B9MI07 (GLMM_ACIET) 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:	Dtpsy_1477

Organism

Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)) [Complete proteome] [HAMAP]

Taxonomic identifier

535289 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Acidovorax

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 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 – 444	444	Phosphoglucosamine mutase HAMAP MF_01554_B		PRO_1000185365
Sites
	Active site	102	1	Phosphoserine intermediate By similarity
	Metal binding	102	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	102	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	B9MI07 [UniParc]. Last modified March 24, 2009. Version 1. Checksum: A6070E0C759798F5	FASTA	444	47,793
	10 20 30 40 50 60 MTRKYFGTDG IRGTVGQSPI TPDFALRLAH AVGRVLRRTQ ERPTVLIGKD TRISGYMLES 70 80 90 100 110 120 ALESGFNSAG VDVVLLGPLP TPGVAYLTRA QRASLGVVIS ASHNPYPDNG IKFFSAQGTK 130 140 150 160 170 180 LPDAWEEEVE AALEQPPVWA DSASLGKTRR LDDAAGRYIE FCKSTFANDL TLRGLKIVVD 190 200 210 220 230 240 AAHGAAYHIA PKVFHELGAE VLAIGCAPDG LNINHQVGAT HPDALVRAVR ANHADYGIAL 250 260 270 280 290 300 DGDADRVQMV DAAGRLFNGD ELLYVMVAAR LARDEHVPGV VGTLMTNMAV EEALQRRGVK 310 320 330 340 350 360 FMRAKVGDRY VLEELQRQHW LLGGEGSGHL LALDRHTTGD GLISALQVLQ ACVRSGKTLA 370 380 390 400 410 420 QLLADVPLFP QVLLNVRLNP GQDWKTNPVL ADAIRDAEAE LGAHGRVLVR ASGTEPLLRV 430 440 MVEAREAEQA NRCAQRIADA ARAG

References

[1]

"Complete sequence of Diaphorobacter sp. TPSY." US DOE Joint Genome Institute Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D. Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TPSY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001392 Genomic DNA. Translation: ACM32939.1.
RefSeq	YP_002552939.1. NC_011992.1.
3D structure databases
ProteinModelPortal	B9MI07.
ModBase	Search...
Protein-protein interaction databases
STRING	B9MI07.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	7385119.
GenomeReviews	Gene locus Dtpsy_1477 in contig CP001392_GR.
KEGG	dia:Dtpsy_1477.
PATRIC	21780035. VBIDiaSp55748_1508.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	PLEDIQV.
ProtClustDB	PRK10887.
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_ACIET

Accession

Primary (citable) accession number: B9MI07

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	March 24, 2009
Last modified:	January 25, 2012
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program