SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0CI73

- GLMS_BACSU

UniProt

P0CI73 - GLMS_BACSU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]
Gene
glmS, gcaA, ybxD, BSU01780
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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.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 activity By similarity
Active sitei595 – 5951For Fru-6P isomerization activity By similarity

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

BioCyciBSUB:BSU01780-MONOMER.

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

Organism-specific databases

GenoListiBSU01780. [Micado]

Subcellular locationi

Cytoplasm By similarity 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 – 11Removed By similarity
Chaini2 – 600599Glutamine--fructose-6-phosphate aminotransferase [isomerizing]UniRule annotation
PRO_0000135300Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

IntActiP0CI73. 1 interaction.
MINTiMINT-8366747.

Structurei

3D structure databases

ProteinModelPortaliP0CI73.
SMRiP0CI73. Positions 2-600.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 2 SIS domains.

Keywords - Domaini

Glutamine amidotransferase, Repeat

Phylogenomic databases

HOGENOMiHOG000258896.
KOiK00820.
OMAiPVTRRFM.
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

MCGIVGYIGQ LDAKEILLKG LEKLEYRGYD SAGIAVANEQ GIHVFKEKGR    50
IADLREVVDA NVEAKAGIGH TRWATHGEPS YLNAHPHQSA LGRFTLVHNG 100
VIENYVQLKQ EYLQDVELKS DTDTEVVVQV IEQFVNGGLE TEEAFRKTLT 150
LLKGSYAIAL FDNDNRETIF VAKNKSPLLV GLGDTFNVVA SDAMAMLQVT 200
NEYVELMDKE MVIVTDDQVV IKNLDGDVIT RASYIAELDA SDIEKGTYPH 250
YMLKETDEQP VVMRKIIQTY QDENGKLSVP GDIAAAVAEA DRIYIIGCGT 300
SYHAGLVGKQ YIEMWANVPV EVHVASEFSY NMPLLSKKPL FIFLSQSGET 350
ADSRAVLVQV KALGHKALTI TNVPGSTLSR EADYTLLLHA GPEIAVASTK 400
AYTAQIAVLA VLASVAADKN GINIGFDLVK ELGIAANAME ALCDQKDEME 450
MIAREYLTVS RNAFFIGRGL DYFVCVEGAL KLKEISYIQA EGFAGGELKH 500
GTIALIEQGT PVFALATQEH VNLSIRGNVK EVAARGANTC IISLKGLDDA 550
DDRFVLPEVN PALAPLVSVV PLQLIAYYAA LHRGCDVDKP RNLAKSVTVE 600
Length:600
Mass (Da):65,338
Last modified:January 11, 2011 - v1
Checksum:i358A3E95823CA83B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U21932 Genomic DNA. Translation: AAA64224.1 .
AB006424 Genomic DNA. Translation: BAA33071.1 .
AL009126 Genomic DNA. Translation: CAB11954.1 .
PIRi B69633.
RefSeqi NP_388059.1. NC_000964.3.

3D structure databases

ProteinModelPortali P0CI73.
SMRi P0CI73. Positions 2-600.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P0CI73. 1 interaction.
MINTi MINT-8366747.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB11954 ; CAB11954 ; BSU01780 .
GeneIDi 938736.
KEGGi bsu:BSU01780.
PATRICi 18971911. VBIBacSub10457_0184.

Organism-specific databases

GenoListi BSU01780. [Micado ]

Phylogenomic databases

HOGENOMi HOG000258896.
KOi K00820.
OMAi PVTRRFM.
OrthoDBi EOG6KT2Q1.
PhylomeDBi P0CI73.

Enzyme and pathway databases

BioCyci BSUB:BSU01780-MONOMER.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
HAMAPi MF_00164. GlmS.
InterProi IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR005855. GlmS_trans.
IPR029055. Ntn_hydrolases_N.
IPR001347. SIS.
[Graphical view ]
PANTHERi PTHR10937:SF0. PTHR10937:SF0. 1 hit.
Pfami PF00310. GATase_2. 1 hit.
PF01380. SIS. 2 hits.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
TIGRFAMsi TIGR01135. glmS. 1 hit.
PROSITEi PS51278. GATASE_TYPE_2. 1 hit.
PS51464. SIS. 2 hits.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 30 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