ID   GLTD_MYCTO              Reviewed;         488 AA.
AC   P9WN18; F2GDM0; L0TFG6; P96219; Q7D4Q4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Glutamate synthase [NADPH] small chain;
DE            EC=1.4.1.13;
DE   AltName: Full=Glutamate synthase subunit beta;
DE            Short=GLTS beta chain;
GN   Name=gltD; OrderedLocusNames=MT3973;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. {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.
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DR   EMBL; AE000516; AAK48341.1; -; Genomic_DNA.
DR   PIR; G70655; G70655.
DR   RefSeq; WP_003899732.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WN18; -.
DR   SMR; P9WN18; -.
DR   EnsemblBacteria; AAK48341; AAK48341; MT3973.
DR   GeneID; 45427862; -.
DR   KEGG; mtc:MT3973; -.
DR   PATRIC; fig|83331.31.peg.4273; -.
DR   HOGENOM; CLU_000422_3_1_11; -.
DR   UniPathway; UPA00634; UER00689.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   4Fe-4S; Amino-acid biosynthesis; Glutamate biosynthesis; Iron; Iron-sulfur;
KW   Metal-binding; NADP; Oxidoreductase.
FT   CHAIN           1..488
FT                   /note="Glutamate synthase [NADPH] small chain"
FT                   /id="PRO_0000427204"
FT   DOMAIN          38..69
FT                   /note="4Fe-4S ferredoxin-type"
SQ   SEQUENCE   488 AA;  53452 MW;  22455022F7EF0D9F CRC64;
     MADPGGFLKY THRKLPKRRP VPLRLRDWRE VYEEFDNESL RQQATRCMDC GIPFCHNGCP
     LGNLIPEWND LVRRGRWRDA IERLHATNNF PDFTGRLCPA PCEPACVLGI NQDPVTIKQI
     ELEIIDKAFD EGWVQPRPPR KLTGQTVAVV GSGPAGLAAA QQLTRAGHTV TVFEREDRIG
     GLLRYGIPEF KMEKRHLDRR LDQMRSEGTE FRPGVNVGVD ISAEKLRADF DAVVLAGGAT
     AWRELPIPGR ELEGVHQAME FLPWANRVQE GDDVLDEDGQ PPITAKGKKV VIIGGGDTGA
     DCLGTVHRQG AIAVHQFEIM PRPPDARAES TPWPTYPLMY RVSAAHEEGG ERVFSVNTEA
     FVGTDGRVSA LRAHEVTMLD GKFVKVEGSD FELEADLVLL AMGFVGPERA GLLTDLGVKF
     TERGNVARGD DFDTSVPGVF VAGDMGRGQS LIVWAIAEGR AAAAAVDRYL MGSSALPAPV
     KPTAAPLQ