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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei101 – 1011Phosphoserine intermediateUniRule annotation
Metal bindingi101 – 1011Magnesium; via phosphate groupUniRule annotation
Metal bindingi239 – 2391MagnesiumUniRule annotation
Metal bindingi241 – 2411MagnesiumUniRule annotation
Metal bindingi243 – 2431MagnesiumUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciFTUL177416:GNBP-80-MONOMER.

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443Phosphoglucosamine mutasePRO_0000147890Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011PhosphoserineUniRule annotation

Post-translational modificationi

Activated by phosphorylation.UniRule annotation

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi177416.FTT_0079.

Structurei

Secondary structure

1
443
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 2014Combined sources
Helixi21 – 3717Combined sources
Beta strandi42 – 487Combined sources
Helixi54 – 6815Combined sources
Beta strandi71 – 777Combined sources
Helixi80 – 8910Combined sources
Beta strandi93 – 986Combined sources
Beta strandi107 – 1148Combined sources
Helixi122 – 13211Combined sources
Beta strandi147 – 1493Combined sources
Turni151 – 1544Combined sources
Helixi155 – 16511Combined sources
Turni166 – 1683Combined sources
Beta strandi173 – 1786Combined sources
Turni183 – 1864Combined sources
Helixi187 – 1948Combined sources
Beta strandi198 – 2036Combined sources
Turni211 – 2144Combined sources
Helixi220 – 23011Combined sources
Beta strandi233 – 2386Combined sources
Beta strandi244 – 2485Combined sources
Helixi257 – 26610Combined sources
Turni267 – 2726Combined sources
Beta strandi277 – 2804Combined sources
Helixi285 – 2939Combined sources
Beta strandi298 – 3047Combined sources
Helixi307 – 3159Combined sources
Beta strandi319 – 3213Combined sources
Beta strandi325 – 3295Combined sources
Turni330 – 3323Combined sources
Helixi338 – 34811Combined sources
Turni349 – 3513Combined sources
Helixi356 – 3583Combined sources
Beta strandi367 – 3748Combined sources
Helixi381 – 3855Combined sources
Helixi388 – 39811Combined sources
Helixi399 – 4013Combined sources
Beta strandi402 – 4098Combined sources
Beta strandi412 – 42312Combined sources
Helixi424 – 44118Combined sources

3D structure databases

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

Enzyme and pathway databases

BioCyciFTUL177416:GNBP-80-MONOMER.

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: September 7, 2016
This is version 69 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.