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Protein

Phosphoglucosamine mutase

Gene

glmM

Organism
Escherichia coli (strain SE11)
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 sitei102 – 1021Phosphoserine intermediateUniRule annotation
Metal bindingi102 – 1021Magnesium; via phosphate groupUniRule annotation
Metal bindingi241 – 2411MagnesiumUniRule annotation
Metal bindingi243 – 2431MagnesiumUniRule annotation
Metal bindingi245 – 2451MagnesiumUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciECOL409438:GHUU-3520-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglucosamine mutaseUniRule annotation (EC:5.4.2.10UniRule annotation)
Gene namesi
Name:glmMUniRule annotation
Ordered Locus Names:ECSE_3460
OrganismiEscherichia coli (strain SE11)
Taxonomic identifieri409438 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000008199 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445Phosphoglucosamine mutasePRO_1000201091Add
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

Proteomic databases

PRIDEiB6I1P9.

Structurei

3D structure databases

ProteinModelPortaliB6I1P9.
SMRiB6I1P9. Positions 5-444.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphohexose mutase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000268678.
KOiK03431.
OMAiNSHCDGR.
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.

B6I1P9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNRKYFGTD GIRGRVGDAP ITPDFVLKLG WAAGKVLARH GSRKIIIGKD
60 70 80 90 100
TRISGYMLES ALEAGLAAAG LSALFTGPMP TPAVAYLTRT FRAEAGIVIS
110 120 130 140 150
ASHNPFYDNG IKFFSIDGTK LPDAVEEAIE AEMEKEISCV DSAELGKASR
160 170 180 190 200
IVDAAGRYIE FCKATFPNEL SLSELKIVVD CANGATYHIA PNVLRELGAN
210 220 230 240 250
VIAIGCEPNG VNINAEVGAT DVRALQARVL AEKADLGIAF DGDGDRVIMV
260 270 280 290 300
DHEGNKVDGD QIMYIIAREG LRQGQLRGGA VGTLMSNMGL ELALKQLGIP
310 320 330 340 350
FARAKVGDRY VLEKMQEKGW RIGAENSGHV ILLDKTTTGD GIVAGLQVLA
360 370 380 390 400
AMARNHMSLH DLCSGMKMFP QILVNVRYTA GSGDPLEHES VKAVTAEVEA
410 420 430 440
ALGNRGRVLL RKSGTEPLIR VMVEGEDEAQ VTEFAHRIAD AVKAV
Length:445
Mass (Da):47,544
Last modified:December 16, 2008 - v1
Checksum:iECDF9A0378A980EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009240 Genomic DNA. Translation: BAG78984.1.
RefSeqiWP_000071134.1. NC_011415.1.

Genome annotation databases

EnsemblBacteriaiBAG78984; BAG78984; ECSE_3460.
KEGGiecy:ECSE_3460.
PATRICi18425538. VBIEscCol83070_3629.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009240 Genomic DNA. Translation: BAG78984.1.
RefSeqiWP_000071134.1. NC_011415.1.

3D structure databases

ProteinModelPortaliB6I1P9.
SMRiB6I1P9. Positions 5-444.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiB6I1P9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAG78984; BAG78984; ECSE_3460.
KEGGiecy:ECSE_3460.
PATRICi18425538. VBIEscCol83070_3629.

Phylogenomic databases

HOGENOMiHOG000268678.
KOiK03431.
OMAiNSHCDGR.
OrthoDBiEOG6TN467.

Enzyme and pathway databases

BioCyciECOL409438:GHUU-3520-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. "Complete genome sequence and comparative analysis of the wild-type commensal Escherichia coli strain SE11 isolated from a healthy adult."
    Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.
    DNA Res. 15:375-386(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SE11.

Entry informationi

Entry nameiGLMM_ECOSE
AccessioniPrimary (citable) accession number: B6I1P9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: December 16, 2008
Last modified: November 11, 2015
This is version 51 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.