ID   GLTB_SPIOL              Reviewed;        1621 AA.
AC   Q43155; A0A0K9RGS1; O81234;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 4.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Ferredoxin-dependent glutamate synthase, chloroplastic {ECO:0000303|PubMed:8286406};
DE            EC=1.4.7.1 {ECO:0000269|PubMed:9507092};
DE   AltName: Full=Fd-GOGAT {ECO:0000305};
DE            Short=SoFdGOGAT {ECO:0000305};
DE   Flags: Precursor;
GN   Name=FdGOGAT {ECO:0000305};
GN   ORFNames=SOVF_067910 {ECO:0000312|EMBL:KNA18696.1};
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 105-1621.
RC   STRAIN=cv. Melody; TISSUE=Leaf;
RA   Dincturk H.B., Knaff D.B.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 140-1621, PROTEIN SEQUENCE OF 105-128;
RP   213-218; 351-362; 376-391; 634-644; 646-651; 862-869; 890-903; 1049-1057;
RP   1092-204; 1108-1110; 1134-1149; 1174-1183; 1299-1304 AND 1372-1375, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Leaf;
RX   PubMed=8286406; DOI=10.1016/0005-2728(94)90086-8;
RA   Nalbantoglu B., Hirasawa M., Moomaw C., Nguyen H., Knaff D.B., Allen R.;
RT   "Cloning and sequencing of the gene encoding spinach ferredoxin-dependent
RT   glutamate synthase.";
RL   Biochim. Biophys. Acta 1183:557-561(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Viroflay;
RX   PubMed=24352233; DOI=10.1038/nature12817;
RA   Dohm J.C., Minoche A.E., Holtgraewe D., Capella-Gutierrez S.,
RA   Zakrzewski F., Tafer H., Rupp O., Soerensen T.R., Stracke R., Reinhardt R.,
RA   Goesmann A., Kraft T., Schulz B., Stadler P.F., Schmidt T., Gabaldon T.,
RA   Lehrach H., Weisshaar B., Himmelbauer H.;
RT   "The genome of the recently domesticated crop plant sugar beet (Beta
RT   vulgaris).";
RL   Nature 505:546-549(2014).
RN   [4]
RP   INTERACTION WITH FERREDOXIN.
RX   PubMed=1910284; DOI=10.1016/0003-9861(91)90024-d;
RA   Hirasawa M., Chang K.T., Knaff D.B.;
RT   "The interaction of ferredoxin and glutamate synthase: cross-linking and
RT   immunological studies.";
RL   Arch. Biochem. Biophys. 286:171-177(1991).
RN   [5]
RP   FUNCTION, AND COFACTOR.
RX   PubMed=8651698; DOI=10.1006/abbi.1996.0244;
RA   Hirasawa M., Hurley J.K., Salamon Z., Tollin G., Knaff D.B.;
RT   "Oxidation-reduction and transient kinetic studies of spinach ferredoxin-
RT   dependent glutamate synthase.";
RL   Arch. Biochem. Biophys. 330:209-215(1996).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=9507092; DOI=10.1016/s0005-2728(97)00098-4;
RA   Hirasawa M., Hurley J.K., Salamon Z., Tollin G., Markley J.L., Cheng H.,
RA   Xia B., Knaff D.B.;
RT   "The role of aromatic and acidic amino acids in the electron transfer
RT   reaction catalyzed by spinach ferredoxin-dependent glutamate synthase.";
RL   Biochim. Biophys. Acta 1363:134-146(1998).
RN   [7]
RP   FUNCTION, INTERACTION WITH SQD1, AND 3D-STRUCTURE MODELING.
RX   PubMed=15752726; DOI=10.1016/j.abb.2005.02.005;
RA   Shimojima M., Hoffmann-Benning S., Garavito R.M., Benning C.;
RT   "Ferredoxin-dependent glutamate synthase moonlights in plant sulfolipid
RT   biosynthesis by forming a complex with SQD1.";
RL   Arch. Biochem. Biophys. 436:206-214(2005).
