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F0S7V6 (F0S7V6_PEDSD) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] HAMAP-Rule MF_00164
EC=2.6.1.16 HAMAP-Rule MF_00164
Alternative name(s):
D-fructose-6-phosphate amidotransferase HAMAP-Rule MF_00164
GFAT HAMAP-Rule MF_00164
Glucosamine-6-phosphate synthase HAMAP-Rule MF_00164
Hexosephosphate aminotransferase HAMAP-Rule MF_00164
L-glutamine--D-fructose-6-phosphate amidotransferase HAMAP-Rule MF_00164
Gene names
Name:glmS HAMAP-Rule MF_00164
Ordered Locus Names:Pedsa_2820 EMBL ADY53361.1
OrganismPedobacter saltans (strain ATCC 51119 / DSM 12145 / JCM 21818 / LMG 10337 / NBRC 100064 / NCIMB 13643) [Complete proteome] [HAMAP] EMBL ADY53361.1
Taxonomic identifier762903 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Sphingobacteriia › Sphingobacteriales › Sphingobacteriaceae › Pedobacter ›

Protein attributes

Sequence length613 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. HAMAP-Rule MF_00164

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity HAMAP-Rule MF_00164

Regions

Domain2 – 221220Glutamine amidotransferase type-2 By similarity HAMAP-Rule MF_00164

Sites

Active site21Nucleophile; for GATase activity By similarity HAMAP-Rule MF_00164
Active site6081For Fru-6P isomerization activity By similarity HAMAP-Rule MF_00164

Sequences

Sequence LengthMass (Da)Tools
F0S7V6 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: 92DB10943C2BA063

FASTA61367,527
        10         20         30         40         50         60 
MCGIVGYIGS REAYPIVIKG LHRLEYRGYD SAGVALMNNQ NSLNIYKKAG KVKDLEDFVS 

        70         80         90        100        110        120 
GKDISGTVGM GHTRWATHGE PSDRNSHPHQ SGNDRLAIIH NGIIENYGPL KEELIARGHI 

       130        140        150        160        170        180 
FKSDTDTEVL IHLIENIQEE ENISLQEAVR VALHQVIGAF AIVIMDKDDP TELIAARKGS 

       190        200        210        220        230        240 
PMVIGVGKGE YFVASDATPI VEYTKNVIYL NDNEIAYLKR DELLIKSIDN IVQTPYIQEL 

       250        260        270        280        290        300 
ELKLEMLEKG GYDHFMLKEI YEQPRSIYDS MRGRIYPLDG KVQLGGLVEY SEKLRNANRI 

       310        320        330        340        350        360 
IIVACGTSWH AGLVGEYLIE EFARLPVEVE YASEFRYRNP IINENDIVIA ISQSGETADT 

       370        380        390        400        410        420 
MAAIQLAKEK GATLLGICNV VGSSIPRLTH GGAYTHAGPE IGVASTKAFT AQVTVLTLMA 

       430        440        450        460        470        480 
LYIAQIKGTI SQSKLISLLT ELETIPSLVE ETLKTNDQII QIASELQDSR NCIFLGRGTG 

       490        500        510        520        530        540 
FPVALEGALK LKEISYIHAE GYPAAEMKHG PIALIDEEMP VIVIATKNSS YEKVISNIQE 

       550        560        570        580        590        600 
VKARKGKVVA IVTEGDVDVK DMADYSIEIP HADEAFLPLL ATIPLQLISY HIAVMRGCNV 

       610 
DQPRNLAKSV TVE

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002545 Genomic DNA. Translation: ADY53361.1.
RefSeqYP_004275183.1. NC_015177.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADY53361; ADY53361; Pedsa_2820.
GeneID10232410.
KEGGpsn:Pedsa_2820.
PATRIC47006535. VBIPedSal163994_2930.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00820.
OMACLQGLER.

Enzyme and pathway databases

BioCycPSAL762903:GHB2-2879-MONOMER.

Family and domain databases

HAMAPMF_00164. GlmS.
InterProIPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR005855. GlmS_trans.
IPR001347. SIS.
[Graphical view]
PANTHERPTHR10937:SF0. PTHR10937:SF0. 1 hit.
PfamPF00310. GATase_2. 1 hit.
PF01380. 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 nameF0S7V6_PEDSD
AccessionPrimary (citable) accession number: F0S7V6
Entry history
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: May 1, 2013
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info