GLT1_ORYSJ
ID GLT1_ORYSJ Reviewed; 2167 AA.
AC Q0JKD0; Q9ZNX7;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Glutamate synthase 1 [NADH], chloroplastic;
DE EC=1.4.1.14;
DE AltName: Full=NADH-dependent glutamate synthase 1;
DE Short=NADH-GOGAT 1;
DE Flags: Precursor;
GN OrderedLocusNames=Os01g0681900, LOC_Os01g48960;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Sasanishiki; TISSUE=Root;
RX PubMed=9748637; DOI=10.1016/s0167-4838(98)00142-3;
RA Goto S., Akagawa T., Kojima S., Hayakawa T., Yamaya T.;
RT "Organization and structure of NADH-dependent glutamate synthase gene from
RT rice plants.";
RL Biochim. Biophys. Acta 1387:298-308(1998).
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).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=9952435; DOI=10.1104/pp.119.2.409;
RA Hayakawa T., Hopkins L., Peat L.J., Yamaya T., Tobin A.K.;
RT "Quantitative intercellular localization of NADH-dependent glutamate
RT synthase protein in different types of root cells in rice plants.";
RL Plant Physiol. 119:409-416(1999).
RN [6]
RP INDUCTION.
RC STRAIN=cv. Sasanishiki; TISSUE=Shoot;
RX PubMed=17350935; DOI=10.1093/jxb/erm016;
RA Tabuchi M., Abiko T., Yamaya T.;
RT "Assimilation of ammonium ions and reutilization of nitrogen in rice (Oryza
RT sativa L.).";
RL J. Exp. Bot. 58:2319-2327(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20213442; DOI=10.1007/s00726-010-0531-5;
RA Tamura W., Hidaka Y., Tabuchi M., Kojima S., Hayakawa T., Sato T.,
RA Obara M., Kojima M., Sakakibara H., Yamaya T.;
RT "Reverse genetics approach to characterize a function of NADH-glutamate
RT synthase1 in rice plants.";
RL Amino Acids 39:1003-1012(2010).
CC -!- FUNCTION: Involved in glutamate biosynthesis and plays a major role in
CC the primary ammonium ions assimilation in seedling roots. May be
CC involved in the reutilization of glutamine in developing organs. Plays
CC a role in the development of tillers. {ECO:0000269|PubMed:20213442}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + L-glutamine +
CC NADH; Xref=Rhea:RHEA:13753, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58359; EC=1.4.1.14;
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 (NAD(+)
CC route): step 1/1.
CC -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:9952435}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots.
CC {ECO:0000269|PubMed:9748637}.
CC -!- INDUCTION: By ammonium supply in roots. {ECO:0000269|PubMed:17350935}.
CC -!- DISRUPTION PHENOTYPE: Inhibition of the main root elongation when grown
CC in presence of ammonium chloride. Reduced plant height, biomass and
CC panicle number. {ECO:0000269|PubMed:20213442}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family. {ECO:0000305}.
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DR EMBL; AB008845; BAA35120.1; -; mRNA.
DR EMBL; AP008207; BAF05798.1; -; Genomic_DNA.
DR EMBL; AP014957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015649242.1; XM_015793756.1.
DR AlphaFoldDB; Q0JKD0; -.
DR SMR; Q0JKD0; -.
DR STRING; 4530.OS01T0682001-01; -.
DR PaxDb; Q0JKD0; -.
DR PRIDE; Q0JKD0; -.
DR GeneID; 4324398; -.
DR KEGG; osa:4324398; -.
DR eggNOG; KOG0399; Eukaryota.
DR HOGENOM; CLU_000422_5_3_1; -.
DR InParanoid; Q0JKD0; -.
DR OrthoDB; 126283at2759; -.
DR BRENDA; 1.4.1.14; 8948.
DR PlantReactome; R-OSA-1119443; Ammonia assimilation cycle.
DR PlantReactome; R-OSA-1119535; Glutamate biosynthesis IV.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q0JKD0; OS.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; IDA:UniProtKB.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
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:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0019676; P:ammonia assimilation cycle; IMP:UniProtKB.
DR GO; GO:0048589; P:developmental growth; IMP:UniProtKB.
DR GO; GO:0006537; P:glutamate biosynthetic process; IMP:UniProtKB.
DR GO; GO:0097054; P:L-glutamate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0060359; P:response to ammonium ion; IEP:UniProtKB.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 1.10.1060.10; -; 1.
DR Gene3D; 2.160.20.60; -; 1.
DR Gene3D; 3.20.20.70; -; 2.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
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; IPR012220; Glu_synth_euk.
DR InterPro; IPR002932; Glu_synthdom.
DR InterPro; IPR006005; Glut_synth_ssu1.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR Pfam; PF14691; Fer4_20; 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 Pfam; PF07992; Pyr_redox_2; 1.
DR PIRSF; PIRSF000187; GOGAT; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR SUPFAM; SSF69336; SSF69336; 1.
