Q49869 (GLMM_MYCLE) 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:	ML0366

Organism

Mycobacterium leprae [Complete proteome] [HAMAP]

Taxonomic identifier

1769 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	463 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.
Sequence caution	The sequence AAA17297.1 differs from that shown. Reason: Erroneous initiation.

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 – 463	463	Phosphoglucosamine mutase HAMAP MF_01554_B		PRO_0000147916
Sites
	Active site	102	1	Phosphoserine intermediate By similarity
	Metal binding	102	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	102	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q49869 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: C0F1D18BB7697AC2	FASTA	463	47,644
	10 20 30 40 50 60 MGRLFGTDGV RGVANRELTP ELVLALGAAA ARCLANSGEP GRRVAVIGRD PRASGEMLEA 70 80 90 100 110 120 AVIAGLTSAG VDALRVGVLP TPAVAYLTGA YDADFGVMIS ASHNPMVDNG IKIFGPGGHK 130 140 150 160 170 180 LDDDTEDQIE DLVTGGPGLR PAGVAIGRVI DAEDATERYL RHVGKASTIR LDGLTVVVDC 190 200 210 220 230 240 AHGAASSAAP RAYRAAGARV IAINADPNGI NINDRCGSTD LGSLRSAVLA HRADLGLAHD 250 260 270 280 290 300 GDADRCLAVD ANGDLVDGDA IMVVLALAMQ EAGELSSNTL VTTVMSNLGL HLAMRSVGVI 310 320 330 340 350 360 VRTTDVGDRY VLEELRAGDF SLGGEQSGHI VMPALGSTGD GIITGLRLMT RMVQTSSSLA 370 380 390 400 410 420 ALASAMRALP QVLINVEVAD KTTAAAAPLV QTAVETAEVE LGNTGRILLR PSGTEPMIRV 430 440 450 460 MVEAAEEDVA HRVATRVAAA VSAQGSPLRC WNPDAISGVE LRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Smith D.R., Robison K. Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. , Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., Barrell B.G. Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00020 Genomic DNA. Translation: AAA17306.1. U00020 Genomic DNA. Translation: AAA17297.1. Different initiation. AL583918 Genomic DNA. Translation: CAC29874.1.
PIR	S72992.
RefSeq	NP_301362.1. NC_002677.1.
3D structure databases
ProteinModelPortal	Q49869.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000028969; EBMYCP00000028575; EBMYCG00000028964.
GeneID	909025.
GenomeReviews	Gene locus ML0366 in contig AL450380_GR.
KEGG	mle:ML0366.
NMPDR	fig|272631.1.peg.234.
PATRIC	18051338. VBIMycLep78757_0618.
Organism-specific databases
Leproma	ML0366.
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000015909.
HOGENOM	HBG644964.
OMA	GVGSTHL.
ProtClustDB	PRK14318.
Enzyme and pathway databases
BioCyc	MLEP272631:ML0366-MONOMER.
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_MYCLE

Accession

Primary (citable) accession number: Q49869
Secondary accession number(s): Q49862

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program