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Protein

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

Gene

glmS

Organism
Sphingobium yanoikuyae (Sphingomonas yanoikuyae)
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.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei151 – 1511For Fru-6P isomerization activityBy similarity

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Aminotransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:glmS
OrganismiSphingobium yanoikuyae (Sphingomonas yanoikuyae)
Taxonomic identifieri13690 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeSphingobium

Subcellular locationi

Cytoplasm By similarity

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
Chaini‹1 – 156›156Glutamine--fructose-6-phosphate aminotransferase [isomerizing]PRO_0000135378Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ56206.
SMRiQ56206. Positions 1-156.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 146143SISPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 SIS domain.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase

Family and domain databases

InterProiIPR005855. GlmS_trans.
IPR001347. SIS.
[Graphical view]
PANTHERiPTHR10937:SF0. PTHR10937:SF0. 1 hit.
PfamiPF01380. SIS. 1 hit.
[Graphical view]
PROSITEiPS51464. SIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q56206-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
IEAMAHHIVP ARDVLYLGRG TDYPLALEGA LKLKEISYIH AEGYAAGEMK
60 70 80 90 100
HGPIALIDEL VPVICIAPSG PLFEKTVSNM QEVQARGGKV VLISAYDGVQ
110 120 130 140 150
AAGEGCLATI TMPKVHPLIA PMVYAVPVQL LAYHVAVLKG TDVDQPRNLA

KSVTVE
Length:156
Mass (Da):16,606
Last modified:November 1, 1996 - v1
Checksum:i5D661DE8EEFD4EDD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37523 Genomic DNA. Translation: AAC43642.1.
PIRiPC4141.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37523 Genomic DNA. Translation: AAC43642.1.
PIRiPC4141.

3D structure databases

ProteinModelPortaliQ56206.
SMRiQ56206. Positions 1-156.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR005855. GlmS_trans.
IPR001347. SIS.
[Graphical view]
PANTHERiPTHR10937:SF0. PTHR10937:SF0. 1 hit.
PfamiPF01380. SIS. 1 hit.
[Graphical view]
PROSITEiPS51464. SIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Sequence and expression of an isocitrate dehydrogenase-encoding gene from a polycyclic aromatic hydrocarbon oxidizer, Sphingomonas yanoikuyae B1."
    Wang Y., Lau P.C.K.
    Gene 168:15-21(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DSM 6900 / JCM 10274 / B1.

Entry informationi

Entry nameiGLMS_SPHYA
AccessioniPrimary (citable) accession number: Q56206
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: January 7, 2015
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

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.