GLTB_ORYSJ
ID GLTB_ORYSJ Reviewed; 1615 AA.
AC Q69RJ0; A2V654; A2V657; Q0D3Y9;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Ferredoxin-dependent glutamate synthase, chloroplastic;
DE EC=1.4.7.1;
DE AltName: Full=Fd-GOGAT;
DE Flags: Precursor;
GN Name=GLU; OrderedLocusNames=Os07g0658400, LOC_Os07g46460;
GN ORFNames=OJ1477_F01.112, P0047B07.133;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Sasanishiki; TISSUE=Root;
RA Hayakawa T., Sakai T., Ishiyama K., Hirose N., Nakajima H., Takezawa M.,
RA Naito K., Hino-Nakayama M., Akagawa T., Goto S., Yamaya T.;
RT "Organization and structure of ferredoxin-dependent glutamate synthase gene
RT and intracellular localization of the enzyme protein in rice plants.";
RL Plant Biotechnol. 20:43-55(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
CC -!- FUNCTION: Involved in glutamate biosynthesis in leaf. Required for the
CC reassimilation of ammonium ions generated during photorespiration (By
CC similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf blades and at lower levels in
CC roots. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD30339.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD31105.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF22434.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB024716; BAF46921.1; -; mRNA.
DR EMBL; AB061357; BAF46922.1; -; Genomic_DNA.
DR EMBL; AP003833; BAD30339.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP005184; BAD31105.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008213; BAF22434.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015646712.1; XM_015791226.1.
DR AlphaFoldDB; Q69RJ0; -.
DR SMR; Q69RJ0; -.
DR STRING; 4530.OS07T0658400-02; -.
DR PaxDb; Q69RJ0; -.
DR PRIDE; Q69RJ0; -.
DR EnsemblPlants; Os07t0658400-02; Os07t0658400-02; Os07g0658400.
DR GeneID; 4344164; -.
DR Gramene; Os07t0658400-02; Os07t0658400-02; Os07g0658400.
DR KEGG; osa:4344164; -.
DR eggNOG; KOG0399; Eukaryota.
DR HOGENOM; CLU_000422_12_0_1; -.
DR InParanoid; Q69RJ0; -.
DR OrthoDB; 126283at2759; -.
DR BRENDA; 1.4.7.1; 8948.
DR PlantReactome; R-OSA-1119420; Glutamate biosynthesis V.
DR PlantReactome; R-OSA-1119443; Ammonia assimilation cycle.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00691.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR Genevisible; Q69RJ0; OS.
DR GO; GO:0009507; C:chloroplast; 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:0016040; F:glutamate synthase (NADH) activity; IBA:GO_Central.
DR GO; GO:0015930; F:glutamate synthase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0019676; P:ammonia assimilation cycle; IBA:GO_Central.
DR GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW 3Fe-4S; Amino-acid biosynthesis; Chloroplast; FAD; Flavoprotein; FMN;
KW Glutamate biosynthesis; Glutamine amidotransferase; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..1615
FT /note="Ferredoxin-dependent glutamate synthase,
FT chloroplastic"
FT /id="PRO_0000395203"
FT DOMAIN 97..496
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT ACT_SITE 97
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT BINDING 1175..1232
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 1228
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1234
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1239
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT CONFLICT 1588
FT /note="P -> A (in Ref. 1; BAF46922)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1615 AA; 175044 MW; 6654E2ECB74536CA CRC64;
MATLPRAAAA AAPSPAAALL PLPRAAPLLA GRAAARSAAR RLRARGTRAP PLAAARRGWG
GVSPRAVLDL PRRREAAEKP AQKAADLNEI LSERGACGVG FVANLKNEPS FNIVRDALVA
LGCMEHRGGC GADNDSGDGS GLMSGIPWDL FNDWANKQGL APLDRTNTGV GMVFLPQDEN
SMEEAKAVVA KVFTDEGLEV LGWRTVPFNV SVVGRYAKET MPNIQQIFVK VAKEDNADDI
ERELYICRKL IERATKSASW ADELYFCSLS SRTIVYKGML RSEILGQFYL DLQNELYKSP
FAIYHRRYST NTSPRWPLAQ PMRLLGHNGE INTIQGNLNW MRSREATLQS PVWRGREHEI
RPFGDPKASD SANLDSTAEL LLRSGRSPAE AMMILVPEAY KNHPTLSIKY PEVIDFYDYY
KGQMEAWDGP ALLLFSDGRT VGACLDRNGL RPARYWRTSD DFVYVASEVG VIPMDESKVV
MKGRLGPGMM ITVDLQTGQV LENTEVKKSV ASANPYGSWL QQSTRSIKPV NFQSSVAMDN
ETVLRHQQAF GYSSEDVQMV IETMASQGKE PTFCMGDDIP LAVLSQKPHM LFDYFKQRFA
QVTNPAIDPL REGLVMSLEV NIGKRRNILE VGPENADQVT LSSPVLNEGE LESLLNDSKL
KPKVLSTYFD IRKGLDGSLD KAIKVLCDEA DAAVRNGSQL LVLSDRSEAL EPTRPAIPIL
LAVGAIHQHL IQNGLRMSAS IVADTAQCFS THQFACLIGY GASAICPYLA LETCRQWRLS
NKTVNLMRNG KMPTVTIEQA QRNFIKAVKS GLLKILSKMG ISLLSSYCGA QIFEIYGLGQ
EVVDLAFCGS VSKIGGLTLD ELGRETLSFW VKAFSEDTAK RLENFGFIQS RPGGEYHANN
PEMSKLLHKA VREKSDNAYT VYQQHLASRP VNVLRDLLEL KSDRAPIPIG KVEPATSIVE
RFCTGGMSLG AISRETHEAI AIAMNRIGGK SNSGEGGEDP IRWSPLADVE DGYSPTLPHL
KGLQNGDTAT SAIKQVASGR FGVTPTFLVN AEQIEIKIAQ GAKPGEGGQL PGKKVSAYIA
RLRNSKPGVP LISPPPHHDI YSIEDLAQLI YDLHQINPKA KVSVKLVAEA GIGTVASGVS
KGNADIIQIS GHDGGTGASP ISSIKHAGGP WELGLSETHQ TLIQNGLRER VVLRVDGGFR
SGLDVLMAAA MGADEYGFGS VAMIATGCVM ARICHTNNCP VGVASQREEL RARFPGVPGD
LVNYFLFVAE EVRATLAQLG FEKLDDIIGR TDILKAKHVS LAKTQHIDLK YLLSSAGLPK
WSSSQIRSQD VHSNGPVLDE TILADPDISD AIENEKEVSK TFQIYNVDRA VCGRVAGVIA
KKYGDTGFAG QLNITFTGSA GQSFGCFLTP GMNIRLVGEA NDYVGKGMAG GELVVVPVEK
TGFVPEDAAI VGNTCLYGAT GGQVFVRGKT GERFAVRNSL GQAVVEGTGD HCCEYMTGGC
VVVLGKVGRN VAAGMTGGLA YILDEDDTLV PKVNKEIVKM QRVNAPAGQM QLKGLIEAYV
EKTGSEKGAT ILREWEAYLP LFWQLVPPSE EDSPEACAEF ERVLAKQATT VQSAK
