Q72JS7 (GLMM_THET2) 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:	TT_C0691

Organism

Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [Complete proteome] [HAMAP]

Taxonomic identifier

262724 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus › Thermus thermophilus

Protein attributes

Sequence length	437 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
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 – 437	437	Phosphoglucosamine mutase HAMAP-Rule MF_01554		PRO_0000147992
Sites
	Active site	101	1	Phosphoserine intermediate By similarity
	Metal binding	101	1	Magnesium; via phosphate group By similarity
	Metal binding	234	1	Magnesium By similarity
	Metal binding	236	1	Magnesium By similarity
	Metal binding	238	1	Magnesium By similarity
Amino acid modifications
	Modified residue	101	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q72JS7 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: D5E1827E3F7F61FD	FASTA	437	47,257
	10 20 30 40 50 60 MRRYFGTDGV RGEAGKPPLT PEFVLKLGQA AGAYFRTQEK RPVVLLAKDT RESSDLLEAA 70 80 90 100 110 120 LAAGLMSQGV RVEHLGVLPT PGVAHLTKAL KATAGAVISA SHNPYQDNGI KFFGPTGEKL 130 140 150 160 170 180 PDEAEEEIER LLLEDHPTRG IGTVGDFREA ERMYLDFLLA HAPDLTGLKV GLDLAHGATY 190 200 210 220 230 240 RIGPKLFQKA GAEVMAFFNT PDGRNINRGC GSTHPEALSR FVVELGLDLG LAFDGDGDRV 250 260 270 280 290 300 QFIDRKGRLF HGDHVLYLAA LAFGEKGVVG TVMSNMALEV ALKERGLAFH RAAVGDRYVL 310 320 330 340 350 360 EKLKETGLAL GGEPSGHVIF LRHHTTGDGL LTALLTLKAL KALGGDLADW YEALPLYPQV 370 380 390 400 410 420 LLNVRVSDKA KVMADPRLGE AVREAEARLG GRGRVNVRPS GTEPVIRVMV EAEEWAEEVA 430 RELAERVRAL SQEAQAV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The bacterium Thermus thermophilus, like hyperthermophilic archaea, uses a two-step pathway for the synthesis of mannosylglycerate." Empadinhas N., Albuquerque L., Henne A., Santos H., da Costa M.S. Appl. Environ. Microbiol. 69:3272-3279(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of the extreme thermophile Thermus thermophilus." Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J. Nat. Biotechnol. 22:547-553(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HB27 / ATCC BAA-163 / DSM 7039.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY194230 Genomic DNA. Translation: AAO67721.1. AE017221 Genomic DNA. Translation: AAS81039.1.
RefSeq	YP_004666.1. NC_005835.1.
3D structure databases
ProteinModelPortal	Q72JS7.
ModBase	Search...
Protein-protein interaction databases
STRING	262724.TTC0691.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAS81039; AAS81039; TT_C0691.
GeneID	2774886.
KEGG	tth:TTC0691.
PATRIC	23951787. VBITheThe54392_0688.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1109.
KO	K03431.
OMA	TLMSNMS.
ProtClustDB	PRK14323.
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. 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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLMM_THET2

Accession

Primary (citable) accession number: Q72JS7
Secondary accession number(s): Q846D2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program