O06258 (GLMM_MYCTU) 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:	Rv3441c, MT3546

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	448 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
Miscellaneous	Was identified as a high-confidence drug target. HAMAP MF_01554_B
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 growth Inferred from mutant phenotype. Source: MTBBASE
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_B		PRO_0000147918
Sites
	Active site	102	1	Phosphoserine intermediate By similarity
	Metal binding	102	1	Magnesium; via phosphate group By similarity
	Metal binding	243	1	Magnesium By similarity
	Metal binding	245	1	Magnesium By similarity
	Metal binding	247	1	Magnesium By similarity
Amino acid modifications
	Modified residue	102	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O06258 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 1A796BAC81742A04	FASTA	448	45,873
	10 20 30 40 50 60 MGRLFGTDGV RGVANRELTA ELALALGAAA ARRLSRSGAP GRRVAVLGRD PRASGEMLEA 70 80 90 100 110 120 AVIAGLTSEG VDALRVGVLP TPAVAYLTGA YDADFGVMIS ASHNPMPDNG IKIFGPGGHK 130 140 150 160 170 180 LDDDTEDQIE DLVLGVSRGP GLRPAGAGIG RVIDAEDATE RYLRHVAKAA TARLDDLAVV 190 200 210 220 230 240 VDCAHGAASS AAPRAYRAAG ARVIAINAEP NGRNINDGCG STHLDPLRAA VLAHRADLGL 250 260 270 280 290 300 AHDGDADRCL AVDANGDLVD GDAIMVVLAL AMKEAGELAC NTLVATVMSN LGLHLAMRSA 310 320 330 340 350 360 GVTVRTTAVG DRYVLEELRA GDYSLGGEQS GHIVMPALGS TGDGIVTGLR LMTRMVQTGS 370 380 390 400 410 420 SLSDLASAMR TLPQVLINVE VVDKATAAAA PSVRTAVEQA AAELGDTGRI LLRPSGTEPM 430 440 IRVMVEAADE GVAQRLAATV ADAVSTAR

References

[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis." Raman K., Yeturu K., Chandra N. BMC Syst. Biol. 2:109-109(2008) [PubMed: 19099550] [Abstract] Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842583 Genomic DNA. Translation: CAB08690.1. AE000516 Genomic DNA. Translation: AAK47887.1.
PIR	G70976.
RefSeq	NP_217958.1. NC_000962.2. NP_338073.1. NC_002755.2.
3D structure databases
ProteinModelPortal	O06258.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000000937; EBMYCP00000000937; EBMYCG00000000937. EBMYCT00000072259; EBMYCP00000070318; EBMYCG00000072254.
GeneID	887589. 922957.
GenomeReviews	Gene locus MT3546 in contig AE000516_GR. Gene locus Rv3441c in contig AL123456_GR.
KEGG	mtc:MT3546. mtu:Rv3441c.
PATRIC	18129533. VBIMycTub22151_3862.
TIGR	MT3546.
Organism-specific databases
TubercuList	Rv3441c.
Phylogenomic databases
GeneTree	EBGT00050000015909.
HOGENOM	HBG644964.
OMA	GVGSTHL.
PhylomeDB	O06258.
ProtClustDB	PRK14318.
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_MYCTU

Accession

Primary (citable) accession number: O06258
Secondary accession number(s): Q7D5J3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	July 1, 1997
Last modified:	January 25, 2012
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program