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Protein

Phosphoglucosamine mutase

Gene

glmM

Organism
Staphylococcus aureus (strain bovine RF122 / ET3-1)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.UniRule annotation

Catalytic activityi

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei102 – 1021Phosphoserine intermediateUniRule annotation
Metal bindingi102 – 1021Magnesium; via phosphate groupUniRule annotation
Metal bindingi242 – 2421MagnesiumUniRule annotation
Metal bindingi244 – 2441MagnesiumUniRule annotation
Metal bindingi246 – 2461MagnesiumUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciSAUR273036:GJVS-2106-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglucosamine mutaseUniRule annotation (EC:5.4.2.10UniRule annotation)
Gene namesi
Name:glmMUniRule annotation
Ordered Locus Names:SAB2041c
OrganismiStaphylococcus aureus (strain bovine RF122 / ET3-1)
Taxonomic identifieri273036 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Phosphoglucosamine mutasePRO_0000301384Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021PhosphoserineUniRule annotation

Post-translational modificationi

Activated by phosphorylation.UniRule annotation

Keywords - PTMi

Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliQ2YYE6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphohexose mutase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000268678.
KOiK03431.
OMAiNSHCDGR.

Family and domain databases

CDDicd05802. GlmM. 1 hit.
Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
HAMAPiMF_01554_B. GlmM_B. 1 hit.
InterProiIPR005844. 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_bact.
[Graphical view]
PfamiPF02878. 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]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
TIGRFAMsiTIGR01455. glmM. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2YYE6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKYFGTDGV RGVANQELTP ELAFKLGRYG GYVLAHNKGE KHPRVLVGRD
60 70 80 90 100
TRVSGEMLES ALIAGLISIG AEVMRLGIIS TPGVAYLTRD MGAELGVMIS
110 120 130 140 150
ASHNPVADNG IKFFGSDGFK LSDEQENEIE ALLDQENPEL PRPVGNDIVH
160 170 180 190 200
YSDYFEGAQK YLSYLKSTVD VNFEGLKIVL DGANGSTSSL APFLFGDLEA
210 220 230 240 250
DTETIGCSPD GYNINEKCGS THPEKLAEKV VETESDFGLA FDGDGDRIIA
260 270 280 290 300
VDENGQIVDG DQIMFIIGQE MHKNQELNND MIVSTVMSNL GFYKALEQEG
310 320 330 340 350
IKSNKTKVGD RYVVEEMRRG NYNLGGEQSG HIVMMDYNTT GDGLLTGIQL
360 370 380 390 400
ASVIKMTGKS LSELAGQMKK YPQSLINVRV TDKYRVEENV DVKEVMTKVE
410 420 430 440 450
VEMNGEGRIL VRPSGTEPLV RVMVEAATDE DAERYAQQIA DVVQDKMGLD

K
Length:451
Mass (Da):49,310
Last modified:December 20, 2005 - v1
Checksum:iB15FDC90CA7F9CD8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ938182 Genomic DNA. Translation: CAI81730.1.
RefSeqiWP_000521496.1. NC_007622.1.

Genome annotation databases

EnsemblBacteriaiCAI81730; CAI81730; SAB2041c.
KEGGisab:SAB2041c.
PATRICi19525091. VBIStaAur92441_2150.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ938182 Genomic DNA. Translation: CAI81730.1.
RefSeqiWP_000521496.1. NC_007622.1.

3D structure databases

ProteinModelPortaliQ2YYE6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAI81730; CAI81730; SAB2041c.
KEGGisab:SAB2041c.
PATRICi19525091. VBIStaAur92441_2150.

Phylogenomic databases

HOGENOMiHOG000268678.
KOiK03431.
OMAiNSHCDGR.

Enzyme and pathway databases

BioCyciSAUR273036:GJVS-2106-MONOMER.

Family and domain databases

CDDicd05802. GlmM. 1 hit.
Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
HAMAPiMF_01554_B. GlmM_B. 1 hit.
InterProiIPR005844. 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_bact.
[Graphical view]
PfamiPF02878. 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]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
TIGRFAMsiTIGR01455. glmM. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGLMM_STAAB
AccessioniPrimary (citable) accession number: Q2YYE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: December 20, 2005
Last modified: September 7, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.