ID   GLTB_HORVU              Reviewed;         436 AA.
AC   Q08258;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Ferredoxin-dependent glutamate synthase;
DE            EC=1.4.7.1;
DE   AltName: Full=FD-GOGAT;
DE   Flags: Fragment;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-436, AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Maris Mink;
RX   PubMed=7763576; DOI=10.1007/bf00198209;
RA   Avila C., Marquez A.J., Pajuelo P., Cannell M.E., Wallsgrove R.M.,
RA   Forde B.G.;
RT   "Cloning and sequence analysis of a cDNA for barley ferredoxin-dependent
RT   glutamate synthase and molecular analysis of photorespiratory mutants
RT   deficient in the enzyme.";
RL   Planta 189:475-483(1993).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 L-glutamate + 2 oxidized [2Fe-2S]-[ferredoxin] = 2-
CC         oxoglutarate + 2 H(+) + L-glutamine + 2 reduced [2Fe-2S]-
CC         [ferredoxin]; Xref=Rhea:RHEA:12128, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC         COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:58359; EC=1.4.7.1;
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC       Note=Binds 1 [3Fe-4S] cluster.;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC       pathway; L-glutamate from 2-oxoglutarate and L-glutamine (ferredoxin
CC       route): step 1/1.
CC   -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC   -!- SIMILARITY: Belongs to the glutamate synthase family. {ECO:0000305}.
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DR   EMBL; S58774; AAC60547.1; -; mRNA.
DR   PIR; T06210; T06210.
DR   AlphaFoldDB; Q08258; -.
DR   SMR; Q08258; -.
DR   UniPathway; UPA00045; -.
DR   UniPathway; UPA00634; UER00691.
DR   ExpressionAtlas; Q08258; baseline and differential.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016041; F:glutamate synthase (ferredoxin) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0097054; P:L-glutamate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   Pfam; PF00310; GATase_2; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   1: Evidence at protein level;
KW   3Fe-4S; Amino-acid biosynthesis; Chloroplast; Direct protein sequencing;
KW   FAD; Flavoprotein; FMN; Glutamate biosynthesis; Glutamine amidotransferase;
KW   Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Plastid.
FT   CHAIN           1..>436
FT                   /note="Ferredoxin-dependent glutamate synthase"
FT                   /id="PRO_0000170795"
FT   DOMAIN          1..400
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   ACT_SITE        1
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   NON_TER         436
SQ   SEQUENCE   436 AA;  48752 MW;  63E0C7CCD04400B6 CRC64;
     CGVGFVANLS NEPSFNVVRD ALTALGCMEH RGGCGADNDS GDGAGLMSGI PWDLFDDWAS
     KEGLVPFERT HTGVGMVFLP QNENSMEEAK AAVEKVFTDE GLEVLGWRPV PFNLSVAGRN
     AKETMPNILQ IFVRIAKEDD ADDIERELYI CRKLIERATK SASWADELYF CSLSSRTIIY
     KGMLRSEVLG QFYLDLQNEL YKSPFAIYHR RFSTNTSPRW PLAQPMRLLG HNGEINTIQG
     NLNWMRSREA TIQSPVWRGR ENELRPFGDP KASDSANLDN AAELLLRSGR SPAEAMMMLV
     PEAYKNHPTL SVKYPEVIDF YEYYKGQMEA WDGPALLLFS DGRTVGACLD RNGLRPARYW
     KTSDGFVYVA SEVGVIPMDE SKVVMKGRLG PGMMITVDLE TGQVLENTEV KKNVASAKPY
     GTWLQESTRS IKPVNF