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Protein

Probable phosphoglucosamine mutase

Gene

glmM

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
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 sitei96Phosphoserine intermediateUniRule annotation1
Metal bindingi96Magnesium; via phosphate groupUniRule annotation1
Metal bindingi233MagnesiumUniRule annotation1
Metal bindingi235MagnesiumUniRule annotation1
Metal bindingi237MagnesiumUniRule 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:
Probable phosphoglucosamine mutaseUniRule annotation (EC:5.4.2.10UniRule annotation)
Gene namesi
Name:glmMUniRule annotation
Ordered Locus Names:PH1210
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003378241 – 451Probable phosphoglucosamine mutaseAdd BLAST451

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei96PhosphoserineUniRule annotation1

Post-translational modificationi

Activated by phosphorylation.UniRule annotation

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiO58973.

Interactioni

Protein-protein interaction databases

STRINGi70601.PH1210.

Structurei

3D structure databases

ProteinModelPortaliO58973.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphohexose mutase family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG00767. Archaea.
COG1109. LUCA.
HOGENOMiHOG000268680.
KOiK03431.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
HAMAPiMF_01554_A. GlmM_A. 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.
IPR023666. GlmM_arc.
IPR024086. GlmM_arc-type.
[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.
TIGRFAMsiTIGR03990. Arch_GlmM. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O58973-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRYFGTSGI REVVNEKLTP ELALKVGLAL GTYLQEGKVV IGCDTRTSSV
60 70 80 90 100
MLKNAVISGL LATGIDVIDI GLAPTPLTGF AIRLYNAEAG VTITASHNPP
110 120 130 140 150
QYNGIKVWDR DGMAYTPDKE HELEKIIESG NFRRVPWNEV GTLKTANPRK
160 170 180 190 200
EYIEAILREI NLKGSYTVVI DAGNGAGSIV SPYLHRELGN RVITLNSDPS
210 220 230 240 250
GFFVRELEPN KESLSMLEKT VKVLNADIGI AHDGDADRVG VVDENGEFVE
260 270 280 290 300
YEVMLSLIAG YMLKKYGKGK IVTTVDAGFA LDDYIRELGG EVVRTRVGDV
310 320 330 340 350
AVAEELVKHG GVFGGEPSGT WIMPQWNLTP DGIFASALVL EMIDRLGPIG
360 370 380 390 400
ELAKDVPKYV TLRKKIPCSN ELKNKVMNKI ADLIPREFSY ERIITIDGIR
410 420 430 440 450
IENDDWWILF RPSGTEPIMR ITLEAHTEEM AERLMKKAEN LVKSVIKDLS

S
Length:451
Mass (Da):49,721
Last modified:June 10, 2008 - v2
Checksum:i0DF52E8A8B2A7B2E
GO

Sequence cautioni

The sequence BAA30310 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30310.1. Different initiation.
PIRiD71064.
RefSeqiWP_048053334.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA30310; BAA30310; BAA30310.
GeneIDi1443531.
KEGGipho:PH1210.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30310.1. Different initiation.
PIRiD71064.
RefSeqiWP_048053334.1. NC_000961.1.

3D structure databases

ProteinModelPortaliO58973.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH1210.

Proteomic databases

PRIDEiO58973.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA30310; BAA30310; BAA30310.
GeneIDi1443531.
KEGGipho:PH1210.

Phylogenomic databases

eggNOGiarCOG00767. Archaea.
COG1109. LUCA.
HOGENOMiHOG000268680.
KOiK03431.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
HAMAPiMF_01554_A. GlmM_A. 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.
IPR023666. GlmM_arc.
IPR024086. GlmM_arc-type.
[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.
TIGRFAMsiTIGR03990. Arch_GlmM. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGLMM_PYRHO
AccessioniPrimary (citable) accession number: O58973
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: November 2, 2016
This is version 93 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

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.