A5WT14 (A5WT14_MYCTF) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Phosphoglucosamine mutase HAMAP MF_01554 RuleBase RU004327
EC=5.4.2.10 HAMAP MF_01554 RuleBase RU004327

Gene names

Name:	glmM HAMAP MF_01554
Ordered Locus Names:	TBFG_13478

Organism

Mycobacterium tuberculosis (strain F11) [Complete proteome] [HAMAP]

Taxonomic identifier

336982 [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 RuleBase RU004327
Catalytic activity	Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP MF_01554 RuleBase RU004327
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. HAMAP MF_01554 RuleBase RU004326

Ontologies

Keywords
Ligand	Magnesium HAMAP MF_01554 RuleBase RU004326 Metal-binding HAMAP MF_01554 RuleBase RU004326
Molecular function	Isomerase HAMAP MF_01554 RuleBase RU004327
PTM	Phosphoprotein HAMAP MF_01554
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
Sites
	Active site	102	1	Phosphoserine intermediate By similarity HAMAP MF_01554
	Metal binding	102	1	Magnesium; via phosphate group By similarity HAMAP MF_01554
	Metal binding	243	1	Magnesium By similarity HAMAP MF_01554
	Metal binding	245	1	Magnesium By similarity HAMAP MF_01554
	Metal binding	247	1	Magnesium By similarity HAMAP MF_01554
Amino acid modifications
	Modified residue	102	1	Phosphoserine By similarity HAMAP MF_01554

Sequences

	Sequence		Length	Mass (Da)
	A5WT14 [UniParc]. Last modified July 28, 2009. 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]

"The complete genome sequence of Mycobacterium tuberculosis F11." Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L., Grabherr M., Mauceli E., Brockman W., Young S., LaButti K., Pushparaj V., Sykes S., Baldwin J., Fitzgerald M., Bloom T., Zimmer A., Settipalli S. , Shea T., Arachchi H., Macdonald P., Abouelleil A., Lui A., Priest M., Berlin A., Gearin G., Brown A., Aftuck L., Bessette D., Allen N., Lubonja R., Lokyitsang T., Matthews C., Dunbar C., Benamara M., Nguyen T., Negash T., DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C., Kodira C., Zeng Q., Yandava C., O'Leary S., Alvarado L., Victor T., Murray M. Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000717 Genomic DNA. Translation: ABR07803.1.
RefSeq	YP_001289405.1. NC_009565.1.
3D structure databases
ProteinModelPortal	A5WT14.
ModBase	Search...
Protein-protein interaction databases
STRING	A5WT14.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5224167.
GenomeReviews	Gene locus TBFG_13478 in contig CP000717_GR.
KEGG	mtf:TBFG_13478.
PATRIC	18138474. VBIMycTub9078_3870.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	GVGSTHL.
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

A5WT14_MYCTF

Accession

Primary (citable) accession number: A5WT14

Entry history

Integrated into UniProtKB/TrEMBL:	July 28, 2009
Last sequence update:	July 28, 2009
Last modified:	December 14, 2011
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)