Q89AF3 (GLMM_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoglucosamine mutase
EC=5.4.2.10

Gene names

Name:	glmM
Synonyms:	mrsA
Ordered Locus Names:	bbp_344

Organism

Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]

Taxonomic identifier

224915 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Baizongia pistaciae)

Protein attributes

Sequence length	453 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-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
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
Molecule processing
	Chain	1 – 453	453	Phosphoglucosamine mutase HAMAP-Rule MF_01554		PRO_0000147861
Sites
	Active site	100	1	Phosphoserine intermediate By similarity
	Metal binding	100	1	Magnesium; via phosphate group By similarity
	Metal binding	239	1	Magnesium By similarity
	Metal binding	241	1	Magnesium By similarity
	Metal binding	243	1	Magnesium By similarity
Amino acid modifications
	Modified residue	100	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q89AF3 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 013FD17F082BB570	FASTA	453	50,698
	10 20 30 40 50 60 MIKYFGTDGI RGVVGKTPIT ADFFFKLGAV IGKILYFYDV KKIIIGRDTR LSSYMLEEAL 70 80 90 100 110 120 QFGLSLVGVS VISVGVLPTP AISYFTKLFN LEVGVVISAS HNQFRDNGIK FFVKNGVKLS 130 140 150 160 170 180 AKFERRIEKQ LNKTIILKQF VDLGHISYKR ALQQKYINFC ISTLPNNFRL NNFKIVLDCA 190 200 210 220 230 240 NGSTYELAPI IFRELGANVV LMSAAPNGLN INDKCGTTDL QEIQRLVLSE KADLGISFDG 250 260 270 280 290 300 DGDRVIMIDH FGNSVNGDQI LYILAKNYKK NKKLRGGVVG TKMSNGGLSL ALSKIGIPFI 310 320 330 340 350 360 TVNIGDRYIF KKLKEKQWRL GAESSGHVIL LDYAPVGDGI ITSLQILKII FDENSTLKSL 370 380 390 400 410 420 CSDIHMLPQI IINIKNNIDI SFLKNFKIQS VLSKYKDFLG KYSRIMLRLS GTEKCIRIMI 430 440 450 EGCCSKKINI FSKMLINVIN SVKKSRFSII TMF

References

[1]

"Reductive genome evolution in Buchnera aphidicola." van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bp.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016826 Genomic DNA. Translation: AAO27063.1.
RefSeq	NP_777958.1. NC_004545.1.
3D structure databases
ProteinModelPortal	Q89AF3.
ModBase	Search...
Protein-protein interaction databases
STRING	224915.bbp344.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO27063; AAO27063; bbp_344.
GeneID	1058615.
KEGG	bab:bbp344.
PATRIC	21245481. VBIBucAph80364_0339.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1109.
KO	K03431.
OMA	TLMSNMS.
Enzyme and pathway databases
BioCyc	BAPH224915:GJ9D-344-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. 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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLMM_BUCBP

Accession

Primary (citable) accession number: Q89AF3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program