B7M082 (GLMM_ECO8A) 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:	ECIAI1_3324

Organism

Escherichia coli O8 (strain IAI1) [Complete proteome] [HAMAP]

Taxonomic identifier

585034 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	445 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
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP phosphoglucosamine mutase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 445	445	Phosphoglucosamine mutase HAMAP-Rule MF_01554		PRO_1000201097
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)
	B7M082 [UniParc]. Last modified March 24, 2009. Version 1. Checksum: ECDF9A0378A980EC	FASTA	445	47,544
	10 20 30 40 50 60 MSNRKYFGTD GIRGRVGDAP ITPDFVLKLG WAAGKVLARH GSRKIIIGKD TRISGYMLES 70 80 90 100 110 120 ALEAGLAAAG LSALFTGPMP TPAVAYLTRT FRAEAGIVIS ASHNPFYDNG IKFFSIDGTK 130 140 150 160 170 180 LPDAVEEAIE AEMEKEISCV DSAELGKASR IVDAAGRYIE FCKATFPNEL SLSELKIVVD 190 200 210 220 230 240 CANGATYHIA PNVLRELGAN VIAIGCEPNG VNINAEVGAT DVRALQARVL AEKADLGIAF 250 260 270 280 290 300 DGDGDRVIMV DHEGNKVDGD QIMYIIAREG LRQGQLRGGA VGTLMSNMGL ELALKQLGIP 310 320 330 340 350 360 FARAKVGDRY VLEKMQEKGW RIGAENSGHV ILLDKTTTGD GIVAGLQVLA AMARNHMSLH 370 380 390 400 410 420 DLCSGMKMFP QILVNVRYTA GSGDPLEHES VKAVTAEVEA ALGNRGRVLL RKSGTEPLIR 430 440 VMVEGEDEAQ VTEFAHRIAD AVKAV

References

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. , Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E. PLoS Genet. 5:E1000344-E1000344(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: IAI1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928160 Genomic DNA. Translation: CAR00138.1.
RefSeq	YP_002388659.1. NC_011741.1.
3D structure databases
ProteinModelPortal	B7M082.
SMR	B7M082. Positions 5-444.
ModBase	Search...
Protein-protein interaction databases
STRING	585034.ECIAI1_3324.
Proteomic databases
PRIDE	B7M082.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAR00138; CAR00138; ECIAI1_3324.
GeneID	7124696.
KEGG	ecr:ECIAI1_3324.
PATRIC	18325919. VBIEscCol26572_3259.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1109.
HOGENOM	HOG000268678.
KO	K03431.
OMA	KVIAIGC.
ProtClustDB	PRK10887.
Enzyme and pathway databases
BioCyc	ECOL585034:GJ84-3364-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. 3 hits.
TIGRFAMs	TIGR01455. glmM. 1 hit.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLMM_ECO8A

Accession

Primary (citable) accession number: B7M082

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	March 24, 2009
Last modified:	May 1, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program