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Protein

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

Gene

glmS

Organism
Bacillus subtilis (strain 168)
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 sitei595 – 5951For Fru-6P isomerization activityUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Enzyme and pathway databases

BioCyciBSUB:BSU01780-MONOMER.

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
Synonyms:gcaA, ybxD
Ordered Locus Names:BSU01780
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU01780. [Micado]

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedUniRule annotation
Chaini2 – 600599Glutamine--fructose-6-phosphate aminotransferase [isomerizing]PRO_0000135300Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

IntActiP0CI73. 1 interaction.
MINTiMINT-8366747.
STRINGi224308.Bsubs1_010100001013.

Structurei

3D structure databases

ProteinModelPortaliP0CI73.
SMRiP0CI73. Positions 2-600.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 217216Glutamine amidotransferase type-2UniRule annotationAdd
BLAST
Domaini283 – 422140SIS 1UniRule annotationAdd
BLAST
Domaini452 – 590139SIS 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

HOGENOMiHOG000258896.
InParanoidiP0CI73.
KOiK00820.
OMAiSEFRYAP.
OrthoDBiEOG6KT2Q1.
PhylomeDBiP0CI73.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_00164. GlmS.
InterProiIPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR005855. GlmS_trans.
IPR029055. Ntn_hydrolases_N.
IPR001347. SIS.
[Graphical view]
PANTHERiPTHR10937:SF0. PTHR10937:SF0. 1 hit.
PfamiPF00310. GATase_2. 1 hit.
PF01380. 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.

P0CI73-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCGIVGYIGQ LDAKEILLKG LEKLEYRGYD SAGIAVANEQ GIHVFKEKGR
60 70 80 90 100
IADLREVVDA NVEAKAGIGH TRWATHGEPS YLNAHPHQSA LGRFTLVHNG
110 120 130 140 150
VIENYVQLKQ EYLQDVELKS DTDTEVVVQV IEQFVNGGLE TEEAFRKTLT
160 170 180 190 200
LLKGSYAIAL FDNDNRETIF VAKNKSPLLV GLGDTFNVVA SDAMAMLQVT
210 220 230 240 250
NEYVELMDKE MVIVTDDQVV IKNLDGDVIT RASYIAELDA SDIEKGTYPH
260 270 280 290 300
YMLKETDEQP VVMRKIIQTY QDENGKLSVP GDIAAAVAEA DRIYIIGCGT
310 320 330 340 350
SYHAGLVGKQ YIEMWANVPV EVHVASEFSY NMPLLSKKPL FIFLSQSGET
360 370 380 390 400
ADSRAVLVQV KALGHKALTI TNVPGSTLSR EADYTLLLHA GPEIAVASTK
410 420 430 440 450
AYTAQIAVLA VLASVAADKN GINIGFDLVK ELGIAANAME ALCDQKDEME
460 470 480 490 500
MIAREYLTVS RNAFFIGRGL DYFVCVEGAL KLKEISYIQA EGFAGGELKH
510 520 530 540 550
GTIALIEQGT PVFALATQEH VNLSIRGNVK EVAARGANTC IISLKGLDDA
560 570 580 590 600
DDRFVLPEVN PALAPLVSVV PLQLIAYYAA LHRGCDVDKP RNLAKSVTVE
Length:600
Mass (Da):65,338
Last modified:January 11, 2011 - v1
Checksum:i358A3E95823CA83B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U21932 Genomic DNA. Translation: AAA64224.1.
AB006424 Genomic DNA. Translation: BAA33071.1.
AL009126 Genomic DNA. Translation: CAB11954.1.
PIRiB69633.
RefSeqiNP_388059.1. NC_000964.3.
WP_003234943.1. NZ_JNCM01000030.1.

Genome annotation databases

EnsemblBacteriaiCAB11954; CAB11954; BSU01780.
GeneIDi938736.
KEGGibsu:BSU01780.
PATRICi18971911. VBIBacSub10457_0184.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U21932 Genomic DNA. Translation: AAA64224.1.
AB006424 Genomic DNA. Translation: BAA33071.1.
AL009126 Genomic DNA. Translation: CAB11954.1.
PIRiB69633.
RefSeqiNP_388059.1. NC_000964.3.
WP_003234943.1. NZ_JNCM01000030.1.

3D structure databases

ProteinModelPortaliP0CI73.
SMRiP0CI73. Positions 2-600.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0CI73. 1 interaction.
MINTiMINT-8366747.
STRINGi224308.Bsubs1_010100001013.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB11954; CAB11954; BSU01780.
GeneIDi938736.
KEGGibsu:BSU01780.
PATRICi18971911. VBIBacSub10457_0184.

Organism-specific databases

GenoListiBSU01780. [Micado]

Phylogenomic databases

HOGENOMiHOG000258896.
InParanoidiP0CI73.
KOiK00820.
OMAiSEFRYAP.
OrthoDBiEOG6KT2Q1.
PhylomeDBiP0CI73.

Enzyme and pathway databases

BioCyciBSUB:BSU01780-MONOMER.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_00164. GlmS.
InterProiIPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR005855. GlmS_trans.
IPR029055. Ntn_hydrolases_N.
IPR001347. SIS.
[Graphical view]
PANTHERiPTHR10937:SF0. PTHR10937:SF0. 1 hit.
PfamiPF00310. GATase_2. 1 hit.
PF01380. 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

« Hide 'large scale' publications
  1. Morohoshi F.
    Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "Sequence analysis of the 70kb region between 17 and 23 degree of the Bacillus subtilis chromosome."
    Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.
    Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.

Entry informationi

Entry nameiGLMS_BACSU
AccessioniPrimary (citable) accession number: P0CI73
Secondary accession number(s): P39754
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: January 11, 2011
Last modified: June 24, 2015
This is version 35 of the entry and version 1 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. 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.