Reviewed, UniProtKB/Swiss-Prot Q5PBV0 (GLMU_ANAMM)

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
Ordered Locus Names:	AM058

Organism

Anaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]

Taxonomic identifier

234826 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

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. HAMAP MF_01631
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. HAMAP MF_01631
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 HAMAP MF_01631.
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.

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 cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW isoprenoid biosynthetic process Inferred from electronic annotation. Source: InterPro 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 428	428	Bifunctional protein glmU HAMAP MF_01631		PRO_0000233723
Regions
	Region	1 – 221	221	Pyrophosphorylase By similarity
	Region	6 – 9	4	Substrate binding By similarity
	Region	79 – 80	2	Substrate binding By similarity
	Region	222 – 242	21	Linker By similarity
	Region	243 – 428	186	N-acetyltransferase By similarity
Sites
	Active site	338	1	Proton acceptor By similarity
	Metal binding	105	1	Magnesium By similarity
	Metal binding	219	1	Magnesium By similarity
	Binding site	74	1	Substrate By similarity
	Binding site	140	1	Substrate; via amide nitrogen By similarity
	Binding site	362	1	Acetyl-CoA By similarity
	Binding site	398	1	Acetyl-CoA; via amide nitrogen By similarity
	Binding site	415	1	Acetyl-CoA By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5PBV0-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 6973CB6AC2326801	FASTA	428	45,168
	10 20 30 40 50 60 MDIVILAAGC GSRMCSTTPK ILHKLGNAPI IKHVLQLADE LRPKRAVIVT NAAVNGPVAA 70 80 90 100 110 120 LAGEHNLRLN TVLQGEIAGT GGAATSALQA LKNPSEEIVL ILYGDTPLLD KATVCHALDR 130 140 150 160 170 180 LSSGAKIVLV AFKSENNQYG RIVLGSSGNV LEVSHGRDTN GLAVSGAIAG YRQVISGLLG 190 200 210 220 230 240 GLSCRDGELY LTDIVQSAAE KNVEVGYVIA DERKAMGINT RADLAIAESY FQCMKRASFL 250 260 270 280 290 300 QSGVTLTSPD QVFFSIDTQI AQDVIVHPYV VFGAGVAVEP GAEILSYSHL EFCHIKKGAI 310 320 330 340 350 360 VGPFARVRGN STIDRGCVVG NFVEIKESSL GEMSKVKHLS YLGNSTIGKN TNVGAGTVIC 370 380 390 400 410 420 NYDGRNKQHS DIGNNCFVGA NSTIVSPIKV GDNAAIAAGS VITEDLPPRS LGIARSRQTT KPEYKTRR

References

[1]

"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins." Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr. Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000030 Genomic DNA. Translation: AAV86229.1.
RefSeq	YP_153484.1.
3D structure databases
SMR	Q5PBV0. Positions 3-427.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5PBV0.
Genome annotation databases
GeneID	3171039.
GenomeReviews	Gene locus AM058 in contig CP000030_GR.
KEGG	ama:AM058.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1207.
HOGENOM	HBG688195.
OMA	MERTCLA.
Enzyme and pathway databases
BioCyc	AMAR234826:AM058-MONOMER.
Family and domain databases
HAMAP	MF_01631. GlmU. [Tree]
InterPro	IPR005882. Bifunctional_GlmU. IPR018357. Hexapep_transf_CS. IPR001228. ISPD_synthase. IPR011004. Trimer_LpxA-like. [Graphical view]
Pfam	PF01128. IspD. 1 hit. [Graphical view]
PROSITE	PS00101. HEXAPEP_TRANSFERASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLMU_ANAMM

Accession

Primary (citable) accession number: Q5PBV0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	January 4, 2005
Last modified:	January 19, 2010
This is version 39 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)