Bifunctional protein glmU - Bacillus subtilis

Names and origin

Protein names

Recommended name:
    Bifunctional protein glmU
Including the following 2 domains:
    1- Recommended name:
            UDP-N-acetylglucosamine pyrophosphorylase
              EC=2.7.7.23
        Alternative name(s):
            N-acetylglucosamine-1-phosphate uridyltransferase
    2- Recommended name:
            Glucosamine-1-phosphate N-acetyltransferase
              EC=2.3.1.157

Gene names

Name:	glmU
Synonyms:	gcaD, tms, tms-26
Ordered Locus Names:	BSU00500

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length	456 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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General annotation (Comments)

Function	Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-GlcNAc. Responsible for the acetylation of Glc-N-1-P to give GlcNAc-1-P and for the uridyl transfer from UTP to GlcNAc-1-P which produces UDP-GlcNAc By similarity.
Catalytic activity	Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. HAMAP MF_01631 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-D-glucosamine. HAMAP MF_01631
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	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 MF_01631 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. Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. HAMAP MF_01631
Subcellular location	Cytoplasm By similarity.
Sequence similarities	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.

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Ontologies

Keywords
Biological process	Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Domain	Repeat
Ligand	Magnesium Metal-binding
Molecular function	Acyltransferase Nucleotidyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	cell morphogenesis Inferred from electronic annotation. Source: HAMAP cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: InterPro peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	UDP-N-acetylglucosamine diphosphorylase activity Inferred from electronic annotation. Source: HAMAP glucosamine-1-phosphate N-acetyltransferase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 456

456

Bifunctional protein glmU HAMAP MF_01631

PRO_0000068706

Regions

Region

1 – 230

230

Pyrophosphorylase By similarity

Region

9 – 12

4

Substrate binding By similarity

Region

78 – 79

2

Substrate binding By similarity

Region

231 – 251

21

Linker By similarity

Region

252 – 456

205

N-acetyltransferase By similarity

Sites

Active site

363

1

Proton acceptor By similarity

Metal binding

103

1

Magnesium By similarity

Metal binding

228

1

Magnesium By similarity

Binding site

73

1

Substrate By similarity

Binding site

140

1

Substrate; via amide nitrogen By similarity

Binding site

155

1

Substrate By similarity

Binding site

170

1

Substrate By similarity

Binding site

387

1

Acetyl-CoA By similarity

Binding site

423

1

Acetyl-CoA; via amide nitrogen By similarity

Binding site

440

1

Acetyl-CoA By similarity

Experimental info

Sequence conflict

19

1

S → L Ref.4

Sequence conflict

71 – 72

2

RV → AL in BAA05285. Ref.2

Sequence conflict

71 – 72

2

RV → AL in CAB11826. Ref.2

Sequence conflict

126

1

R → A in BAA05285. Ref.2

Sequence conflict

126

1

R → A in CAB11826. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P14192-1 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 6D65E0A05D5E9261
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FASTA

456

49,610

        10         20         30         40         50         60 
MDKRFAVVLA AGQGTRMKSK LYKVLHPVCG KPMVEHVVDE ALKLSLSKLV TIVGHGAEEV 

        70         80         90        100        110        120 
KKQLGDKSEY RVQAKQLGTA HAVKQAQPFL ADEKGVTIVI CGDTPLLTAE TMEQMLKEHT 

       130        140        150        160        170        180 
QREAKRTILT AVAEDPTGYG RIIRSENGAV QKIVEHKDAS EEERLVTEIN TGTYCFDNEA 

       190        200        210        220        230        240 
LFRAIDQVSN DNAQGEYYLP DVIEILKNEG ETVAAYQTGN FQETLGVNDR VALSQAEQFM 

       250        260        270        280        290        300 
KERINKRHMQ NGVTLIDPMN TYISPDAVIG SDTVIYPGTV IKGEVQIGED TIIGPHTEIM 

       310        320        330        340        350        360 
NSAIGSRTVI KQSVVNHSKV GNDVNIGPFA HIRPDSVIGN EVKIGNFVEI KKTQFGDRSK 

       370        380        390        400        410        420 
ASHLSYVGDA EVGTDVNLGC GSITVNYDGK NKYLTKIEDG AFIGCNSNLV APVTVGEGAY 

       430        440        450 
VAAGSTVTED VPGKALAIAR ARQVNKDDYV KNIHKK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of the tms and prs genes of Bacillus subtilis." Nilsson D., Hove-Jensen B., Arnvig K. Mol. Gen. Genet. 218:565-571(1989) [PubMed: 2555671] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin." Ogasawara N., Nakai S., Yoshikawa H. DNA Res. 1:1-14(1994) [PubMed: 7584024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"Nucleotide sequences that signal the initiation of transcription and translation in Bacillus subtilis." Moran C.P. Jr., Lang N., LeGrice S.F.J., Lee G., Stephens M., Sonenshein A.L., Pero J., Losick R. Mol. Gen. Genet. 186:339-346(1982) [PubMed: 6181373] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21. Strain: 168.
[5]	"spoVG sequence of Bacillus megaterium and Bacillus subtilis." Hudspeth D.S.S., Vary P.S. Biochim. Biophys. Acta 1130:229-231(1992) [PubMed: 1373326] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21. Strain: 168.

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Cross-references

Sequence databases
	X16518 Genomic DNA. Translation: CAA34522.1. D26185 Genomic DNA. Translation: BAA05285.1. AL009126 Genomic DNA. Translation: CAB11826.1. J01550 Genomic DNA. Translation: AAA22854.1. X62378 Genomic DNA. Translation: CAA44243.1.
PIR	S66080.
RefSeq	NP_387931.1.
3D structure databases
HSSP	HSSP built from PDB template 1HM0 based on UniProtKB Q97R46.
ModBase	Search...
Genome annotation databases
GeneID	936139.
GenomeReviews	Gene locus BSU00500 in contig AL009126_GR.
KEGG	bsu:BSU00500.
Organism-specific databases
SubtiList	BG10113. gcaD. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P14192.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU0050-MON.
BRENDA	2.3.1.157. 150. 2.7.7.23. 150.
Family and domain databases
HAMAP	MF_01631. [Tree]
InterPro	IPR001451. Hexapep_transf. IPR018357. Hexapep_transf_CS. IPR005835. NTP_transferase. IPR005882. UDP_GlcNAc_PyrPase. [Graphical view]
Pfam	PF00132. Hexapep. 5 hits. PF00483. NTP_transferase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01173. glmU. 1 hit.
PROSITE	PS00101. HEXAPEP_TRANSFERASES. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

GLMU_BACSU

Accession

Primary (citable) accession number: P14192
Secondary accession number(s): Q45684

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	September 22, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents