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Q890U2 (GLMS_CLOTE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]

EC=2.6.1.16
Alternative name(s):
D-fructose-6-phosphate amidotransferase
GFAT
Glucosamine-6-phosphate synthase
Hexosephosphate aminotransferase
L-glutamine--D-fructose-6-phosphate amidotransferase
Gene names
Name:glmS
Ordered Locus Names:CTC_02543
OrganismClostridium tetani (strain Massachusetts / E88) [Complete proteome] [HAMAP]
Taxonomic identifier212717 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length608 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source By similarity. HAMAP-Rule MF_00164

Catalytic activity

L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate. HAMAP-Rule MF_00164

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00164

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00164.

Sequence similarities

Contains 1 glutamine amidotransferase type-2 domain.

Contains 2 SIS domains.

Sequence caution

The sequence AAO37003.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 608607Glutamine--fructose-6-phosphate aminotransferase [isomerizing] HAMAP-Rule MF_00164
PRO_0000135324

Regions

Domain2 – 217216Glutamine amidotransferase type-2
Domain284 – 424141SIS 1
Domain453 – 598146SIS 2

Sites

Active site21Nucleophile; for GATase activity By similarity
Active site6031For Fru-6P isomerization activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q890U2 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 01F969978DE4D07E

FASTA60867,826
        10         20         30         40         50         60 
MCGIVGYIGK KEAAPILVEG LSKLEYRGYD SAGVAIIEDQ VIRTRKCKGR LVNLEEKLNE 

        70         80         90        100        110        120 
ESMIGDIGIG HTRWATHGEP SDKNSHPHNN EKGTISVVHN GIIENYIELR EWLTSEGYKF 

       130        140        150        160        170        180 
VSETDTEVLP HLIDYYYKGD LLEAVMTAIS KVEGSYAIGV VCSEEPDKVV AVRKDSPLIV 

       190        200        210        220        230        240 
GLGEEEYFIA SDIPAVLNHT RDIYLLKDNE FVLMTKDGVK LFDKEGKEIK REIYHVTWNA 

       250        260        270        280        290        300 
DAAEKGGYDH FMLKEIHEQP KVIKDTMTSR IMLGKDIKLD NIEISKEQME KINKIYIVAC 

       310        320        330        340        350        360 
GTAYHAGLVG KYTIEKLARI PVEVDIASEF RYKNPIIDKD TLMIVISQSG ETADTLAALR 

       370        380        390        400        410        420 
EAKKKGARVI AVTNVVGSSI SREADDILYT WAGPEIAVAS TKAYETQLVA MYILALYFAQ 

       430        440        450        460        470        480 
EKGTLNKEEL EELKEEMLSI PDKAEKCLET DEIMKKLASK THMKKDMFFL GRGLDYAVAL 

       490        500        510        520        530        540 
EGSLKLKEIS YIHSEAYAAG ELKHGPIALI EEGTIVITLA TQEELFDKTV SNIKEVTTRG 

       550        560        570        580        590        600 
AKAIGIAFEG QKNMDKAVEE AIYIPKTKSI FAPLLSVIPL QLYSYYVSLE KGCDVDKPRN 


LAKSVTVE 

« Hide

References

[1]"The genome sequence of Clostridium tetani, the causative agent of tetanus disease."
Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.
Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Massachusetts / E88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015927 Genomic DNA. Translation: AAO37003.1. Different initiation.
RefSeqNP_783066.1. NC_004557.1.

3D structure databases

ProteinModelPortalQ890U2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING212717.CTC02543.

Protein family/group databases

MEROPSC44.971.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO37003; AAO37003; CTC_02543.
GeneID1060148.
KEGGctc:CTC02543.
PATRIC19513205. VBICloTet101274_2633.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0449.
KOK00820.
OMALGIGENF.
OrthoDBEOG6KT2Q1.
ProtClustDBPRK00331.

Enzyme and pathway databases

BioCycCTET212717:GJAM-2350-MONOMER.

Family and domain databases

HAMAPMF_00164. GlmS.
InterProIPR017932. GATase_2_dom.
IPR005855. GlmS_trans.
IPR001347. SIS.
[Graphical view]
PANTHERPTHR10937:SF0. PTHR10937:SF0. 1 hit.
PfamPF01380. SIS. 2 hits.
[Graphical view]
TIGRFAMsTIGR01135. glmS. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
PS51464. SIS. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMS_CLOTE
AccessionPrimary (citable) accession number: Q890U2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families