Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphoglucosamine mutase

Gene

glmM

Organism
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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 sitei101Phosphoserine intermediateUniRule annotation1
Metal bindingi101Magnesium; via phosphate groupUniRule annotation1
Metal bindingi239MagnesiumUniRule annotation1
Metal bindingi241MagnesiumUniRule annotation1
Metal bindingi243MagnesiumUniRule 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:FTT_0079
OrganismiFrancisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Taxonomic identifieri177416 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
Proteomesi
  • UP000001174 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001478901 – 443Phosphoglucosamine mutaseAdd BLAST443

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei101PhosphoserineUniRule annotation1

Post-translational modificationi

Activated by phosphorylation.UniRule annotation

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi177416.FTT_0079.

Structurei

Secondary structure

1443
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 20Combined sources14
Helixi21 – 37Combined sources17
Beta strandi42 – 48Combined sources7
Helixi54 – 68Combined sources15
Beta strandi71 – 77Combined sources7
Helixi80 – 89Combined sources10
Beta strandi93 – 98Combined sources6
Beta strandi107 – 114Combined sources8
Helixi122 – 132Combined sources11
Beta strandi147 – 149Combined sources3
Turni151 – 154Combined sources4
Helixi155 – 165Combined sources11
Turni166 – 168Combined sources3
Beta strandi173 – 178Combined sources6
Turni183 – 186Combined sources4
Helixi187 – 194Combined sources8
Beta strandi198 – 203Combined sources6
Turni211 – 214Combined sources4
Helixi220 – 230Combined sources11
Beta strandi233 – 238Combined sources6
Beta strandi244 – 248Combined sources5
Helixi257 – 266Combined sources10
Turni267 – 272Combined sources6
Beta strandi277 – 280Combined sources4
Helixi285 – 293Combined sources9
Beta strandi298 – 304Combined sources7
Helixi307 – 315Combined sources9
Beta strandi319 – 321Combined sources3
Beta strandi325 – 329Combined sources5
Turni330 – 332Combined sources3
Helixi338 – 348Combined sources11
Turni349 – 351Combined sources3
Helixi356 – 358Combined sources3
Beta strandi367 – 374Combined sources8
Helixi381 – 385Combined sources5
Helixi388 – 398Combined sources11
Helixi399 – 401Combined sources3
Beta strandi402 – 409Combined sources8
Beta strandi412 – 423Combined sources12
Helixi424 – 441Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3I3WX-ray2.30A/B1-443[»]
ProteinModelPortaliQ5NII8.
SMRiQ5NII8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5NII8.

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphohexose mutase family.UniRule annotation

Phylogenomic databases

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

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.
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.

Sequencei

Sequence statusi: Complete.

Q5NII8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKYFGTDGI RGEVANSTIT VEFTQKLGNA VGSLINQKNY PKFVIVGQDT
60 70 80 90 100
RSSGGFLKFA LVSGLNAAGI DVLDLGVVPT PVVAFMTVKH RAAAGFVITA
110 120 130 140 150
SHNKFTDNGI KLFSSNGFKL DDALEEEVED MIDGDFIYQP QFKFGSYKIL
160 170 180 190 200
ANAIDEYIES IYSRFAKFVN YKGKVVVDCA HGAASHNFEA LLDKFGINYV
210 220 230 240 250
SIASNPDGLN INVGCGATCV SNIKKAVKEQ KADLGISLDG DADRIIIVDE
260 270 280 290 300
NGQEIDGDGI LNILAQYSDI CGGTNGIVGT QMTNMSYENH YRANKIPFIR
310 320 330 340 350
SKVGDRYVLE DLVKYGYKIG GESSGHVINL NFGTTGDGLF TAIQLLAIFS
360 370 380 390 400
QADKPVSEFK LQGELMQQTL INVPLTKKVA REDLQKVASD VNDVEKRLGN
410 420 430 440
RGRVLLRPSG TEPVLRVMVE ADDKSLATNE AEYLVEKVKQ KLV
Length:443
Mass (Da):48,185
Last modified:February 1, 2005 - v1
Checksum:i8EE0B69868BDEECE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA. Translation: CAG44712.1.
RefSeqiWP_003019799.1. NZ_CP010290.1.
YP_169154.1. NC_006570.2.

Genome annotation databases

EnsemblBacteriaiCAG44712; CAG44712; FTT_0079.
GeneIDi3191618.
KEGGiftu:FTT_0079.
PATRICi17963117. VBIFraTul2086_0085.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA. Translation: CAG44712.1.
RefSeqiWP_003019799.1. NZ_CP010290.1.
YP_169154.1. NC_006570.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3I3WX-ray2.30A/B1-443[»]
ProteinModelPortaliQ5NII8.
SMRiQ5NII8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi177416.FTT_0079.

Protocols and materials databases

DNASUi3191618.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG44712; CAG44712; FTT_0079.
GeneIDi3191618.
KEGGiftu:FTT_0079.
PATRICi17963117. VBIFraTul2086_0085.

Phylogenomic databases

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

Miscellaneous databases

EvolutionaryTraceiQ5NII8.

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.
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.
ProtoNetiSearch...

Entry informationi

Entry nameiGLMM_FRATT
AccessioniPrimary (citable) accession number: Q5NII8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 1, 2005
Last modified: November 2, 2016
This is version 70 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.