Q03GV0 (GLMM_PEDPA) 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:	PEPE_0477

Organism

Pediococcus pentosaceus (strain ATCC 25745 / 183-1w) [Complete proteome] [HAMAP]

Taxonomic identifier

278197 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Pediococcus

Protein attributes

Sequence length	452 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 – 452	452	Phosphoglucosamine mutase HAMAP MF_01554_B		PRO_0000305659
Sites
	Active site	104	1	Phosphoserine intermediate By similarity
	Metal binding	104	1	Magnesium; via phosphate group By similarity
	Metal binding	244	1	Magnesium By similarity
	Metal binding	246	1	Magnesium By similarity
	Metal binding	248	1	Magnesium By similarity
Amino acid modifications
	Modified residue	104	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q03GV0 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: BEDDCDB636686E73	FASTA	452	48,780
	10 20 30 40 50 60 MKLKYFGTDG VRGIANETLT PELAFQLGRA GGYVLTKHAK DDEQPRVLVS RDTRISGQLL 70 80 90 100 110 120 KHALISGLLS VGIEVMDMGI VTTPGVAYLV RKQEADAGVM ITASHNPVQD NGIKFFGSDG 130 140 150 160 170 180 YKLSDELEAE IEVLLDADKD NLPRPSSTGL GSVTDYPEGG LNYTAFLEQT IPDDLEGLHI 190 200 210 220 230 240 AIDAANGATS SYVSQIFADL NTEFDTMATN PDGLNINAGV GSTHPEGLAK FVVEKGADMG 250 260 270 280 290 300 VAFDGDGDRC IAVDELGNIV DGDKIMYICG KFLSERGRLK DDTVVTTVMS NLGLYKALEA 310 320 330 340 350 360 NDMHSVKTQV GDRYVVEEML KDGYNLGGEQ SGHIVFLDHN TTGDGMLTAI QLMYVVKQTG 370 380 390 400 410 420 KKLSELAADV TTYPQKLVNV RVQDKKLALE NQAIKDIIEK VENEMNGEGR VLVRPSGTED 430 440 450 LLRIMAEAPT KEAVGQYVDR IVAVVQSEVG VD

References

[1]

"Comparative genomics of the lactic acid bacteria." Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., Hawkins T. , Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., Weimer B.C., Mills D.A. Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006) [PubMed: 17030793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25745 / 183-1w.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000422 Genomic DNA. Translation: ABJ67572.1.
RefSeq	YP_804014.1. NC_008525.1.
3D structure databases
ProteinModelPortal	Q03GV0.
ModBase	Search...
Protein-protein interaction databases
STRING	Q03GV0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4418340.
GenomeReviews	Gene locus PEPE_0477 in contig CP000422_GR.
KEGG	ppe:PEPE_0477.
NMPDR	fig|278197.10.peg.444.
PATRIC	22874314. VBIPedPen34213_0469.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1109.
HOGENOM	HBG644964.
OMA	GVGSTHL.
PhylomeDB	Q03GV0.
ProtClustDB	PRK14316.
Enzyme and pathway databases
BioCyc	PPEN278197:PEPE_0477-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_PEDPA

Accession

Primary (citable) accession number: Q03GV0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	November 14, 2006
Last modified:	January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program