CC   -!- FUNCTION: Catalyzes the reductive conversion of 2-oxoglutarate plus
CC       glutamine to two molecules of glutamate, using reduced ferredoxin as
CC       the electron donor (PubMed:9507092). Contains one FMN but no FAD
CC       (PubMed:8651698). The FMN-binding domain is also involved in the
CC       delivery of sulfite to the reaction center of SQD1 (PubMed:15752726).
CC       {ECO:0000269|PubMed:15752726, ECO:0000269|PubMed:8651698,
CC       ECO:0000269|PubMed:9507092}.
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         Evidence={ECO:0000269|PubMed:9507092};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12130;
CC         Evidence={ECO:0000269|PubMed:9507092};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000269|PubMed:8651698};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000269|PubMed:8651698};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:8651698};
CC   -!- ACTIVITY REGULATION: Inhibited by N-bromosuccinimide, which is specific
CC       for modification of tryptophan residues probably involved in the
CC       electron transfer from ferredoxin. {ECO:0000269|PubMed:9507092}.
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. {ECO:0000305}.
CC   -!- PATHWAY: Energy metabolism; nitrogen metabolism. {ECO:0000305}.
CC   -!- SUBUNIT: Interacts with ferredoxin (PubMed:1910284). Interacts (via
CC       FMN-binding domain) with SQD1 (PubMed:15752726).
CC       {ECO:0000269|PubMed:15752726, ECO:0000269|PubMed:1910284}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in young leaves. Not detected in mature
CC       leaves. {ECO:0000269|PubMed:8286406}.
CC   -!- SIMILARITY: Belongs to the glutamate synthase family. {ECO:0000305}.
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DR   EMBL; AF061515; AAC26853.1; -; mRNA.
DR   EMBL; U03006; AAA18948.1; -; mRNA.
DR   EMBL; KQ141620; KNA18696.1; -; Genomic_DNA.
DR   PIR; S67496; S67496.
DR   AlphaFoldDB; Q43155; -.
DR   STRING; 3562.A0A0K9RGS1; -.
DR   MoonProt; Q43155; -.
DR   PRIDE; Q43155; -.
DR   BRENDA; 1.4.7.1; 5812.
DR   UniPathway; UPA00045; -.
DR   UniPathway; UPA00634; UER00691.
DR   Proteomes; UP000054095; Unassembled WGS sequence.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:CAFA.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0019899; F:enzyme binding; IPI:CAFA.
DR   GO; GO:0016041; F:glutamate synthase (ferredoxin) activity; IDA:CAFA.
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; IDA:CAFA.
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   1: Evidence at protein level;
KW   3Fe-4S; Amino-acid biosynthesis; Chloroplast; Direct protein sequencing;
KW   Flavoprotein; FMN; Glutamate biosynthesis; Glutamine amidotransferase;
KW   Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..57
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           58..1621
