Q6AD28 (GLMM_LEIXX) 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:	Lxx20010

Organism

Leifsonia xyli subsp. xyli (strain CTCB07) [Complete proteome] [HAMAP]

Taxonomic identifier

281090 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Microbacteriaceae › Leifsonia › Leifsonia xyli › Leifsonia xyli subsp. xyli

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. HAMAP-Rule MF_01554
Post-translational modification	Activated by phosphorylation By similarity. HAMAP-Rule MF_01554
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_0000147909
Sites
	Active site	109	1	Phosphoserine intermediate By similarity
	Metal binding	109	1	Magnesium; via phosphate group By similarity
	Metal binding	246	1	Magnesium By similarity
	Metal binding	248	1	Magnesium By similarity
	Metal binding	250	1	Magnesium By similarity
Amino acid modifications
	Modified residue	109	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6AD28 [UniParc]. Last modified September 13, 2004. Version 1. Checksum: 78CB26B761529592	FASTA	453	47,319
	10 20 30 40 50 60 MPRLFGTDGV RGLANGTLTA DLALGLAQAA AAVLTRGRSA EARRAVGKRP LAIVARDPRV 70 80 90 100 110 120 SGEFLSAAVA AGLASSGIDV YDAGVIPTPA AAFLIADFDA DFGVMVSASH NPAPDNGIKI 130 140 150 160 170 180 FARGGTKLPD VVEDRIEEHL HLEKLTPTGA EVGRIQCFAD AEDRYVLHLL ASLPHRLDGI 190 200 210 220 230 240 HVVLDCAHGA AAGISPEVFT DAGARVTVIG DAPDGMNIND GVGSTHLDRL AEAVLAAGAD 250 260 270 280 290 300 VGIAHDGDAD RCLAIDASGR TVDGDQIMAI LALGMKERGK LRDDTLVATV MSNLGLKLAM 310 320 330 340 350 360 REAGVRVVET AVGDRYVLEE MNGHGYSLGG EQSGHVIMSD FATTGDGILT GLHLLSEMAR 370 380 390 400 410 420 QRKTLAELAQ AMTVYPQVMV NVRGVDHHSV HSDELLRSAV EAVEAALGDS GRVLLRPSGT 430 440 450 EPLVRVMVEA ADQETAVRMA NELADVVRER LAG

References

[1]

"The genome sequence of the Gram-positive sugarcane pathogen Leifsonia xyli subsp. xyli." Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., Kitajima J.P., Truffi D., do Amaral A.M., Harakava R., de Oliveira J.C.F., Wood D., de Oliveira M.C., Miyaki C.Y., Takita M.A., da Silva A.C.R., Furlan L.R., Carraro D.M., Camarotte G., Almeida N.F. Jr., Carrer H. , Coutinho L.L., El-Dorry H.A., Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S., Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F., Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A., Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C. Mol. Plant Microbe Interact. 17:827-836(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CTCB07.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016822 Genomic DNA. Translation: AAT89716.1.
RefSeq	YP_062821.1. NC_006087.1.
3D structure databases
ProteinModelPortal	Q6AD28.
ModBase	Search...
Protein-protein interaction databases
STRING	281090.Lxx20010.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAT89716; AAT89716; Lxx20010.
GeneID	2938565.
KEGG	lxx:Lxx20010.
PATRIC	22337678. VBILeiXyl11655_2076.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1109.
HOGENOM	HOG000268678.
KO	K03431.
OMA	KVIAIGC.
ProtClustDB	PRK14318.
Enzyme and pathway databases
BioCyc	LXYL281090:GH0X-1888-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_LEIXX

Accession

Primary (citable) accession number: Q6AD28

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	September 13, 2004
Last modified:	May 29, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program