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Protein

Phosphoglucosamine mutase

Gene

glmM

Organism
Corynebacterium glutamicum (strain R)
Status
Reviewed-Annotation score: Annotation score: 3 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 sitei104 – 1041Phosphoserine intermediateUniRule annotation
Metal bindingi104 – 1041Magnesium; via phosphate groupUniRule annotation
Metal bindingi243 – 2431MagnesiumUniRule annotation
Metal bindingi245 – 2451MagnesiumUniRule annotation
Metal bindingi247 – 2471MagnesiumUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciCGLU340322:GJBE-733-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglucosamine mutaseUniRule annotation (EC:5.4.2.10UniRule annotation)
Gene namesi
Name:glmMUniRule annotation
Ordered Locus Names:cgR_0701
OrganismiCorynebacterium glutamicum (strain R)
Taxonomic identifieri340322 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000006698 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447Phosphoglucosamine mutasePRO_0000301305Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei104 – 1041PhosphoserineUniRule annotation

Post-translational modificationi

Activated by phosphorylation.UniRule annotation

Keywords - PTMi

Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliA4QBS5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphohexose mutase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000268678.
KOiK03431.
OMAiFNLGGEQ.
OrthoDBiEOG6TN467.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
HAMAPiMF_01554_B. GlmM_B.
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.

A4QBS5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRLFGTDGV RGLANEVLTA PLALKLGAAA AHVLTAEKRV DGRRPVAIVG
60 70 80 90 100
RDPRVSGEML AAALSAGMAS QGVDVIRVGV IPTPAVAFLT DDYGADMGVM
110 120 130 140 150
ISASHNPMPD NGIKFFSAGG HKLPDHVEDE IERVMDSLPA EGPTGHGVGR
160 170 180 190 200
VIEEATDAQD RYLEHLKEAV PTSLEGIKIV VDAANGAASV VAPKAYEAAG
210 220 230 240 250
ATVIAIHNKP DSYNINMDCG STHIDQVQAA VLKHGADLGL AHDGDADRCL
260 270 280 290 300
AVDKDGNLID GDQIMAMLAI AMKENGELRK NTLVGTVMSN LGLKIAMDEA
310 320 330 340 350
GITLRTTKVG DRYVLEDLNA GGFSLGGEQS GHIVLPDHGT TGDGTLTGLS
360 370 380 390 400
IMARMAETGK SLGELAQAMT VLPQVLINVP VSDKSTIVSH PSVVAAIAEA
410 420 430 440
EAELGSTGRV LLRASGTEEL FRVMVEAGDK EQARRIAGRL SAVVAEV
Length:447
Mass (Da):46,445
Last modified:May 15, 2007 - v1
Checksum:i935440E7BE929323
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009044 Genomic DNA. Translation: BAF53672.1.
RefSeqiWP_003854539.1. NC_009342.1.

Genome annotation databases

EnsemblBacteriaiBAF53672; BAF53672; cgR_0701.
KEGGicgt:cgR_0701.
PATRICi21505903. VBICorGlu58097_0726.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009044 Genomic DNA. Translation: BAF53672.1.
RefSeqiWP_003854539.1. NC_009342.1.

3D structure databases

ProteinModelPortaliA4QBS5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAF53672; BAF53672; cgR_0701.
KEGGicgt:cgR_0701.
PATRICi21505903. VBICorGlu58097_0726.

Phylogenomic databases

HOGENOMiHOG000268678.
KOiK03431.
OMAiFNLGGEQ.
OrthoDBiEOG6TN467.

Enzyme and pathway databases

BioCyciCGLU340322:GJBE-733-MONOMER.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
HAMAPiMF_01554_B. GlmM_B.
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...

Publicationsi

  1. "Comparative analysis of the Corynebacterium glutamicum group and complete genome sequence of strain R."
    Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M., Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.
    Microbiology 153:1042-1058(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: R.

Entry informationi

Entry nameiGLMM_CORGB
AccessioniPrimary (citable) accession number: A4QBS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 15, 2007
Last modified: December 9, 2015
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

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.