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Q031P2 (GLMM_LACLS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoglucosamine mutase

EC=5.4.2.10
Gene names
Name:glmM
Ordered Locus Names:LACR_0479
OrganismLactococcus lactis subsp. cremoris (strain SK11) [Complete proteome] [HAMAP]
Taxonomic identifier272622 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Protein existenceInferred 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
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionmagnesium ion binding

Inferred from electronic annotation. Source: HAMAP

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 452452Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_0000301332

Sites

Active site1011Phosphoserine intermediate By similarity
Metal binding1011Magnesium; via phosphate group By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity

Amino acid modifications

Modified residue1011Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q031P2 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: AA83AC15F8BE1136

FASTA45248,645
        10         20         30         40         50         60 
MGKYFGTDGV RGEANVELTP EMAFKLGRFG GYVLSQHELE TPKVYVGRDT RISGQMLASS 

        70         80         90        100        110        120 
LISGLLSVGI EVYDLGVIAT PGVAYLVKKD GASAGVMISA SHNPALDNGI KFFGGDGYKL 

       130        140        150        160        170        180 
EDEKELEIEA LIDAKEDTLP RPSAQGLGML HDYIEGVRKY QAFLKTTAEG DFEGYNVVLD 

       190        200        210        220        230        240 
TANGASYTSA RAVFADLKAN LTVIGENPDG LNINVKVGST HPEAMAKKVV ETGSDLGLAF 

       250        260        270        280        290        300 
DGDADRLIAV DENGEIVDGD KIMFIVGKYL LEQGKLAQDT LVTTVMSNLG FHLALEEAGI 

       310        320        330        340        350        360 
NSVITAVGDR YVVEEMKKNN YNFGGEQSGH MIFLDYNTTG DGQLSAIQLL KVMRETGKTL 

       370        380        390        400        410        420 
SELASEVTIY PQKLVNVRVK DNAAKKSAMD VPAIQKVISE METSMNGKGR ILVRPSGTEP 

       430        440        450 
LLRVMAEAPT HEQVEHVVDT IVEVVEAEIG VK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000425 Genomic DNA. Translation: ABJ72080.1.
RefSeqYP_808502.1. NC_008527.1.

3D structure databases

ProteinModelPortalQ031P2.
ModBaseSearch...

Protein-protein interaction databases

STRING272622.LACR_0479.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ72080; ABJ72080; LACR_0479.
GeneID4432382.
KEGGllc:LACR_0479.
PATRIC22287736. VBILacLac38071_0644.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMASGHIILF.
ProtClustDBPRK14316.

Enzyme and pathway databases

BioCycLLAC272622:GJUG-479-MONOMER.

Family and domain databases

Gene3D3.40.120.10. 3 hits.
HAMAPMF_01554_B. GlmM_B.
InterProIPR005844. 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]
PfamPF02878. 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]
PRINTSPR00509. PGMPMM.
SUPFAMSSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
TIGRFAMsTIGR01455. glmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_LACLS
AccessionPrimary (citable) accession number: Q031P2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: November 14, 2006
Last modified: May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families