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Protein

Phosphoglucosamine mutase

Gene

glmM

Organism
Rhodococcus opacus (strain B4)
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

BioCyciROPA632772:GH0Q-6278-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglucosamine mutaseUniRule annotation (EC:5.4.2.10UniRule annotation)
Gene namesi
Name:glmMUniRule annotation
Ordered Locus Names:ROP_62320
OrganismiRhodococcus opacus (strain B4)
Taxonomic identifieri632772 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesNocardiaceaeRhodococcus
Proteomesi
  • UP000002212 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445Phosphoglucosamine mutasePRO_1000185379Add
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

Interactioni

Protein-protein interaction databases

STRINGi632772.ROP_62320.

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphohexose mutase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107QJF. Bacteria.
COG1109. LUCA.
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.

C1B058-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRLFGTDGV RGLANTELTA ELALQVASAA ATVLASPGSG GRKTAVVGRD
60 70 80 90 100
PRASGEMLEA AVVAGLTSAG VDVLNVGVLP TPAVAFLTAE LDAALGVMIS
110 120 130 140 150
ASHNPMPDNG IKIFAAGGHK LDDEVEDRIE SVATGTATRR APTGAGIGRV
160 170 180 190 200
HTVPDAADRY LQHLTTALPN RLDGLTVVVD CAHGAASDVA PAAYRAAGAT
210 220 230 240 250
VVAINAEPDG LNINENCGST HLEGLQKAVV RHGADLGLAH DGDADRCLAV
260 270 280 290 300
DAGGSLVDGD AIMTVLALGM RDAGELVDDT LVATVMSNLG LHIAMREAGI
310 320 330 340 350
SLVTTAVGDR YVLEGLRSGG FSLGGEQSGH VVFPAFGTTG DGVLTGLRLM
360 370 380 390 400
GRMAETGQPI AELASAMTTL PQVLVNVKVA DKRAVAASPV VLDAVLAAER
410 420 430 440
SLGENGRVLL RPSGTEQLVR VMVEASDLEV ARKLADELAG TVASV
Length:445
Mass (Da):45,066
Last modified:May 26, 2009 - v1
Checksum:iAFA7E148E13901A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP011115 Genomic DNA. Translation: BAH54479.1.
RefSeqiWP_015889942.1. NC_012522.1.

Genome annotation databases

EnsemblBacteriaiBAH54479; BAH54479; ROP_62320.
KEGGirop:ROP_62320.
PATRICi23229861. VBIRhoOpa21106_6299.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP011115 Genomic DNA. Translation: BAH54479.1.
RefSeqiWP_015889942.1. NC_012522.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi632772.ROP_62320.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAH54479; BAH54479; ROP_62320.
KEGGirop:ROP_62320.
PATRICi23229861. VBIRhoOpa21106_6299.

Phylogenomic databases

eggNOGiENOG4107QJF. Bacteria.
COG1109. LUCA.
HOGENOMiHOG000268678.
KOiK03431.
OMAiFNLGGEQ.
OrthoDBiEOG6TN467.

Enzyme and pathway databases

BioCyciROPA632772:GH0Q-6278-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. "Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
    Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
    Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B4.

Entry informationi

Entry nameiGLMM_RHOOB
AccessioniPrimary (citable) accession number: C1B058
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: November 11, 2015
This is version 47 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.