GLTB_ANTSP
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 03-AUG-2022, entry version 102.
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; unclassified 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 PRIDE; 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; 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 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