FT                   /note="Ferredoxin-dependent glutamate synthase,
FT                   chloroplastic"
FT                   /id="PRO_0000170796"
FT   DOMAIN          105..504
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   ACT_SITE        105
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   BINDING         1183..1240
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         1236
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         1242
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         1247
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        459
FT                   /note="R -> A (in Ref. 1; AAC26853 and 2; AAA18948)"
FT   CONFLICT        810
FT                   /note="K -> N (in Ref. 1; AAC26853 and 2; AAA18948)"
FT   CONFLICT        1128
FT                   /note="E -> A (in Ref. 1; AAC26853 and 2; AAA18948)"
SQ   SEQUENCE   1621 AA;  176752 MW;  28FEEDA82B9F2624 CRC64;
     MALQSAPKLL YSSPSPSVFS ANERRVAFSD FVGLSKKRSR RRRIAGTFRN FPALSAVSSA
     IKAVVDVDRA HHSTDSGSPT VSTSSHPLDQ QVVNLEDILA ERGACGVGFI ANLDNKGSFQ
     IVKDALTALG CMEHRGGCGS DNDSGDGSGV MTAIPWDLFN DWGKDQGIGP FDRSHTGVGM
     VFLPKDDLLA EEAKKVVLDT FAQEGIEVIG WRSVPTNVSV VGRNAKETMP NIQQVFVRII
     KEDSTDDIER ELYICRKLIE RAASSHTWAS ELYFCSLSNQ TIIYKGMLRS EVLGMFYYDL
     QNERYTSPFA IYHRRYSTNT SPRWPLAQPM RFLGHNGEIN TIQGNLNWMR SREPSIQSPV
     WRGRENEIRP YGNPKASDSA NLDSAAELLI RSGRTPEEAL MILVPEAYKN HPTLMIKYPE
     AVDFYDYYKG QMETWDGPAL LLFSDGKTVG ACLDRNGLRP ARYWRTVDNV VYVASEVGVL
     PMDESKVTMK GRLGPGMMIS VDLSSGQVYE NTEVKKRVAS SNPYGKWVKE NLRSLKAVNF
     LSRALLENDT ILRNQQAFGY SSEDVQMVIE SMASQGKEPT FCMGDDIPLA VMSQKPHMLY
     DYFKQRFAQV TNPAIDPLRE GLVMSLEVNI GKRGNILEVG PENASQVILP SPVLNEGELE
     ALVNDPLLKA QMLPIFFDIR KGVEGTLEKR LNRLCEAADE AVRNGSQMLV LSDRSEELEP
     TRPAIPILLA VGAVHQHLIQ NGLRMYTSIV VDTAQCFSTH QFACLIGYGA SAICPYLALE
     TCRQWRLSNK TVNLMRTGKI PTVTIEQAQK NFCKAVKSGL LKILSKMGIS LLSSYCGAQI
     FEIYGLGKDV VDIAFQGSVS KMGGLTLDEL ARETLSFWVK AFSEDTAKRL ENFGFIQFRP
     GGEYHVNNPE MSKLLHKAVR NKSESAYAVY QQHLANRPVS VLRDLLEFKS DRAPISVGKV
     EPATSIVERF CTGGMSLGAI SRETHEAIAI AMNRLGGKSN SGEGGEDPIR WRPLTDVVDG
     YSSTLPHLKG LQNGDTATSA IKQVASGRFG VTPTFLVNAD QIEIKIAQGA KPGEGGQLPG
     KKVSAYIARL RNSKPGVPLI SPPPHHDIYS IEDLAQLIYD LHQINPKEKV SVKLVAEAGI
     GTVASGVAKG NADIIQVSGH DGGTGASPIS SIKHAGGPWE LGLSETHQTL ISNGLRERVI
     LRVDGGLKCG VDVMMAAAMG ADEYGFGSLA MIATGCVMAR ICHTNNCPVG VASQREELRA
     RFPGVPGDLV NFFLYVAEEV RGILAQLGFE KLDDIIGRTD ILKPRDISLM KTQHLDLSYI
     LASAGLPTMS STAIRKQEVH TNGPVLDDQI LSDPEIIDAI ENEKIVNKTV KIFNVDRAVC
     GRIAGVIAKK YGDTGFAGQL NLTFEGSAGQ SFAVFLTPGM NIRLVGESND YVGKGMAGGE
     LIVTPAENPG FRPEDATIVG NTCLYGATGG QIFVRGKAGE RFAVRNSLAE AVVEGTGDHC
     CEYMTGGCVV ILGKVGRNVA AGMTGGLAYI LDEDDTLIPK VNKEIVKIQR VTAPVGQMQL
     KNLIEAHVEK TGSSKGASIL KDWDKYLPLF WQLVPPSEED TPEASAMFEQ MTSEGASLQS
     A