Q8Y5E6 (GLMM_LISMO) 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:	lmo2118

Organism

Listeria monocytogenes

Taxonomic identifier

1639 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

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 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 – 450	450	Phosphoglucosamine mutase HAMAP MF_01554_B		PRO_0000147911
Sites
	Active site	101	1	Phosphoserine intermediate By similarity
	Metal binding	101	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	101	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8Y5E6 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 829B7485BDA78B8B	FASTA	450	48,488
	10 20 30 40 50 60 MGKYFGTDGV RGVANSELTP ELAFRLGRMG GYVLTRHVGE HPRVLVARDT RISGEMLESA 70 80 90 100 110 120 LIAGLVSVGI EVMRLGVIST PGVAYLTKAQ GASASVMISA SHNPVDDNGI KFFGSDGFKL 130 140 150 160 170 180 SDDQEEEIEQ LLDTAEDTLP RPSGEGLGTV SDYFEGKQKY IQYLKQTIEN DFNGYHIALD 190 200 210 220 230 240 CANGATSGLA THLFADLDAD ISSMGASPNG LNINDGVGST HPEALAAFVL DKKADVGLAF 250 260 270 280 290 300 DGDGDRVIAI DEIGQIVDGD KIMFICAKYL REQGLLNNNT IVSTVMSNLG FYKGLKELEI 310 320 330 340 350 360 EDVQTAVGDR YVVEAMREGN YNLGGEQSGH IIFLDHNTTG DGLLSGIQLI NVMKATGKKL 370 380 390 400 410 420 SELAAEMKTF PQKLENIRVS DKNHVTDNPK VSKVIDEVEA EMAGNGRVLV RPSGTEPLVR 430 440 450 VMVEAATKEE TDEYCERISA VVRSEMALND

References

[1]

"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e / Serovar 1/2a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL591982 Genomic DNA. Translation: CAD00196.1.
PIR	AF1339.
RefSeq	NP_465642.1. NC_003210.1.
3D structure databases
ProteinModelPortal	Q8Y5E6.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	984740.
GenomeReviews	Gene locus lmo2118 in contig AL591824_GR.
KEGG	lmo:lmo2118.
PATRIC	20313446. VBILisMon69206_2170.
Organism-specific databases
GenoList	LMO2118.
Phylogenomic databases
HOGENOM	HBG644964.
OMA	PLEDIQV.
ProtClustDB	PRK14316.
Enzyme and pathway databases
BioCyc	LMON169963:LMO2118-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. IPR018247. EF_Hand_1_Ca_BS. 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_LISMO

Accession

Primary (citable) accession number: Q8Y5E6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	March 1, 2002
Last modified:	January 25, 2012
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