Q58500 (GLMM_METJA) 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:	MJ1100

Organism

Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)

Taxonomic identifier

243232 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus

Protein attributes

Sequence length	448 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 By similarity. HAMAP MF_01554_A
Catalytic activity	Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP MF_01554_A
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01554_A
Subunit structure	Forms large aggregates. Ref.1
Post-translational modification	Activated by phosphorylation By similarity. HAMAP 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 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 – 448	448	Phosphoglucosamine mutase HAMAP MF_01554_A		PRO_0000148029
Sites
	Active site	89	1	Phosphoserine intermediate By similarity
	Metal binding	89	1	Magnesium; via phosphate group By similarity
	Metal binding	232	1	Magnesium By similarity
	Metal binding	234	1	Magnesium By similarity
	Metal binding	236	1	Magnesium By similarity
Amino acid modifications
	Modified residue	89	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	209	1	L → I in ABZ91903. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q58500 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: FBC7EF17A73DF9B4	FASTA	448	50,099
	10 20 30 40 50 60 MGRLFGTSGI RMKNLSPKIA YKVGLAVAKK YKKVVVGRDT RTTGKLIETA LTAGILNGGG 70 80 90 100 110 120 EVTTINIVPT PVLGFNARNY DVGIMITASH NPPEYNGIKL FNKNGLAFNK KEEDEIEEII 130 140 150 160 170 180 FKEDFIEVEW HSVGEIWEDS RAIRNYMEHI LKNVEINEKF NVVIDCANAS ACLVSPYLFT 190 200 210 220 230 240 DLGCHVISVN SHMDGRFIGR LPEPDEKNLK KTMDMIKGLN MSGDNYIGIA HDGDADRMVA 250 260 270 280 290 300 IDEKGRLADF DKLLAAFSRY MVEKTGNKKI VTTVDASMII DEYLKDLDVE IIRTKVGDVA 310 320 330 340 350 360 VAEEMIKNSA VFGGEPSGTW IHADIHLTPD GILSGLRVLE MLDFYNKKLY EILDEIPSYV 370 380 390 400 410 420 NLREKIPCED DKKEKVMSYV IENGESLFKT VPETVDGARF NLENGWVLIR PSGTEPYIRV 430 440 RVEAKNNKDA KELLEKGIKL VKEALSAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Acetamido sugar biosynthesis in the Euryarchaea." Namboori S.C., Graham D.E. J. Bacteriol. 190:2987-2996(2008) [PubMed: 18263721] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]	"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed: 8688087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.

Cross-references

Sequence databases
EMBL GenBank DDBJ	EU430076 Genomic DNA. Translation: ABZ91903.1. L77117 Genomic DNA. Translation: AAB99103.1.
PIR	C64437.
RefSeq	NP_248093.1. NC_000909.1.
3D structure databases
ProteinModelPortal	Q58500.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1451997.
GenomeReviews	Gene locus MJ1100 in contig L77117_GR.
KEGG	mja:MJ_1100.
NMPDR	fig|243232.1.peg.1130.
TIGR	MJ1100.
Phylogenomic databases
HOGENOM	HBG644964.
OMA	AKEVPRY.
ProtClustDB	CLSK2517686.
Enzyme and pathway databases
BioCyc	MJAN243232:MJ_1100-MONOMER.
Family and domain databases
HAMAP	MF_01554_A. GlmM_A. [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. IPR023666. GlmM_arc. IPR024086. GlmM_arc-related. [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	TIGR03990. Arch_GlmM. 1 hit.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLMM_METJA

Accession

Primary (citable) accession number: Q58500
Secondary accession number(s): B1A8K6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	November 16, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program