Q4L837 (GLMM_STAHJ) 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:	SH0879

Organism

Staphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]

Taxonomic identifier

279808 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	450 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 MF_01554_B
Catalytic activity	Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP MF_01554_B
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
Sequence similarities	Belongs to the phosphohexose mutase family.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete 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 – 450	450	Phosphoglucosamine mutase HAMAP MF_01554_B		PRO_0000147967
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)
	Q4L837 [UniParc]. Last modified August 2, 2005. Version 1. Checksum: 2B980B8D57EC2C97	FASTA	450	48,923
	10 20 30 40 50 60 MVKYFGTDGV RGIANKELTP ELAFKLGRYG GYVLAHNEGA DRPKVLVGRD TRVSGEMLES 70 80 90 100 110 120 ALISGLASIG AEVMRLGVIS TPGVAYLTRE MGAELGVMIS ASHNPVADNG IKFFGADGFK 130 140 150 160 170 180 LSDAQEEEIE TLLDQDNPDL PRPVGTDIVH FSDYFEGAQK YLSYLKSTID VNLEGLKITL 190 200 210 220 230 240 DGANGSTSAL APFLFGDLEA DTETIGCSPD GYNINDNCGS THPELLAEKV LETESDFGLA 250 260 270 280 290 300 FDGDGDRLIA VDEKGNIIDG DQIMFVIGQE MHKNQELNND MIVSTVMSNL GFYKALENEG 310 320 330 340 350 360 IKSNKTKVGD RYVVEEMRKG NYNLGGEQSG HIVMMDYNTT GDGLLTGVQL AAVIKMSGKP 370 380 390 400 410 420 LSELAAQMKK YPQSLINVKV TDKHHVEDNE DVKKVMDEVE TEMNGEGRIL VRPSGTEPLV 430 440 450 RVMVEASTDE DAQRFAQRIA DEVQSKMGLE

References

[1]

"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species." Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K. J. Bacteriol. 187:7292-7308(2005) [PubMed: 16237012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JCSC1435.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP006716 Genomic DNA. Translation: BAE04188.1.
RefSeq	YP_252794.1. NC_007168.1.
3D structure databases
ProteinModelPortal	Q4L837.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4L837.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000045461; EBSTAP00000043912; EBSTAG00000045458.
GeneID	3482257.
GenomeReviews	Gene locus SH0879 in contig AP006716_GR.
KEGG	sha:SH0879.
NMPDR	fig|279808.3.peg.892.
PATRIC	19617796. VBIStaHae67511_0865.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1109.
GeneTree	EBGT00050000024615.
HOGENOM	HBG644964.
OMA	GVGSTHL.
PhylomeDB	Q4L837.
ProtClustDB	PRK14316.
Enzyme and pathway databases
BioCyc	SHAE279808:SH0879-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_STAHJ

Accession

Primary (citable) accession number: Q4L837

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	August 2, 2005
Last modified:	January 25, 2012
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program