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O34399 (GLTB_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutamate synthase [NADPH] small chain

EC=1.4.1.13
Alternative name(s):
NADPH-GOGAT
Gene names
Name:gltB
Ordered Locus Names:BSU18440
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH.

Pathway

Amino-acid biosynthesis; L-glutamate biosynthesis via GLT pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+) route): step 1/1.

Energy metabolism; nitrogen metabolism.

Subunit structure

Aggregate of 4 catalytic active heterodimers, consisting of a large and a small subunit By similarity.

Induction

The gltAB operon is positively regulated by gltC and negatively regulated by tnrA under nitrogen-limited conditions. Ref.3

Sequence similarities

Belongs to the glutamate synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 493493Glutamate synthase [NADPH] small chain
PRO_0000170798

Regions

Nucleotide binding299 – 31315NADP Potential

Sequences

Sequence LengthMass (Da)Tools
O34399 [UniParc].

Last modified June 16, 2009. Version 2.
Checksum: EBEA7171A4AA0270

FASTA49354,862
        10         20         30         40         50         60 
MGKPTGFMEI KREKPAERDP LTRLKDWKEY SAPFSEEASK RQGARCMDCG TPFCQIGADI 

        70         80         90        100        110        120 
NGFTSGCPIY NLIPEWNDLV YRGRWKEALE RLLKTNNFPE FTGRVCPAPC EGSCTLAISD 

       130        140        150        160        170        180 
PAVSIKNIER TIIDKGFENG WIQPRIPKKR TGKKVAIVGS GPAGLASADQ LNQAGHSVTV 

       190        200        210        220        230        240 
FERADRAGGL LTYGIPNMKL EKGIVERRIK LLTQEGIDFV TNTEIGVDIT ADELKEQFDA 

       250        260        270        280        290        300 
VILCTGAQKQ RDLLIEGRDS KGVHYAMDYL TLATKSYLDS NFKDKQFIDA KGKDVIVIGG 

       310        320        330        340        350        360 
GDTGADCVAT ALRQKAKSVH QFGKHPKLPP ARTNDNMWPE QPHVFTLEYA YEEAEAKFGR 

       370        380        390        400        410        420 
DPREYSIQTT KMVADKNGKL KELHTIQMEK VKNEHGKYEF RELPGTEKVW PAQLVFIAIG 

       430        440        450        460        470        480 
FEGTEQPLLK QFGVNSVNNK ISAAYGDYQT NIDGVFAAGD ARRGQSLIVW AINEGREVAR 

       490 
EVDRYLMGSS VLP 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[2]"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract]
Cited for: SEQUENCE REVISION TO 354.
[3]"Role of TnrA in nitrogen source-dependent repression of Bacillus subtilis glutamate synthase gene expression."
Belitsky B.R., Wray L.V. Jr., Fisher S.H., Bohannon D.E., Sonenshein A.L.
J. Bacteriol. 182:5939-5947(2000) [PubMed: 11029411] [Abstract]
Cited for: REGULATION BY TNRA.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL009126 Genomic DNA. Translation: CAB13727.2.
PIRH69634.
RefSeqNP_389726.2. NC_000964.3.

3D structure databases

ProteinModelPortalO34399.
SMRO34399. Positions 4-493.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000000114; EBBACP00000000114; EBBACG00000000114.
GeneID940053.
GenomeReviewsGene locus BSU18440 in contig AL009126_GR.
KEGGbsu:BSU18440.
NMPDRfig|224308.1.peg.1848.
PATRIC18975527. VBIBacSub10457_1954.

Organism-specific databases

GenoListBSU18440. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000000438.
HOGENOMHBG715033.
PhylomeDBO34399.
ProtClustDBPRK12810.

Enzyme and pathway databases

BioCycBSUB:BSU18440-MONOMER.

Family and domain databases

InterProIPR012285. Fum_reductase_C.
IPR006005. Glut_synth_ssu1.
IPR009051. Helical_ferredxn.
IPR016040. NAD(P)-bd_dom.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
Gene3DG3DSA:1.10.1060.10. Fum_reductase_C. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00266.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMSSF46548. Helical_ferredxn. 1 hit.
TIGRFAMsTIGR01317. GOGAT_sm_gam. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLTB_BACSU
AccessionPrimary (citable) accession number: O34399
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: June 16, 2009
Last modified: January 25, 2012
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families