ID   GLTB_ANTSP              Reviewed;        1536 AA.
AC   Q06434;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=Ferredoxin-dependent glutamate synthase;
DE            EC=1.4.7.1;
DE   AltName: Full=Fd-GOGAT;
GN   Name=gltB; Synonyms=glsF;
OS   Antithamnion sp. (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Ceramiales;
OC   Ceramiaceae; Antithamnion.
OX   NCBI_TaxID=2767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8219058; DOI=10.1007/bf00021421;
RA   Valentin K.-U., Kostrzewa M., Zetsche K.;
RT   "Glutamate synthase is plastid-encoded in a red alga: implications for the
RT   evolution of glutamate synthases.";
RL   Plant Mol. Biol. 23:77-85(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; Z21705; CAA79809.1; -; Genomic_DNA.
DR   PIR; S39510; S39510.
DR   AlphaFoldDB; Q06434; -.
DR   SMR; Q06434; -.
DR   UniPathway; UPA00045; -.
DR   UniPathway; UPA00634; UER00691.
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   CDD; cd00982; gltB_C; 1.
DR   CDD; cd00713; GltS; 1.
DR   CDD; cd02808; GltS_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 2.
DR   Gene3D; 2.160.20.60; Glutamate synthase, alpha subunit, C-terminal domain; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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   PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11938:SF1; FERREDOXIN-DEPENDENT GLUTAMATE SYNTHASE 1, CHLOROPLASTIC_MITOCHONDRIAL; 1.
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; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   3: Inferred from homology;
KW   3Fe-4S; Amino-acid biosynthesis; Chloroplast; FAD; Flavoprotein; FMN;
KW   Glutamate biosynthesis; Glutamine amidotransferase; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Plastid.
FT   CHAIN           1..1536
FT                   /note="Ferredoxin-dependent glutamate synthase"
FT                   /id="PRO_0000170790"
FT   DOMAIN          27..427
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   ACT_SITE        27
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         1105..1162
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         1158
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         1164
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         1169
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1536 AA;  171112 MW;  E803CED3004F321C CRC64;
     MQVSKYFTHQ LSQFSGYPSI VSERDACGVG FIANLNSKPS NKIVTEALNA LSCMEHRGGC
     GADNISGDGA GVTIQIPWDI FISEGINFLP KLQSNQSILN YGVRMILRSS DDLDKIKKIF
     SWALDEYQLD LISWRNVPVD KSILGEESKF NQPLVVQCIV RSNNLIDYKL DKHLYLVRKK
     IEKLVSKLDI NTNKQFYICS FSSKTIVYKG MLRSEFLVKY YNDLSNSLYV SNFAMYHRRF
     STNTMPKWSL AQPMRFMAHN GEINTLLGNL NWNKSKESLL KSSIWSDYYD ILSPITNLEN
     SDSANLDSVL ELFIHSGRTP QEALMILIPE AYKNQPALSL FPEITDFYEY YSILQEPWDG
     PALVVFTDGK FVGATLDRNG LRPARYTITD DGFISLSSET GVSNINSQNV VTKGRLGPGQ
     MLCVDLSKNL VLDNWMIKQQ ISQKFPYKEW VNKYQSNLNL LEYLNDFTFD KVQMNRWHTA
     FGYTNEDVEL VIEHMASSAK EPTFSMGDDT PLPILSEKPH LIYDYFKQRF AQVTNPAIDP
     LRESLVMSLI TYLGPKGNIL EPTAIMAKSI KLESPIINEN ELAQLNSFNL SVVTVPTFID
     KHLSTQTFVD KILEICSQCD SYISQGIEIL VLSDRIEILP VDKIFVSPLL IVGAVHHYLI
     KKQLRHKVSL VIDTGQCWTT HHFALLIGYG ASAICPYLAF LTVRQWWHNS RTQKLMSTGK
     LSRLTIQESQ DNYRSAIEKG LLKILSKMGI SLLSSYHGAQ IFEILGLGQD VVDLAFSGTV
     SRLNGMTLNE LYEDSLKSYN LAFITEIPKK LPNLGYVQYR PSAEYHVNNP EMSKTLHKAV
     RNNDNILYSK YKSLLNDRRP TNLRDLLELK TDRQPISIDQ VEDVNSVLMR FCTGGMSLGA
     LSRETHETLA IRMNRIGGKS NSGEGGEDST RFKSIQDLDT SGVSRTFSHL KGLKINDLAS
     SAIKQIASGR FGVTPEYLVN AKQLEIKIAQ GAKPGEGGQL PGKKVSPYIA ELRNCKPGVT
     LISPPPHHDI YSIEDLAQLI FDLHQINPDA QVSVKLVASL GIGTIAAGVA KGNADIIQIS
     GHDGGTGASP LSSIKHAGAP WDVGLAEVHT TLVENSLREK VILRVDGGLR TGKDIIIAAL
     MGAEEFGFGT VAMIATGCVM ARVCHTNNCP VGVATQRQDL RNRFPGIPSD VVNFFIFVAE
     EVREILAELG YKSLEELIGL NDLFKVKDIE LSKTKNLNLN ILFNSINMNR NLIPKLKHKT
     VHTNGNVLDD ILLSKSNIIN AINLQSNIVQ DIEILNTDRC VGARISGLIT KMYGRDNFNG
     NLQLNFVGSA GQSFGAFISK GIHLYLKGEA NDYVGKGMNG GEIIICPPIE QKTSSSNQVI
     LGNTCLYGAT GGYLFANGQA GERFAVRNSN GYSVVEGVGD HACEYMTGGL IVVLGTFGRN
     IGAGMTGGIA YFLDEDNTLK NKLNTEIVKA QRLLTKESEE QLKNIMELYE IKTKSEKAKL
     ILDNWSQYLA KFYQIVPPSE QIQHLLMLIF FFSKYC
//