Q6LYB4 (GLMM_METMP) 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:	MMP1077

Organism

Methanococcus maripaludis (strain S2 / LL) [Complete proteome] [HAMAP]

Taxonomic identifier

267377 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanococcaceae › Methanococcus › Methanococcus maripaludis

Protein attributes

Sequence length	447 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. Also catalyzes the isomerization of glucose-1-phosphate to glucose-6-phosphate, but at a 5-fold lower rate. Ref.2
Catalytic activity	Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. Ref.2
Cofactor	Binds 1 magnesium ion per subunit. Ref.2
Subunit structure	Monomer. Also forms large aggregates. Ref.2
Post-translational modification	Activated by phosphorylation. Glucose-1,6-bisphosphate or fructose-1,6-bisphosphate can activate the enzyme in vitro. However, since glucose-1,6-bisphosphate is not believed to form in methanogens, the physiologically relevant activator might be a serine kinase protein. HAMAP-Rule MF_01554_A
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 – 447	447	Phosphoglucosamine mutase HAMAP-Rule MF_01554_A		PRO_0000337813
Sites
	Active site	88	1	Phosphoserine intermediate By similarity
	Metal binding	88	1	Magnesium; via phosphate group By similarity
	Metal binding	231	1	Magnesium By similarity
	Metal binding	233	1	Magnesium By similarity
	Metal binding	235	1	Magnesium By similarity
Amino acid modifications
	Modified residue	88	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6LYB4 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: F50B41234C5B6EAA	FASTA	447	49,384
	10 20 30 40 50 60 MKLFGTSGIR MKNLDPLIAY KVGFAISKNF KKAVIGRDTR TTGNLIESAI TAGLLNGGCD 70 80 90 100 110 120 VTTIGMVPTP VLGYSAKDYD LGIMITASHN PPEYNGIKLF NKNGTAFDPK QEKELENIIN 130 140 150 160 170 180 NDDFNECTWD NIGCVVEDKT AVKKYFEYIL QNLNLNTNFN VVVDCANAAG CVVSPNIFTE 190 200 210 220 230 240 AGCKVISVNS HCDGRFVGRM PEPNETNLKE TVDIIKGLNS NGRNYVGIAH DGDADRMIAI 250 260 270 280 290 300 DELGRVTDFD KLLAAFCKYL VQKTGADKIV TTVDASMAIE EYLNEFGAKV IRTKIGDVAV 310 320 330 340 350 360 AEELEKTGAI FGGEPSGTWI HRDIHLTPDG ILSGLRVLEM MEFYGKKLHE IIDEVPSYCN 370 380 390 400 410 420 MREKISCPDN LKQNVMDYVS KEGEKIFEKK PETLDGVRFS FENGWILIRP SGTESYVRVR 430 440 VEAKEKDFAE KLMKTGISMV KTGISGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis." Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J., Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M., Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A., Moore B.C. , Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D., Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W., Olson M.V., Leigh J.A. J. Bacteriol. 186:6956-6969(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: S2 / LL.
[2]	"Acetamido sugar biosynthesis in the Euryarchaea." Namboori S.C., Graham D.E. J. Bacteriol. 190:2987-2996(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PTM, PH DEPENDENCE, SUBUNIT. Strain: 900.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX950229 Genomic DNA. Translation: CAF30633.1.
RefSeq	NP_988197.1. NC_005791.1.
3D structure databases
HSSP	HSSP built from PDB template 1WQA based on UniProtKB O58651.
ProteinModelPortal	Q6LYB4.
ModBase	Search...
Protein-protein interaction databases
STRING	267377.MMP1077.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAF30633; CAF30633; MMP1077.
GeneID	2762645.
KEGG	mmp:MMP1077.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1109.
HOGENOM	HOG000268680.
KO	K03431.
OMA	TWIHRDI.
ProtClustDB	CLSK2517686.
Enzyme and pathway databases
BioCyc	MMAR267377:GJ77-1108-MONOMER.
Family and domain databases
Gene3D	3.40.120.10. 3 hits.
HAMAP	MF_01554_A. GlmM_A.
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. IPR023666. GlmM_arc. IPR024086. GlmM_arc-related. [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	TIGR03990. Arch_GlmM. 1 hit.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLMM_METMP

Accession

Primary (citable) accession number: Q6LYB4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program