ID   GLTB_BACSU              Reviewed;         493 AA.
AC   O34399;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Glutamate synthase [NADPH] small chain;
DE            EC=1.4.1.13;
DE   AltName: Full=NADPH-GOGAT;
GN   Name=gltB; OrderedLocusNames=BSU18440;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [2]
RP   SEQUENCE REVISION TO 354.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [3]
RP   REGULATION BY TNRA.
RX   PubMed=11029411; DOI=10.1128/jb.182.21.5939-5947.2000;
RA   Belitsky B.R., Wray L.V. Jr., Fisher S.H., Bohannon D.E., Sonenshein A.L.;
RT   "Role of TnrA in nitrogen source-dependent repression of Bacillus subtilis
RT   glutamate synthase gene expression.";
RL   J. Bacteriol. 182:5939-5947(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + L-glutamine
CC         + NADPH; Xref=Rhea:RHEA:15501, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:58359; EC=1.4.1.13;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC       pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+)
CC       route): step 1/1.
CC   -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC   -!- SUBUNIT: Aggregate of 4 catalytic active heterodimers, consisting of a
CC       large and a small subunit. {ECO:0000250}.
CC   -!- INDUCTION: The gltAB operon is positively regulated by GltC and
CC       negatively regulated by TnrA under nitrogen-limited conditions.
CC   -!- SIMILARITY: Belongs to the glutamate synthase family. {ECO:0000305}.
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DR   EMBL; AL009126; CAB13727.2; -; Genomic_DNA.
DR   PIR; H69634; H69634.
DR   RefSeq; NP_389726.2; NC_000964.3.
DR   RefSeq; WP_003231462.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34399; -.
DR   SMR; O34399; -.
DR   IntAct; O34399; 1.
DR   MINT; O34399; -.
DR   STRING; 224308.BSU18440; -.
DR   PaxDb; O34399; -.
DR   EnsemblBacteria; CAB13727; CAB13727; BSU_18440.
DR   GeneID; 940053; -.
DR   KEGG; bsu:BSU18440; -.
DR   PATRIC; fig|224308.179.peg.2011; -.
DR   eggNOG; COG0493; Bacteria.
DR   InParanoid; O34399; -.
DR   OMA; DCVGTAH; -.
DR   PhylomeDB; O34399; -.
DR   BioCyc; BSUB:BSU18440-MON; -.
DR   SABIO-RK; O34399; -.
DR   UniPathway; UPA00045; -.
DR   UniPathway; UPA00634; UER00689.
DR   PRO; PR:O34399; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0097054; P:L-glutamate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1060.10; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR006005; Glut_synth_ssu1.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   TIGRFAMs; TIGR01317; GOGAT_sm_gam; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Glutamate biosynthesis; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..493
FT                   /note="Glutamate synthase [NADPH] small chain"
FT                   /id="PRO_0000170798"
FT   BINDING         299..313
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   493 AA;  54862 MW;  EBEA7171A4AA0270 CRC64;
     MGKPTGFMEI KREKPAERDP LTRLKDWKEY SAPFSEEASK RQGARCMDCG TPFCQIGADI
     NGFTSGCPIY NLIPEWNDLV YRGRWKEALE RLLKTNNFPE FTGRVCPAPC EGSCTLAISD
     PAVSIKNIER TIIDKGFENG WIQPRIPKKR TGKKVAIVGS GPAGLASADQ LNQAGHSVTV
     FERADRAGGL LTYGIPNMKL EKGIVERRIK LLTQEGIDFV TNTEIGVDIT ADELKEQFDA
     VILCTGAQKQ RDLLIEGRDS KGVHYAMDYL TLATKSYLDS NFKDKQFIDA KGKDVIVIGG
     GDTGADCVAT ALRQKAKSVH QFGKHPKLPP ARTNDNMWPE QPHVFTLEYA YEEAEAKFGR
     DPREYSIQTT KMVADKNGKL KELHTIQMEK VKNEHGKYEF RELPGTEKVW PAQLVFIAIG
     FEGTEQPLLK QFGVNSVNNK ISAAYGDYQT NIDGVFAAGD ARRGQSLIVW AINEGREVAR
     EVDRYLMGSS VLP