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Protein

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

Gene

glmS

Organism
Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans)
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 sitei606 – 6061For 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

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
OrganismiAcidithiobacillus ferrooxidans (Thiobacillus ferrooxidans)
Taxonomic identifieri920 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus

Subcellular locationi

  1. 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 – 611610Glutamine--fructose-6-phosphate aminotransferase [isomerizing]PRO_0000135404Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ56275.
SMRiQ56275. Positions 2-611.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 219218Glutamine amidotransferase type-2UniRule annotationAdd
BLAST
Domaini287 – 427141SIS 1UniRule annotationAdd
BLAST
Domaini460 – 601142SIS 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

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.

Q56275-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCGIVGGVSK TDLVPMILEG LQRLEYRGYD SAGLAILGAD ADLLRVRSVG
60 70 80 90 100
RVAELTAAVV ERGLQGQVGI GHTRWATHGG VRECNAHPMI SHEQIAVVHN
110 120 130 140 150
GIIENFHALR AHLEAAGYTF TSETDTEVIA HLVHHYRQTA PDLFAATRRA
160 170 180 190 200
VGDLRGAYAI AVISSGDPET VCVARMGCPL LLGVADDGHY FASDVAALLP
210 220 230 240 250
VTRRVLYLED GDVAMLQRQT LRITDQAGAS RQREEHWSQL SAAAVDLGPY
260 270 280 290 300
RHFMQKEIHE QPRAVADTLE GALNSQLDLT DLWGDGAAAM FRDVDRVLFL
310 320 330 340 350
ASGTSHYATL VGRQWVESIV GIPAQAELGH EYRYRDSIPD PRQLVVTLSQ
360 370 380 390 400
SGETLDTFEA LRRAKDLGHT RTLAICNVAE SAIPRASALR FLTRAGPEIG
410 420 430 440 450
VASTKAFTTQ LAALYLLALS LAKAPGASER CAAGGSPGRL RQLPGSVQHA
460 470 480 490 500
LNLEPQIQGW AARFASKDHA LFLGRGLHYP IALEGALKLK EISYIHAEAY
510 520 530 540 550
PAGELKHGPL ALVDRDMPVV VIAPNDRLLE KLAANMQEVH ARGGELYVFA
560 570 580 590 600
DSDSHFNASA GVHVMRLPRH AGLLSPIVHA IPVQLLAYHA ALVKGTDVDR
610
PRNLAKSVTV E
Length:611
Mass (Da):65,993
Last modified:January 23, 2007 - v3
Checksum:iC03B2C3A20A0A512
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF032884 Genomic DNA. Translation: AAC21670.1.
PIRiT45493.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF032884 Genomic DNA. Translation: AAC21670.1.
PIRiT45493.

3D structure databases

ProteinModelPortaliQ56275.
SMRiQ56275. Positions 2-611.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC44.971.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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. Sarnovsky R.J., Craig N.L., Oppon J.C., Rawlings D.E.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 33020 / 11Fe.

Entry informationi

Entry nameiGLMS_ACIFR
AccessioniPrimary (citable) accession number: Q56275
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 76 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.