GLTB_PORPU
ID GLTB_PORPU Reviewed; 1538 AA.
AC P51375;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, 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;
OS Porphyra purpurea (Red seaweed) (Ulva purpurea).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX NCBI_TaxID=2787;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Avonport;
RA Reith M.E., Munholland J.;
RT "Complete nucleotide sequence of the Porphyra purpurea chloroplast
RT genome.";
RL Plant Mol. Biol. Rep. 13:333-335(1995).
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; Evidence={ECO:0000250};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC -!- SIMILARITY: Belongs to the glutamate synthase family. {ECO:0000305}.
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DR EMBL; U38804; AAC08261.1; -; Genomic_DNA.
DR PIR; S73296; S73296.
DR RefSeq; NP_053985.1; NC_000925.1.
DR AlphaFoldDB; P51375; -.
DR SMR; P51375; -.
DR GeneID; 810015; -.
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..1538
FT /note="Ferredoxin-dependent glutamate synthase"
FT /id="PRO_0000170792"
FT DOMAIN 34..431
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT ACT_SITE 34
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 1109..1166
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 1162
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1168
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1173
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1538 AA; 168711 MW; 3F647CDB2F5C77CF CRC64;
MFNQKIIEQA SGKLTGSLTK SSSLVSIEKE RDACGVGFIA DVNNIANHKI VVQALEALTC
MEHRGACSAD RDSGDGAGIT TAIPWNLFQS GLKDKGIIIQ KNESIGVGML FLPTSKLQES
KKIIENVLKE ENLEVVGWRL VPTVEEVLGK QAYLNKPHVE QMFCRSSNLS KNELEQQLFL
VRKKIERYIG INGKEWAHEF YVCSLSCYTI VYKGMMRSAV LGQFYQDLYH SEYTSSFAIY
HRRFSTNTMP KWPLAQPMRF ISHNGEINTL LGNLNWMRSR EPLLKSPIWK NRIDELKPIT
NKDNSDSANL DAAVELLIAS GRSAEEALMI LVPEAFQNQP EFNKNTEISD FYEYYSGLQE
PWDGPALVVF TDGKVIGATL DRNGLRPARY VITKDNLVIV SSESGVVQVE PSNIKSKGRL
GPGQMISVDI ISHKILNNKE IKTSVAGKTP YGDLLKESRQ ILGHQAFFSE QQVESKKLMQ
LQTAFGYTNE DVELVIEHMA SQGKEPTFCM GDDIPLAILS EKSHILYDYF KQRFAQVTNP
AIDPLRESLV MSLTIQIGHK SNLLDDQPVL AKHIKLDSPI INEGELNAIL ESKLSCAHIN
TIFKVEKGPN DFKKQIEQLC ESASQAILSG NNILILSDKN DILESEKVSI PPLLAAGAVH
HHLINKGLRQ DASIIIETAQ CWSTHHFACL IGYGASAICP YLAFETARHW WSNPKTKMLM
SKGRLPACNI QEAQANYKKA VEAGLLKILS KMGISLLSSY HGAQIFEILG LGSEVVNFAF
KGTTSQIGGL SMEELGQETV NIHSKAFSQV KTKKLANYGF VQYRPGGEYH INNPEMSKAL
HQAVRGYNPE YYNSYQRLLQ NRPPTALRDL LKLKSNKQPI AIDKVESMEN ILHKFCTGGM
SLGALSRETH ETLAIAMNRI GGKSNSGEGG EDPVRFKVLN DVNESGNSDL LPHLKGLRNG
DTASSAIKQI ASGRFGVTPE YLMNAKQLEI KIAQGAKPGE GGQLPGKKIS PYIATLRKCK
PGVPLISPPP HHDIYSIEDL SQLIFDLHQI NPTAKISVKL VSEIGIGTIA AGVAKGNADI
IQISGHDGGT GASPLSSIKH AGSPWELGLS EVHQLLAENQ LRDRVTLRVD GGLRTGSDIV
LAAIMGAEEF GFGTIAMIAT GCIMARICHT NKCPVGVATQ REELRARFSG VPEALVNFFL
FIGNEVREIL ASLGYKSLDE ITGQNHLLIK NTDIELAKTR GIELNSLINI NTHTWTKFNS
VHTNGPVMDD DILAIPEIND AIKLENEVAK HFKIANTNRT VGTRLSGVIA QKYGNEGFKG
LIKLNFYGSA GQSFGAFLAS GVNLKLMGEA NDYVGKGMNG GSIIIVPPAG TTYEDNNQVI
IGNTCLYGAT GGYLFAQGQA GERFAVRNSL AKSVVEGVGD HACEYMTGGT IVVLGKAGRN
VGAGMTGGLA YFLDEENKFI ERVNSEIVKV QRVITKAGEQ QLKNLIENHS AKTGSLKAHN
ILENWNTYLP QFWQVVPPSE ANIEETNTAY SSNTITAY
