Q9RSQ3 (GLMM_DEIRA) 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:	DR_2071

Organism

Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]

Taxonomic identifier

243230 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus › Deinococcus radiodurans

Protein attributes

Sequence length	444 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	UDP-N-acetylglucosamine biosynthetic process Inferred from Biological aspect of Ancestor. Source: RefGenome carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP phosphoglucosamine mutase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 444	444	Phosphoglucosamine mutase HAMAP-Rule MF_01554		PRO_0000147883
Sites
	Active site	103	1	Phosphoserine intermediate By similarity
	Metal binding	103	1	Magnesium; via phosphate group By similarity
	Metal binding	241	1	Magnesium By similarity
	Metal binding	243	1	Magnesium By similarity
	Metal binding	245	1	Magnesium By similarity
Amino acid modifications
	Modified residue	103	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9RSQ3 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 397CE86FA6AE39E3	FASTA	444	46,962
	10 20 30 40 50 60 MTERKYFGTD GVRAVAGEFP LTPAWVMALG AAAGEVFKRR NPRASVVIGK DTRQSGDMLE 70 80 90 100 110 120 AALAAGLTSR GVNVVHLGVL PTPGVSYLTR HLGAEAGVVI SASHNPYEDN GIKFFGPGGG 130 140 150 160 170 180 KLSDATELEI EAAIDEAATL APVTGVNLGS VTNYTEAERL YTAFLSSHAP DLSGMRIALD 190 200 210 220 230 240 CANGAAYRVA PKVFQQAGAD VFAVYTTPDG RNINRGCGST HMDHLRLIVR EGDYDLGIAF 250 260 270 280 290 300 DGDADRALFV DSRGNMIHGD HMLLLSARAR GEKAVVATIM TNMALEVKLQ EAGLTLERTA 310 320 330 340 350 360 VGDRYVHERL HAKGLNLGGE QSGHVLFLDV SPTGDGVLTA LLTLSSMKKL GTTLDALYDE 370 380 390 400 410 420 LVMFPQTLVN VRVKDKKAIA SDPAVQHAVA DAEKQLAGKG RINLRPSGTE NLIRVMVEGQ 430 440 DEGEIHDIAA AVAKVVEERG AAGA

References

[1]

"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. , McDonald L.A., Utterback T.R., Zalewski C., Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Science 286:1571-1577(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000513 Genomic DNA. Translation: AAF11621.1.
PIR	A75319.
RefSeq	NP_295794.1. NC_001263.1.
3D structure databases
ProteinModelPortal	Q9RSQ3.
ModBase	Search...
Protein-protein interaction databases
STRING	243230.DR_2071.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAF11621; AAF11621; DR_2071.
GeneID	1798453.
KEGG	dra:DR_2071.
PATRIC	21631820. VBIDeiRad64572_2296.
Phylogenomic databases
eggNOG	COG1109.
HOGENOM	HOG000268678.
KO	K03431.
OMA	TLMSNMS.
ProtClustDB	PRK14323.
Enzyme and pathway databases
BioCyc	DRAD243230:GH46-2439-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_DEIRA

Accession

Primary (citable) accession number: Q9RSQ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program