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Protein

Glutamine--fructose-6-phosphate aminotransferase [isomerizing]

Gene

glmS

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 first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.UniRule annotation

Catalytic activityi

L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei2Nucleophile; for GATase activityUniRule annotation1
Active sitei607For Fru-6P isomerization activityUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Protein family/group databases

MEROPSiC44.971.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]UniRule annotation (EC:2.6.1.16UniRule annotation)
Alternative name(s):
D-fructose-6-phosphate amidotransferaseUniRule annotation
GFATUniRule annotation
Glucosamine-6-phosphate synthaseUniRule annotation
Hexosephosphate aminotransferaseUniRule annotation
L-glutamine--D-fructose-6-phosphate amidotransferaseUniRule annotation
Gene namesi
Name:glmSUniRule annotation
Ordered Locus Names:FTT_0388
OrganismiFrancisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Taxonomic identifieri177416 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
Proteomesi
  • UP000001174 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedUniRule annotation
ChainiPRO_00001353322 – 612Glutamine--fructose-6-phosphate aminotransferase [isomerizing]Add BLAST611

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

IntActiQ5NHQ9. 2 interactors.
STRINGi177416.FTT_0388.

Structurei

Secondary structure

1612
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi253 – 259Combined sources7
Helixi261 – 270Combined sources10
Helixi280 – 282Combined sources3
Helixi287 – 292Combined sources6
Beta strandi296 – 301Combined sources6
Helixi303 – 318Combined sources16
Beta strandi324 – 328Combined sources5
Helixi329 – 332Combined sources4
Beta strandi343 – 352Combined sources10
Helixi355 – 364Combined sources10
Turni365 – 368Combined sources4
Beta strandi369 – 381Combined sources13
Helixi382 – 386Combined sources5
Beta strandi387 – 392Combined sources6
Beta strandi400 – 402Combined sources3
Helixi405 – 424Combined sources20
Helixi430 – 441Combined sources12
Helixi443 – 451Combined sources9
Helixi454 – 461Combined sources8
Helixi462 – 464Combined sources3
Beta strandi469 – 474Combined sources6
Helixi478 – 493Combined sources16
Beta strandi496 – 501Combined sources6
Helixi502 – 504Combined sources3
Turni505 – 512Combined sources8
Beta strandi518 – 523Combined sources6
Helixi529 – 541Combined sources13
Beta strandi545 – 551Combined sources7
Helixi552 – 557Combined sources6
Beta strandi564 – 568Combined sources5
Helixi575 – 595Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TBFX-ray2.28A/B/C/D/E/F/G/H241-612[»]
ProteinModelPortaliQ5NHQ9.
SMRiQ5NHQ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 219Glutamine amidotransferase type-2UniRule annotationAdd BLAST218
Domaini287 – 427SIS 1UniRule annotationAdd BLAST141
Domaini460 – 602SIS 2UniRule annotationAdd BLAST143

Sequence similaritiesi

Contains 1 glutamine amidotransferase type-2 domain.UniRule annotation
Contains 2 SIS domains.UniRule annotation

Keywords - Domaini

Glutamine amidotransferase, Repeat

Phylogenomic databases

eggNOGiENOG4105C46. Bacteria.
COG0449. LUCA.
HOGENOMiHOG000258896.
KOiK00820.
OMAiGEFFCAS.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_00164. GlmS. 1 hit.
InterProiIPR017932. GATase_2_dom.
IPR005855. GlmS_trans.
IPR029055. Ntn_hydrolases_N.
IPR001347. SIS.
[Graphical view]
PANTHERiPTHR10937:SF0. PTHR10937:SF0. 1 hit.
PfamiPF01380. SIS. 2 hits.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01135. glmS. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
PS51464. SIS. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5NHQ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCGIVGANST RNVTNILIEG LKKLEYRGYD SAGLAIIDDK NNIDICKEVG
60 70 80 90 100
KVIELEKSVH NLANFKGDIG IAHTRWATHG KPSKNNSHPH ASESFCIVHN
110 120 130 140 150
GVIENFAELK KVLINDGYKF KSDTDTEVIA HLLQKEWRDN FSIVDNIKYI
160 170 180 190 200
MAMLKGAYAV AIISQKFSDK IVAVRSGSPL VIGVGIDENF ISSDALSLLP
210 220 230 240 250
VTNKFSYLDE GDIAIISKDN VEVFDNNGAA KNLEVEEYNY SSSSASKDGY
260 270 280 290 300
KHYMLKEIYE QPEAVSNTIL ASLADGEISL DSFDKRAKEL FEKTKHICIV
310 320 330 340 350
ACGTSYNAGM TAKYWIEKYA KVPCSVEIAS EIRYRDNVVV DGSLFVSISQ
360 370 380 390 400
SGETADTLES LRKSKKQNYV GSMCICNVPN SSLVRESDIA FMTKAGVEIG
410 420 430 440 450
VASTKAFTTQ LVALAIFTLV IAKLKNSLTD QQIAKYTEEL KNIRALVMGA
460 470 480 490 500
LKLDTEIDQI SEYFSDKEHT IFLGRGLYYP IAIEGALKLK EISYIHAEAY
510 520 530 540 550
PSGELKHGPL ALVDKNMPIV AVVPNDELLD KTLSNLQEVH ARGGKLILFV
560 570 580 590 600
DKAVKERVNF DNSIVLELDA GHDFSAPVVF TIPLQLLSYH VAIIKGTDVD
610
QPRNLAKSVT VE
Length:612
Mass (Da):67,444
Last modified:January 23, 2007 - v3
Checksum:i5B358856A65E7245
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA. Translation: CAG45021.1.
RefSeqiWP_003020072.1. NZ_CP010290.1.
YP_169433.1. NC_006570.2.

Genome annotation databases

EnsemblBacteriaiCAG45021; CAG45021; FTT_0388.
GeneIDi3192352.
KEGGiftu:FTT_0388.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA. Translation: CAG45021.1.
RefSeqiWP_003020072.1. NZ_CP010290.1.
YP_169433.1. NC_006570.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TBFX-ray2.28A/B/C/D/E/F/G/H241-612[»]
ProteinModelPortaliQ5NHQ9.
SMRiQ5NHQ9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5NHQ9. 2 interactors.
STRINGi177416.FTT_0388.

Protein family/group databases

MEROPSiC44.971.

Protocols and materials databases

DNASUi3192352.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG45021; CAG45021; FTT_0388.
GeneIDi3192352.
KEGGiftu:FTT_0388.

Phylogenomic databases

eggNOGiENOG4105C46. Bacteria.
COG0449. LUCA.
HOGENOMiHOG000258896.
KOiK00820.
OMAiGEFFCAS.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_00164. GlmS. 1 hit.
InterProiIPR017932. GATase_2_dom.
IPR005855. GlmS_trans.
IPR029055. Ntn_hydrolases_N.
IPR001347. SIS.
[Graphical view]
PANTHERiPTHR10937:SF0. PTHR10937:SF0. 1 hit.
PfamiPF01380. SIS. 2 hits.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01135. glmS. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
PS51464. SIS. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGLMS_FRATT
AccessioniPrimary (citable) accession number: Q5NHQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 86 of the entry and version 3 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.