MYCTU:GLMU

Species (Taxon ID)	Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). (83332)
Gene Name(s)	glmU (ECO:0000255 with HAMAP-Rule:MF_01631)
Protein Name(s)	Bifunctional protein GlmU (ECO:0000255 with HAMAP-Rule:MF_01631) UDP-N-acetylglucosamine pyrophosphorylase (ECO:0000255 with HAMAP-Rule:MF_01631) N-acetylglucosamine-1-phosphate uridyltransferase (ECO:0000255 with HAMAP-Rule:MF_01631) Glucosamine-1-phosphate N-acetyltransferase (ECO:0000255 with HAMAP-Rule:MF_01631)
External Links
UniProt	P9WMN3
EMBL	AL123456
PIR	E70622
RefSeq	NP_215534.1 WP_003405267.1
PDB	2QKX 3D8V 3D98 3DJ4 3FOQ 3SPT 3ST8 4G3Q 4G3S 4G87 4HCQ
PDBsum	2QKX 3D8V 3D98 3DJ4 3FOQ 3SPT 3ST8 4G3Q 4G3S 4G87 4HCQ
ProteinModelPortal	P9WMN3
SMR	P9WMN3
IntAct	P9WMN3
STRING	83332.Rv1018c
ChEMBL	CHEMBL1293297
PaxDb	P9WMN3
EnsemblBacteria	CCP43768
GeneID	886069
KEGG	mtu:Rv1018c
TubercuList	Rv1018c
eggNOG	ENOG4105CAJ COG1207
KO	K04042
OMA	FAHARPK
PhylomeDB	P9WMN3
UniPathway	UPA00113 UPA00113 UPA00973
PRO	PR:P9WMN3
Proteomes	UP000001584
GO	GO:0005737 GO:0019134 GO:0000287 GO:0003977 GO:0070569 GO:0044650 GO:0000902 GO:0071555 GO:0035635 GO:0040007 GO:0009245 GO:0009103 GO:0009252 GO:0008360 GO:0006048
Gene3D	3.90.550.10
HAMAP	MF_01631
InterPro	IPR005882 IPR001451 IPR025877 IPR029044 IPR011004
Pfam	PF00132 PF12804
SUPFAM	SSF51161 SSF53448
TIGRFAMs	TIGR01173

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:0035635	entry of bacterium into host cell	PMID:26829648^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000775)	Seeded From UniProt	complete
involved_in	GO:0044650	adhesion of symbiont to host cell	PMID:26829648^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000775)	Seeded From UniProt	complete
enables	GO:0070569	uridylyltransferase activity	PMID:18573680^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006048	UDP-N-acetylglucosamine biosynthetic process	PMID:18573680^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019134	glucosamine-1-phosphate N-acetyltransferase activity	PMID:19237750^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0019134	glucosamine-1-phosphate N-acetyltransferase activity	PMID:19121323^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0019134	glucosamine-1-phosphate N-acetyltransferase activity	PMID:18573680^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003977	UDP-N-acetylglucosamine diphosphorylase activity	PMID:19237750^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003977	UDP-N-acetylglucosamine diphosphorylase activity	PMID:19121323^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:19237750^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005882	F		Seeded From UniProt	complete
involved_in	GO:0000902	cell morphogenesis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005882	P		Seeded From UniProt	complete
enables	GO:0003977	UDP-N-acetylglucosamine diphosphorylase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005882 InterPro:IPR038009	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005882	C		Seeded From UniProt	complete
involved_in	GO:0006048	UDP-N-acetylglucosamine biosynthetic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR038009	P		Seeded From UniProt	complete
involved_in	GO:0009103	lipopolysaccharide biosynthetic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005882	P		Seeded From UniProt	complete
involved_in	GO:0009252	peptidoglycan biosynthetic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005882	P		Seeded From UniProt	complete
enables	GO:0019134	glucosamine-1-phosphate N-acetyltransferase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005882 InterPro:IPR038009	F		Seeded From UniProt	complete
enables	GO:0003977	UDP-N-acetylglucosamine diphosphorylase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.7.23	F		Seeded From UniProt	complete
enables	GO:0019134	glucosamine-1-phosphate N-acetyltransferase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.3.1.157	F		Seeded From UniProt	complete
involved_in	GO:0000902	cell morphogenesis	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000081051	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000081051	C		Seeded From UniProt	complete
enables	GO:0003977	UDP-N-acetylglucosamine diphosphorylase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000081051	F		Seeded From UniProt	complete
enables	GO:0019134	glucosamine-1-phosphate N-acetyltransferase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000081051	F		Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000081051	F		Seeded From UniProt	complete
involved_in	GO:0009252	peptidoglycan biosynthetic process	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000081051	P		Seeded From UniProt	complete
enables	GO:0016746	transferase activity, transferring acyl groups	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0012	F		Seeded From UniProt	complete
involved_in	GO:0009252	peptidoglycan biosynthetic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0573	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
involved_in	GO:0008360	regulation of cell shape	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0133	P		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
enables	GO:0016779	nucleotidyltransferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0548	F		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0511	P		Seeded From UniProt	complete
involved_in	GO:0071555	cell wall organization	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0961	P		Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0511	F		Seeded From UniProt	complete
involved_in	GO:0006048	UDP-N-acetylglucosamine biosynthetic process	GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniPathway:UPA00113	P		Seeded From UniProt	complete
involved_in	GO:0009245	lipid A biosynthetic process	GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniPathway:UPA00973	P		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Dziadek, B et al. (2016) Mycobacterium tuberculosis AtsG (Rv0296c), GlmU (Rv1018c) and SahH (Rv3248c) Proteins Function as the Human IL-8-Binding Effectors and Contribute to Pathogen Entry into Human Neutrophils. PLoS ONE 11 e0148030 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Zhang, W et al. (2008) Expression, essentiality, and a microtiter plate assay for mycobacterial GlmU, the bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase. Int. J. Biochem. Cell Biol. 40 2560-71 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Zhang, Z et al. (2009) Structure and function of GlmU from Mycobacterium tuberculosis. Acta Crystallogr. D Biol. Crystallogr. 65 275-83 PubMed GONUTS page
↑ ^4.0 ^4.1 Parikh, A et al. (2009) PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity. J. Mol. Biol. 386 451-64 PubMed GONUTS page

[PMID:26829648-1] 1.0 ^1.1 Dziadek, B et al. (2016) Mycobacterium tuberculosis AtsG (Rv0296c), GlmU (Rv1018c) and SahH (Rv3248c) Proteins Function as the Human IL-8-Binding Effectors and Contribute to Pathogen Entry into Human Neutrophils. PLoS ONE 11 e0148030 PubMed GONUTS page

[PMID:18573680-2] 2.0 ^2.1 ^2.2 Zhang, W et al. (2008) Expression, essentiality, and a microtiter plate assay for mycobacterial GlmU, the bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase. Int. J. Biochem. Cell Biol. 40 2560-71 PubMed GONUTS page

[PMID:19237750-3] 3.0 ^3.1 ^3.2 Zhang, Z et al. (2009) Structure and function of GlmU from Mycobacterium tuberculosis. Acta Crystallogr. D Biol. Crystallogr. 65 275-83 PubMed GONUTS page

[PMID:19121323-4] 4.0 ^4.1 Parikh, A et al. (2009) PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity. J. Mol. Biol. 386 451-64 PubMed GONUTS page

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MYCTU:GLMU

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