GLTA_BACSU
ID GLTA_BACSU Reviewed; 1520 AA.
AC P39812;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Glutamate synthase [NADPH] large chain;
DE EC=1.4.1.13;
DE AltName: Full=NADPH-GOGAT;
GN Name=gltA; OrderedLocusNames=BSU18450;
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 1412.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=2548995; DOI=10.1128/jb.171.9.4718-4727.1989;
RA Bohannon D.E., Sonenshein A.L.;
RT "Positive regulation of glutamate biosynthesis in Bacillus subtilis.";
RL J. Bacteriol. 171:4718-4727(1989).
RN [4]
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).
RN [5]
RP REGULATION BY TNRA.
RX PubMed=12823818; DOI=10.1046/j.1365-2958.2003.03567.x;
RA Yoshida K., Yamaguchi H., Kinehara M., Ohki Y.-H., Nakaura Y., Fujita Y.;
RT "Identification of additional TnrA-regulated genes of Bacillus subtilis
RT associated with a TnrA box.";
RL Mol. Microbiol. 49:157-165(2003).
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 -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
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; CAB13728.2; -; Genomic_DNA.
DR EMBL; M28509; AAA16438.1; -; Unassigned_DNA.
DR PIR; G69634; G69634.
DR RefSeq; NP_389727.2; NC_000964.3.
DR RefSeq; WP_009967365.1; NZ_CP053102.1.
DR AlphaFoldDB; P39812; -.
DR SMR; P39812; -.
DR IntAct; P39812; 1.
DR MINT; P39812; -.
DR STRING; 224308.BSU18450; -.
DR MEROPS; C44.003; -.
DR PaxDb; P39812; -.
DR PRIDE; P39812; -.
DR EnsemblBacteria; CAB13728; CAB13728; BSU_18450.
DR GeneID; 940024; -.
DR KEGG; bsu:BSU18450; -.
DR PATRIC; fig|224308.179.peg.2012; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR InParanoid; P39812; -.
DR OMA; TVFRLQH; -.
DR PhylomeDB; P39812; -.
DR BioCyc; BSUB:BSU18450-MON; -.
DR BRENDA; 1.4.1.13; 658.
DR SABIO-RK; P39812; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00689.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0015930; F:glutamate synthase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0019676; P:ammonia assimilation cycle; IBA:GO_Central.
DR GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
DR GO; GO:0097054; P:L-glutamate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 2.160.20.60; -; 1.
DR Gene3D; 3.20.20.70; -; 2.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR InterPro; IPR006982; Glu_synth_centr_N.
DR InterPro; IPR002932; Glu_synthdom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR Pfam; PF00310; GATase_2; 1.
DR Pfam; PF04898; Glu_syn_central; 1.
DR Pfam; PF01645; Glu_synthase; 1.
DR Pfam; PF01493; GXGXG; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR SUPFAM; SSF69336; SSF69336; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 2: Evidence at transcript level;
KW 3Fe-4S; Amino-acid biosynthesis; FAD; Flavoprotein; FMN;
KW Glutamate biosynthesis; Glutamine amidotransferase; Iron; Iron-sulfur;
KW Metal-binding; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..1520
FT /note="Glutamate synthase [NADPH] large chain"
FT /id="PRO_0000170797"
FT DOMAIN 22..415
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT REGION 890..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 22
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 1060..1112
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 1113
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1119
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1124
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1520 AA; 168772 MW; 156A22E65A8CC423 CRC64;
MTYNQMPKAQ GLYRPEFEHD ACGIGLYAHL KGKQTHDIVK QGLKMLCQLD HRGGQGSDPD
TGDGAGLLVQ IPDAFFRKEC KNINLPEKER YGVGMVFFSQ KEDERKKIEK QINALIEQEG
QVVLGWRTVP VNVGKIGTVA QKSCPFVRQV FIGASSDLKD NLSFERKLYV IRKQAENWGV
TEGLDFYFAS LSSQTIVYKG LLTPEQVDAF YSDLQDEAFV SAFALVHSRF STNTFPTWER
AHPNRYLVHN GEINTLRGNI NWMRAREQQF VSESFGEDLN KILPILNADG SDSSILDNAF
EFFVMAGRKP AHTAMMLIPE PWTENTHMSK EKRAFYEYHS SLMEPWDGPT AISFTDGKQI
GAILDRNGLR PARYYVTKDD YIIFSSEVGV IEVEQENVLY KNRLEPGKML LIDLEEGRII
SDEEVKTQIA TEYPYQKWLE EELVQVNPDP ESREEEQFSD LLTRQKAFGY TYEDIQKYLI
PVIKEGKDPL GSMGNDAPLA VLSDRAQSLF NYFKQLFAQV TNPPIDAIRE QLVTSTMTWL
GAEGDLLHPS ERNVRRIKLY TPVLSNEQFY ALKTIVHPDL KSQKIDVLFS EDLERGLKDM
FTQAEKAISQ GVSLLILSDK KMNERLTPIP PLLAVSALHQ HLIRKGLRTK VSIIVESGEA
REVHHFAALI GYGADAINPY LAYATYKQEI DEGRLDISYE EAVSKYGKSI TEGVVKVMSK
MGISTVQSYR GAQIFEAVGI SRDVIDRYFS GTASQLGGID LQTIAEEAQR RHREAYQDDY
SKTLEPGSDF QWRNGGEHHA FNPKTIHTLQ WACRRNDYNL FKQYTKAADE ERIGFLRNLF
AFDGNRKPLK LEEVESAESI VKRFKTGAMS FGSLSKEAHE ALAIAMNRLG GKSNSGEGGE
DPKRFVPDEN GDDRRSAIKQ IASGRFGVKS HYLVNADELQ IKMAQGAKPG EGGQLPGNKV
YPWVADVRGS TPGVGLISPP PHHDIYSIED LAQLIHDLKN ANRDARISVK LVSKAGVGTI
AAGVAKATAD VIVISGYDGG TGASPKTSIK HTGLPWELGL AEAHQTLMLN GLRDRVVLET
DGKLMTGRDV VMAALLGAEE FGFATAPLVV LGCVMMRACH LDTCPVGVAT QNPELRKKFM
GDPDHIVNYM LFIAEEVREY MAALGFKTFD EMIGRTDVLH ASERAKEHWK ASQLDLSTLL
YQPEGVRTFQ SPQNHKIDQS LDITTILPAV QEAIESGKEA DISIEINNTN RVAGTITGSE
ISKRYGEEGL PEDTIKLHFT GSAGQSFGAF VPKGMTLYLD GDSNDYVGKG LSGGKIIVKS
SEGFNSASDD NVIIGNVAFY GATSGEAYIN GRAGERFAVR NSGVNVVVEG IGDHGCEYMT
GGSVVVLGDV GKNFAAGMSG GIAYVLTEDV KAFKRKCNLE MILFESLEDE KEIQQIKAML
ERHTAYTNSQ KAEDLLDQWE DSVKKFVKVI PKNYKQMLAS IEEQKAAGLS DEEAIMFAFE
ANTKPKQNTA ASGQKQAVVQ
