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Protein

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

Gene

glmS

Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21Nucleophile; for GATase activityUniRule annotation
Active sitei599 – 5991For Fru-6P isomerization activityUniRule annotation

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. glutamine-fructose-6-phosphate transaminase (isomerizing) activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. carbohydrate biosynthetic process Source: InterPro
  2. glutamine metabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Enzyme and pathway databases

BioCyciSMUT210007:GC7Z-1126-MONOMER.

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:SMU_1187
OrganismiStreptococcus mutans serotype c (strain ATCC 700610 / UA159)
Taxonomic identifieri210007 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000002512: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedUniRule annotation
Chaini2 – 604603Glutamine--fructose-6-phosphate aminotransferase [isomerizing]PRO_0000135390Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi210007.SMU.1187.

Structurei

3D structure databases

ProteinModelPortaliQ8DTY0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 218217Glutamine amidotransferase type-2UniRule annotationAdd
BLAST
Domaini284 – 423140SIS 1UniRule annotationAdd
BLAST
Domaini456 – 594139SIS 2UniRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Glutamine amidotransferase, Repeat

Phylogenomic databases

eggNOGiCOG0449.
KOiK00820.
OMAiSEFRYAP.
OrthoDBiEOG6KT2Q1.
PhylomeDBiQ8DTY0.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_00164. GlmS.
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.

Q8DTY0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MCGIVGVVGN RNATDILMQG LEKLEYRGYD SAGIYVINQP ENGRLIKSVG
60 70 80 90 100
RIADLRAKIG IDVAGSTGIG HTRWATHGQA TEENAHPHAS ATGRLVLVHN
110 120 130 140 150
GVIENYLQIK ENYLAGHNLK GETDTEIAVH LIGQFVTDGL SVLESFKKAL
160 170 180 190 200
HIIEGSYAFA LIDSQNPDII YVAKNKSPLL IGLGEGYNMV CSDAMAMIRE
210 220 230 240 250
TNQFMEIHDK ELVVLTKDTA QVSDYDGNPV ERQAYTAELD LSDIGKGTYP
260 270 280 290 300
YYMLKEIDEQ PTVMRKLIST YANENGKLTV DPAIVKSVQE ADRIYILAAG
310 320 330 340 350
TSYNAGFASK SMIETLTDTP VELGIASEWG YNMPLLSKKP MFILLSQSGE
360 370 380 390 400
TADSRQVLVK ANAMGVPSLT ITNVPGSTLS REATYTMLLH AGPEIAVAST
410 420 430 440 450
KAYTAQIAAL AFLSKAVGEA NGKKEALEFD LVHELSIVAQ SIEASLSERE
460 470 480 490 500
VIEKKVANLL ATSRNAFYIG RGNDYYVAME ASLKLKEISY IQCEGFAAGE
510 520 530 540 550
LKHGTISLIE EGTPVLALIS SSETVAAHTR GNIQEVAARG ANVLTVVEEG
560 570 580 590 600
LNKEEDDVVV NQVHPYLSSI SMVIPTQLIA YYASLQRGLD VDKPRNLAKA

VTVE
Length:604
Mass (Da):65,421
Last modified:January 23, 2007 - v3
Checksum:iCD810381733F6455
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014133 Genomic DNA. Translation: AAN58876.1.
RefSeqiNP_721570.1. NC_004350.2.

Genome annotation databases

EnsemblBacteriaiAAN58876; AAN58876; SMU_1187.
GeneIDi1028487.
KEGGismu:SMU_1187.
PATRICi19664463. VBIStrMut61772_1064.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014133 Genomic DNA. Translation: AAN58876.1.
RefSeqiNP_721570.1. NC_004350.2.

3D structure databases

ProteinModelPortaliQ8DTY0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi210007.SMU.1187.

Protein family/group databases

MEROPSiC44.971.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN58876; AAN58876; SMU_1187.
GeneIDi1028487.
KEGGismu:SMU_1187.
PATRICi19664463. VBIStrMut61772_1064.

Phylogenomic databases

eggNOGiCOG0449.
KOiK00820.
OMAiSEFRYAP.
OrthoDBiEOG6KT2Q1.
PhylomeDBiQ8DTY0.

Enzyme and pathway databases

BioCyciSMUT210007:GC7Z-1126-MONOMER.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_00164. GlmS.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700610 / UA159.

Entry informationi

Entry nameiGLMS_STRMU
AccessioniPrimary (citable) accession number: Q8DTY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 87 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.