Reviewed, UniProtKB/Swiss-Prot Q0A772 (GLMM_ALHEH)

Names and origin

Protein names

Recommended name:
    Phosphoglucosamine mutase
    EC=5.4.2.10

Gene names

Name:	glmM
Ordered Locus Names:	Mlg_1973

Organism

Alkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]

Taxonomic identifier

187272 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Ectothiorhodospiraceae › Alkalilimnicola

Protein attributes

Sequence length	451 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
Catalytic activity	Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP MF_01554
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01554
Post-translational modification	Activated by phosphorylation By similarity. HAMAP MF_01554
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: UniProtKB-KW 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 – 451	451	Phosphoglucosamine mutase HAMAP MF_01554		PRO_0000301273
Sites
	Active site	101	1	Phosphoserine intermediate By similarity
	Metal binding	101	1	Magnesium; via phosphate group By similarity
	Metal binding	240	1	Magnesium By similarity
	Metal binding	242	1	Magnesium By similarity
	Metal binding	244	1	Magnesium By similarity
Amino acid modifications
	Modified residue	101	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0A772-1 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: 80FE8581598C2E82	FASTA	451	47,692
	10 20 30 40 50 60 MKKEYFGTDG IRGTVGEPPI TPDFMLHLGW AAGRVLARAG QSSVLVGKDT RISGYMLESA 70 80 90 100 110 120 LESGFAAAGV NVKLLGPMPT PAIAYLTRTL RAAAGVVISA SHNPHEDNGI KFFSDDGEKL 130 140 150 160 170 180 DDATELAIEA ELRQPLKPAP SARLGKASRI NDAPGRYIEF CKRSFPYELS LRGLRLVVDC 190 200 210 220 230 240 ANGATYHVAP AVFHELGAEV IPLADDPDGL NINADCGSLH PKGLQAAVRE HDADAGIAFD 250 260 270 280 290 300 GDGDRVIMVD HRGEVVDGDG LLYIIARQRM ANGGLAGPVV GTVMSNLGLE QGIGRLGLPF 310 320 330 340 350 360 LRAKVGDRYV MEMLRREGGI LGGESSGHLI CLDRTTTGDG IVSALQVLEA MAAQERTLAE 370 380 390 400 410 420 LADGMDRLPQ IMVNVPISRG VPVQDHATVT DAVRDAETRL AGRGRVLLRP SGTEPVLRVM 430 440 450 VEGPDQAEVS ATAEAIAGAV REAHATLTAP R

References

[1]

"Complete sequence of Alkalilimnicola ehrilichei MLHE-1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000453 Genomic DNA. Translation: ABI57315.1.
RefSeq	YP_742805.1.
3D structure databases
SMR	Q0A772. Positions 4-443.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0A772.
Genome annotation databases
GeneID	4268516.
GenomeReviews	Gene locus Mlg_1973 in contig CP000453_GR.
KEGG	aeh:Mlg_1973.
NMPDR	fig|187272.6.peg.1880.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1109.
HOGENOM	HBG644964.
OMA	VHDRYIE.
PhylomeDB	Q0A772.
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. A-D-PHexomutase_N. IPR006352. GlmM. [Graphical view]
Gene3D	G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
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.
TIGRFAMs	TIGR01455. glmM. 1 hit.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLMM_ALHEH

Accession

Primary (citable) accession number: Q0A772

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	October 17, 2006
Last modified:	February 9, 2010
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)