A0QSQ1 (GLMM_MYCS2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoglucosamine mutase
EC=5.4.2.10

Gene names

Name:	glmM
Ordered Locus Names:	MSMEG_1559, MSMEI_1521

Organism

Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP]

Taxonomic identifier

246196 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium smegmatis

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate By similarity. HAMAP-Rule MF_01554
Catalytic activity	Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP-Rule MF_01554
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Post-translational modification	Activated by phosphorylation By similarity.
Sequence similarities	Belongs to the phosphohexose mutase family.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP phosphoglucosamine mutase activity 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 – 453	453	Phosphoglucosamine mutase HAMAP-Rule MF_01554		PRO_0000301342
Sites
	Active site	110	1	Phosphoserine intermediate By similarity
	Metal binding	110	1	Magnesium; via phosphate group By similarity
	Metal binding	248	1	Magnesium By similarity
	Metal binding	250	1	Magnesium By similarity
	Metal binding	252	1	Magnesium By similarity
Amino acid modifications
	Modified residue	110	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0QSQ1 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: E485F520273633AE	FASTA	453	46,555
	10 20 30 40 50 60 MARLFGTDGV RGVANRDLTA ELALALGSAA ARRLSTITTA TATDSAERAR RVAVVGRDPR 70 80 90 100 110 120 ASGEMLEAAV IAGLTSEGVD ALRVGVLPTP AVAYLTSAYD ADFGVMISAS HNPMPDNGIK 130 140 150 160 170 180 IFGPGGHKLD DATEDRIEEL VHAGAVARPT GTGIGRVLDA EDALDRYLRH AGKAVTTRLD 190 200 210 220 230 240 GLTVVVDCAH GAAWAAAPRA YRAAGANVIA INAEPTGLNI NDNCGSTHMD VVRAAVVEHG 250 260 270 280 290 300 ADLGLAHDGD ADRCLAVDAT GHVVDGDAIM VILALAMQEA GELAANTLVA TVMSNLGLHL 310 320 330 340 350 360 AMRAAGIDVR TTSVGDRYVL EELRSGEFSL GGEQSGHIVM PSFGTTGDGI VTGLRLMSRM 370 380 390 400 410 420 AQTGSSLAEL ADAMHSLPQV LINVAVADKT TVAQAPSVRS AVAAAEAELG DTGRILLRPS 430 440 450 GTEQVVRVMV EAADEDTARQ VAARVAESVS LQG

References

[1]	Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700084 / mc(2)155.
[2]	"Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?" Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M. Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700084 / mc(2)155.
[3]	"Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol." Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O. Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700084 / mc(2)155.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000480 Genomic DNA. Translation: ABK70035.1. CP001663 Genomic DNA. Translation: AFP37994.1.
RefSeq	YP_006566289.1. NC_018289.1. YP_885939.1. NC_008596.1.
3D structure databases
ProteinModelPortal	A0QSQ1.
ModBase	Search...
Protein-protein interaction databases
STRING	246196.MSMEG_1559.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABK70035; ABK70035; MSMEG_1559.
GeneID	13429335. 4535479.
KEGG	msg:MSMEI_1521. msm:MSMEG_1559.
PATRIC	18075577. VBIMycSme59918_1545.
Phylogenomic databases
eggNOG	COG1109.
HOGENOM	HOG000268678.
KO	K03431.
OMA	TLMSNMS.
ProtClustDB	PRK14318.
Enzyme and pathway databases
BioCyc	MSME246196:GJ4Y-1559-MONOMER.
Family and domain databases
Gene3D	3.40.120.10. 3 hits.
HAMAP	MF_01554_B. GlmM_B.
InterPro	IPR005844. A-D-PHexomutase_a/b/a-I. IPR016055. A-D-PHexomutase_a/b/a-I/II/III. IPR005845. A-D-PHexomutase_a/b/a-II. IPR005846. A-D-PHexomutase_a/b/a-III. IPR005843. A-D-PHexomutase_C. IPR016066. A-D-PHexomutase_CS. IPR005841. Alpha-D-phosphohexomutase_SF. IPR006352. GlmM. [Graphical view]
Pfam	PF02878. PGM_PMM_I. 1 hit. PF02879. PGM_PMM_II. 1 hit. PF02880. PGM_PMM_III. 1 hit. PF00408. PGM_PMM_IV. 1 hit. [Graphical view]
PRINTS	PR00509. PGMPMM.
SUPFAM	SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 2 hits.
TIGRFAMs	TIGR01455. glmM. 1 hit.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLMM_MYCS2

Accession

Primary (citable) accession number: A0QSQ1
Secondary accession number(s): I7G5W8

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	January 9, 2007
Last modified:	May 1, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program