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Protein

Phosphoglucosamine mutase

Gene

glmM

Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
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)DescriptionActionsGraphical viewLength
Active sitei104Phosphoserine intermediateUniRule annotation1
Metal bindingi104Magnesium; via phosphate groupUniRule annotation1
Metal bindingi243MagnesiumUniRule annotation1
Metal bindingi245MagnesiumUniRule annotation1
Metal bindingi247MagnesiumUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglucosamine mutaseUniRule annotation (EC:5.4.2.10UniRule annotation)
Gene namesi
Name:glmMUniRule annotation
Ordered Locus Names:CE0588
OrganismiCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Taxonomic identifieri196164 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000001409 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001478781 – 447Phosphoglucosamine mutaseAdd BLAST447

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei104PhosphoserineUniRule annotation1

Post-translational modificationi

Activated by phosphorylation.UniRule annotation

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi196164.HMPREF0290_1143.

Structurei

3D structure databases

ProteinModelPortaliQ8FS18.
SMRiQ8FS18.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphohexose mutase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107QJF. Bacteria.
COG1109. LUCA.
HOGENOMiHOG000268678.
KOiK03431.
OrthoDBiPOG091H02H5.

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.

Q8FS18-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRLFGTDGV RGLANKTLTA PLALKLGAAA AHVLTAGTRP HGRRPVAIVG
60 70 80 90 100
RDPRVSGEML AAALAAGMAS RGVDVLRVGV IPTPGVAFLT DDYGADMGVM
110 120 130 140 150
ISASHNPMPD NGIKFFSAGG HKLPDEVEDE IERVMDDLPE EGPTGHGIGR
160 170 180 190 200
VIEEAPDARG RYLQHLADAV PTDLSGITVV VDAANGAASV IAPQAYEAAG
210 220 230 240 250
AKVIAIHNTP NAYNINEKCG STHMDQIQAA VLEHGADLGL AHDGDADRCL
260 270 280 290 300
AVDSDGNIVD GDQIMAILAI AMKENSELRK NTLVATVMSN LGLKLAMEKA
310 320 330 340 350
DIQLRTTKVG DRYVLEELNA GGFALGGEQS GHIVLPDHGT TGDGTLTGLS
360 370 380 390 400
LMARMAATGK PLSELAAAMT VLPQVLINVP VADKSSIMKS ANVQAAVAAA
410 420 430 440
EEELGGTGRV LLRPSGTEEL FRVMVEAAEQ EQARRVAGRL AAVVAEA
Length:447
Mass (Da):46,304
Last modified:December 20, 2005 - v2
Checksum:i801CBE0ED537B6D2
GO

Sequence cautioni

The sequence BAC17398 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC17398.1. Different initiation.
RefSeqiWP_035109753.1. NZ_GG700687.1.

Genome annotation databases

EnsemblBacteriaiBAC17398; BAC17398; BAC17398.
KEGGicef:CE0588.
PATRICi21487348. VBICorEff9312_0616.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000035 Genomic DNA. Translation: BAC17398.1. Different initiation.
RefSeqiWP_035109753.1. NZ_GG700687.1.

3D structure databases

ProteinModelPortaliQ8FS18.
SMRiQ8FS18.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196164.HMPREF0290_1143.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC17398; BAC17398; BAC17398.
KEGGicef:CE0588.
PATRICi21487348. VBICorEff9312_0616.

Phylogenomic databases

eggNOGiENOG4107QJF. Bacteria.
COG1109. LUCA.
HOGENOMiHOG000268678.
KOiK03431.
OrthoDBiPOG091H02H5.

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_COREF
AccessioniPrimary (citable) accession number: Q8FS18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: November 2, 2016
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference 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.