O34824 (GLMM_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoglucosamine mutase
EC=5.4.2.10

Gene names

Name:	glmM
Synonyms:	ybbT
Ordered Locus Names:	BSU01770

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

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-Rule MF_01554
Catalytic activity	Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP-Rule MF_01554
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Post-translational modification	Activated by phosphorylation By similarity.
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	UDP-N-acetylglucosamine biosynthetic process Inferred from Biological aspect of Ancestor. Source: RefGenome carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP phosphoglucosamine mutase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
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-Rule MF_01554		PRO_0000147846
Sites
	Active site	100	1	Phosphoserine intermediate
	Metal binding	100	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	100	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	7	1	T → K in BAA33070. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O34824 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: D13861BF333EFFA3	FASTA	448	48,433
	10 20 30 40 50 60 MGKYFGTDGV RGVANSELTP ELAFKVGRFG GYVLTKDKQR PKVLIGRDTR ISGHMLEGAL 70 80 90 100 110 120 VAGLLSIGAE VMRLGVISTP GVSYLTKAMD AEAGVMISAS HNPVQDNGIK FFGGDGFKLS 130 140 150 160 170 180 DEQEAEIERL MDEPEDKLPR PVGADLGLVN DYFEGGQKYL QFLKQTADED FTGIHVALDC 190 200 210 220 230 240 ANGATSSLAT HLFADLDADV STMGTSPNGL NINDGVGSTH PEALSAFVKE KNADLGLAFD 250 260 270 280 290 300 GDGDRLIAVD EKGNIVDGDQ IMYICSKHLK SEGRLKDDTV VSTVMSNLGF YKALEKEGIK 310 320 330 340 350 360 SVQTAVGDRY VVEAMKKDGY NVGGEQSGHL IFLDYNTTGD GLLSAIMLMN TLKATGKPLS 370 380 390 400 410 420 ELAAEMQKFP QLLVNVRVTD KYKVEENEKV KAVISEVEKE MNGDGRILVR PSGTEPLVRV 430 440 MAEAKTKELC DEYVNRIVEV VRSEMGLE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of the 70kb region between 17 and 23 degree of the Bacillus subtilis chromosome." Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H. Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis." Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M. Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, MASS SPECTROMETRY. Strain: 168.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB006424 Genomic DNA. Translation: BAA33070.1. AL009126 Genomic DNA. Translation: CAB11953.1.
PIR	B69745.
RefSeq	NP_388058.1. NC_000964.3.
3D structure databases
ProteinModelPortal	O34824.
SMR	O34824. Positions 3-445.
ModBase	Search...
Protein-protein interaction databases
STRING	224308.BSU01770.
Proteomic databases
PaxDb	O34824.
Protocols and materials databases
DNASU	938632.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB11953; CAB11953; BSU01770.
GeneID	938632.
KEGG	bsu:BSU01770.
PATRIC	18971907. VBIBacSub10457_0182.
Organism-specific databases
GenoList	BSU01770. [Micado]
Phylogenomic databases
eggNOG	COG1109.
HOGENOM	HOG000268678.
KO	K03431.
OMA	SGHIILF.
ProtClustDB	PRK14316.
Enzyme and pathway databases
BioCyc	BSUB:BSU01770-MONOMER.
Family and domain databases
Gene3D	3.40.120.10. 3 hits.
HAMAP	MF_01554_B. GlmM_B.
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]
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_BACSU

Accession

Primary (citable) accession number: O34824
Secondary accession number(s): O87090

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program