Q8NST4 (GLMM_CORGL) 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:	Cgl0583, cg0675

Organism

Corynebacterium glutamicum (Brevibacterium flavum)

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	447 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 – 447	447	Phosphoglucosamine mutase HAMAP MF_01554_B		PRO_0000147879
Sites
	Active site	104	1	Phosphoserine intermediate By similarity
	Metal binding	104	1	Magnesium; via phosphate group By similarity
	Metal binding	243	1	Magnesium By similarity
	Metal binding	245	1	Magnesium By similarity
	Metal binding	247	1	Magnesium By similarity
Amino acid modifications
	Modified residue	104	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8NST4 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: BAD9552F59DCFE6A	FASTA	447	46,354
	10 20 30 40 50 60 MTRLFGTDGV RGLANEVLTA PLALKLGAAA AHVLTAEKRV DGRRPVAIVG RDPRVSGEML 70 80 90 100 110 120 AAALSAGMAS QGVDVIRVGV IPTPAVAFLT DDYGADMGVM ISASHNPMPD NGIKFFSAGG 130 140 150 160 170 180 HKLPDHVEDE IERVMDSLPA EGPTGHGVGR VIEEATDAQD RYLEHLKEAV PTSLEGIKIV 190 200 210 220 230 240 VDAANGAASV VAPTAYEAAG ATVIAIHNKP DSYNINMDCG STHIDQVQAA VLKHGADLGL 250 260 270 280 290 300 AHDGDADRCL AVDKDGNLVD GDQIMALLAI AMKENGELRK NTLVGTVMSN LGLKIAMDEA 310 320 330 340 350 360 GITLRTTKVG DRYVLEDLNA GGFSLGGEQS GHIVLPDHGT TGDGTLTGLS IMARMAETGK 370 380 390 400 410 420 SLGELAQAMT VLPQVLINVP VSDKSTIVSH PSVVAAIAEA EAELGATGRV LLRASGTEEL 430 440 FRVMVEAGDK EQARRIAGRL AAVVAEV

References

[1]

"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

[2]

"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000036 Genomic DNA. Translation: BAB97976.1. BX927149 Genomic DNA. Translation: CAF19288.1.
RefSeq	NP_599819.1. NC_003450.3. YP_224874.1. NC_006958.1.
3D structure databases
ProteinModelPortal	Q8NST4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1018587. 3343718.
GenomeReviews	Gene locus Cgl0583 in contig BA000036_GR. Gene locus cg0675 in contig BX927147_GR.
KEGG	cgb:cg0675. cgl:NCgl0558.
PATRIC	21493216. VBICorGlu203724_0574.
Phylogenomic databases
HOGENOM	HBG644964.
OMA	GVGSTHL.
ProtClustDB	PRK14318.
Enzyme and pathway databases
BioCyc	CGLU196627:CG0675-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_CORGL

Accession

Primary (citable) accession number: Q8NST4
Secondary accession number(s): Q6M7H9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program