTGYG RIIRSENGAV QKIVEHKDAS EEERLVTEIN TGTYCFDNEA 180
LFRAIDQVSN DNAQGEYYLP DVIEILKNEG ETVAAYQTGN FQETLGVNDR VALSQAEQFM 240
KERINKRHMQ NGVTLIDPMN TYISPDAVIG SDTVIYPGTV IKGEVQIGED TIIGPHTEIM 300
NSAIGSRTVI KQSVVNHSKV GNDVNIGPFA HIRPDSVIGN EVKIGNFVEI KKTQFGDRSK 360
ASHLSYVGDA EVGTDVNLGC GSITVNYDGK NKYLTKIEDG AFIGCNSNLV APVTVGEGAY 420
VAAGSTVTED VPGKALAIAR ARQVNKDDYV KNIHKK 456 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:HAMAP.
 GO:0000287; F:magnesium ion binding; IEA:HAMAP.
 GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:HAMAP.
 GO:0000902; P:cell morphogenesis; IEA:HAMAP.
 GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
 GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
 GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
 GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR005882; Bifunctional_GlmU.
 IPR001451; Hexapep_transf.
 IPR018357; Hexapep_transf_CS.
 IPR005835; NTP_transferase.
 IPR011004; Trimer_LpxA-like. 
Pfam
 PF00132; Hexapep
 PF00483; NTP_transferase 
SMART
  
PROSITE
 PS00101; HEXAPEP_TRANSFERASES 
PRINTS