P0C0V7 (GLMM_STAA8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoglucosamine mutase
EC=5.4.2.10

Gene names

Name:	glmM
Synonyms:	femD
Ordered Locus Names:	SAOUHSC_02405

Organism

Staphylococcus aureus (strain NCTC 8325)

Taxonomic identifier

93061 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	451 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. HAMAP MF_01554_B
Catalytic activity	Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. Ref.2
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01554_B
Post-translational modification	Activated by phosphorylation By similarity. HAMAP MF_01554_B
Miscellaneous	Disruption of glmM results in a drastically reduced methicillin resistance and in teicoplanin hypersusceptibility. HAMAP MF_01554_B
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: InterPro phosphoglucosamine mutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 451	451	Phosphoglucosamine mutase HAMAP MF_01554_B		PRO_0000147958
Sites
	Active site	102	1	Phosphoserine intermediate By similarity
	Metal binding	102	1	Magnesium; via phosphate group By similarity
	Metal binding	242	1	Magnesium By similarity
	Metal binding	244	1	Magnesium By similarity
	Metal binding	246	1	Magnesium By similarity
Amino acid modifications
	Modified residue	102	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0C0V7 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: A164B280C4B9ABD8	FASTA	451	49,266
	10 20 30 40 50 60 MGKYFGTDGV RGVANQELTP ELAFKLGRYG GYVLAHNKGE KHPRVLVGRD TRVSGEMLES 70 80 90 100 110 120 ALIAGLISIG AEVMRLGIIS TPGVAYLTRD MGAELGVMIS ASHNPVADNG IKFFGSDGFK 130 140 150 160 170 180 LSDEQENEIE ALLDQENPEL PRPVGNDIVH YSDYFEGAQK YLSYLKSTVD VNFEGLKIAL 190 200 210 220 230 240 DGANGSTSSL APFLFGDLEA DTETIGCSPD GYNINEKCGS THPEKLAEKV VETESDFGLA 250 260 270 280 290 300 FDGDGDRIIA VDENGQIVDG DQIMFIIGQE MHKNQELNND MIVSTVMSNL GFYKALEQEG 310 320 330 340 350 360 IKSNKTKVGD RYVVEEMRRG NYNLGGEQSG HIVMMDYNTT GDGLLTGIQL ASVIKMTGKS 370 380 390 400 410 420 LSELAGQMKK YPQSLINVRV TDKYRVEENV DVKEVMTKVE VEMNGEGRIL VRPSGTEPLV 430 440 450 RVMVEAATDE DAERFAQQIA DVVQDKMGLD K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Glanzmann P.J., Gustafson J., Berger-Baechi B. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"glmM operon and methicillin-resistant glmM suppressor mutants in Staphylococcus aureus." Glanzmann P.J., Gustafson J., Komatsuzawa H., Ohhta K., Berger-Baechi B. Antimicrob. Agents Chemother. 43:240-245(1999) [PubMed: 9925512] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY.
[3]	"The Staphylococcus aureus NCTC8325 genome." Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 8325.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y09570 Genomic DNA. Translation: CAA70762.1. Y15477 Genomic DNA. Translation: CAA75651.1. CP000253 Genomic DNA. Translation: ABD31434.1.
RefSeq	YP_500881.1. NC_007795.1.
3D structure databases
ProteinModelPortal	P0C0V7.
ModBase	Search...
Protein-protein interaction databases
STRING	P0C0V7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000030085; EBSTAP00000029036; EBSTAG00000030083.
GeneID	3919620.
GenomeReviews	Gene locus SAOUHSC_02405 in contig CP000253_GR.
KEGG	sao:SAOUHSC_02405.
PATRIC	19582121. VBIStaAur99865_2177.
Phylogenomic databases
eggNOG	COG1109.
GeneTree	EBGT00050000024615.
HOGENOM	HBG644964.
OMA	PLEDIQV.
PhylomeDB	P0C0V7.
ProtClustDB	PRK14316.
Enzyme and pathway databases
BioCyc	SAUR93061:SAOUHSC_02405-MONOMER.
Family and domain databases
HAMAP	MF_01554_B. GlmM_B. [Tree]
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]
Gene3D	G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
KO	K03431.
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. 3 hits.
TIGRFAMs	TIGR01455. GlmM. 1 hit.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLMM_STAA8

Accession

Primary (citable) accession number: P0C0V7
Secondary accession number(s): P95685, P95710, Q2FW94

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	January 25, 2012
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program