DR TIGRFAMs; TIGR01317; GOGAT_sm_gam; 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..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..2167
FT /note="Glutamate synthase 1 [NADH], chloroplastic"
FT /id="PRO_0000395201"
FT DOMAIN 100..504
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 100
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT BINDING 1192..1249
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 1245
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1251
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1256
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1956..1970
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT CONFLICT 769
FT /note="Missing (in Ref. 1; BAA35120)"
FT /evidence="ECO:0000305"
FT CONFLICT 2056
FT /note="F -> L (in Ref. 1; BAA35120)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2167 AA; 236895 MW; 1CDED150F52B00EB CRC64;
MSAAQGMAYK LRTDAAPTGA GRRARRSHSS VAAPYRAARL VQGGVSIEGG LVGGCQLTEE
RVAARPPRAA ARDAEPVRPL STLPESSIGL YDPSRERDSC GVGFVAELSG DYKRATVNDA
LEMLERMAHR GACGCEKNTG DGAGILVALP HNFFREVTKD AGFELPQPGE YAVGMVFLPI
DEKRRERSKA EFQKVAESLG HVILGWRRVP TDNSDLGESA LQTEPVIEQV FLTKSSSSEA
DFEQQLYILR RLSILSIRAA LNLRRGGKRD FYMCSLSSRT IVYKGQLKPC QLKGYYYADL
GHENFTSYMA LVHSRFSTNT FPSWDRAQPM RVLGHNGEIN TLKGNKNWMK AREGLLECEK
LGLTKDQFSK ILPIVDATSS DSGAFDGVLE LLIRGGRSLP EAVMMMIPEA WQNDVNMEPE
KKALYEFLSA LMEPWDGPAL ISFTDGRYLG ATLDRNGLRP GRFYVTHSGR VVMGSEVGVV
DVPSKDVLRK GRLNPGMMLL VDFENHTVVD DEALKAQYSK AHPYGEWLKR QKIYLKDIVE
SVPETERVAP GISGSLTQKN EKKEHAGVNG IVTPLKAFGY TVEALEMLLL PMAKDGVEAL
GSMGNDTPLA VMSNREKLTF EYFKQMFAQV TNPPIDPIRE KIVTSMECMI GPEGDLLETT
EKQCNRLALE GPLVSIDEME AIKKMNYRGW RSKVLDITYP KKSGRKGLEE TLDRICTEAR
GAIKKGYTVL VLSDRGFSSD RVAVSSLLAV GAVHQHLVAN LERTRVGLLV ESAEPREVHH
FCTLVGFGAD AVCPYLAIEA IWCLQNDGKI PPNGDGKPYS KEELVKKYFY ASNYGMMKVL
AKMGISTLAS YKGAQIFEAL GLSSEVIRKC FDGTPSRIEG ATFEMLARDA LRLHELAFPS
RAPPPGSADA KALPNPGDYH WRKNGEVHLN DPLAMAKLQE AARVNSRAAY KEYSRRIQEL
NKTCNLRGML KFKDTADMIS VDEVEPASEI VKRFVTGAMS YGSISLEAHT ALAMAMNKLG
GKSNTGEGGE QPSRMEPLAN GSMNPKRSAI KQVASGRFGV SSYYLTNADE LQIKMAQGAK
PGEGGELPGH KVIGDIAVTR HSTAGVGLIS PPPHHDIYSI EDLAQLIHDL KNSNPRARIS
VKLVSEAGVG VVASGVVKGH ADHVLISGHD GGTGASRWTG IKNAGLPWEL GLAETHQTLV
ANGLRGRAIL QTDGQLKTGK DVAVACLLGA EEFGFSTAPL ITLGCIMMRK CHTNTCPVGI
ATQDPVLREK FAGEPEHVIN FFFMLAEELR EIMSQLGFRT ITEMVGRSDM LEVDPEVVKS
NEKLENIDLS LILKPAAEIR PGAAQYCVEK QDHGLDMALD NKLIALSKAA LEKEVRVFIE
TPIQNTNRAV GTMLSHEVTK RYHMKGLPAG TIHVKLTGSA GQSLGAFLCP GITLELEGDS
NDYVGKGLSG GKIVVYPPRD STFIPEDNIV IGNVALYGAT IGEAYFNGMA AERFCVRNSG
AQAVVEGIGD HGCEYMTGGT VVILGKTGRN FAAGMSGGIA YVYDIDGKFS VRCNHELVDL
YHVEEEEDIT TLKMMIEQHR LNTGSVVARD ILSNFDTLLP KFVKVFPRDY KRVLDNMKAE
KAAAKLAKEP KISNGVSVTT KKVQPEQSTN RPTRVSNAKK YRGFISYERE SISYRDPNER
VKDWKEVAIE SVPGPLLNTQ SARCMDCGTP FCHQESSGAG CPLGNKIPEF NELVHQNRWR
EALDRLLETN NFPEFTGRVC PAPCEGSCVL GIIENPVSIK SIECAIIDKG FEEGWMVPRP
PLQRTGKKVA IIGSGPAGLA AADQLNKMGH FVTVFERADR IGGLMMYGVP NMKTDKIEIV
QRRVNLMAEE GITFVVNANV GSDPLYSIER LRSENDAVIL ACGATKPRDL GIPGRELSGV
HFAMEFLHAN TKSLLDSNLE DGRYISAKGK KVVVIGGGDT GTDCIGTSIR HGCTSIVNLE
LLTKPPSKRA ADNPWPQWPR IFRVDYGHQE ASSKFGNDPR TYEVLTKRFI GDENGNVKAL
EVVRVKWEKV DGRFQFKEIE GSNETIEADL VLLAMGFLGP EATIAEKLGL EKDNRSNFKA
QFGNFATSVD GIFAAGDCRR GQSLVVWAIT EGRQAAAAVD KYLSRNEQDA AEDITPSGAG
FVQPVAA
