ID GLTB2_ARATH Reviewed; 1629 AA.
AC Q9T0P4; O80665;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 24-JAN-2024, entry version 177.
DE RecName: Full=Ferredoxin-dependent glutamate synthase 2, chloroplastic;
DE EC=1.4.7.1;
DE AltName: Full=Fd-GOGAT 2;
DE Flags: Precursor;
GN Name=GLU2; OrderedLocusNames=At2g41220; ORFNames=F13H10.23;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=9596633; DOI=10.1105/tpc.10.5.741;
RA Coschigano K.T., Melo-Oliveira R., Lim J., Coruzzi G.M.;
RT "Arabidopsis gls mutants and distinct Fd-GOGAT genes. Implications for
RT photorespiration and primary nitrogen assimilation.";
RL Plant Cell 10:741-752(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19555410; DOI=10.1111/j.1742-4658.2009.07114.x;
RA Potel F., Valadier M.H., Ferrario-Mery S., Grandjean O., Morin H.,
RA Gaufichon L., Boutet-Mercey S., Lothier J., Rothstein S.J., Hirose N.,
RA Suzuki A.;
RT "Assimilation of excess ammonium into amino acids and nitrogen
RT translocation in Arabidopsis thaliana--roles of glutamate synthases and
RT carbamoylphosphate synthetase in leaves.";
RL FEBS J. 276:4061-4076(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
CC -!- FUNCTION: May play a role in primary nitrogen assimilation in roots.
CC Could supply a constitutive level of glutamate to maintain a basal
CC level of protein synthesis. {ECO:0000269|PubMed:19555410,
CC ECO:0000269|PubMed:9596633}.
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 stroma {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in roots and slightly in
CC leaves. Low expression in the leaf mesophyll and phloem companion cell-
CC sieve element complex. {ECO:0000269|PubMed:19555410,
CC ECO:0000269|PubMed:9596633}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. The glutamate and glutamine
CC levels were unaffected. {ECO:0000269|PubMed:19555410}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family. {ECO:0000305}.
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DR EMBL; U39288; AAC78552.1; -; mRNA.
DR EMBL; AC005662; AAC78549.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09945.1; -; Genomic_DNA.
DR PIR; C84839; C84839.
DR RefSeq; NP_181655.1; NM_129687.5.
DR AlphaFoldDB; Q9T0P4; -.
DR SMR; Q9T0P4; -.
DR BioGRID; 4058; 10.
DR STRING; 3702.Q9T0P4; -.
DR iPTMnet; Q9T0P4; -.
DR PaxDb; 3702-AT2G41220-1; -.
DR ProteomicsDB; 230405; -.
DR EnsemblPlants; AT2G41220.1; AT2G41220.1; AT2G41220.
DR GeneID; 818721; -.
DR Gramene; AT2G41220.1; AT2G41220.1; AT2G41220.
DR KEGG; ath:AT2G41220; -.
DR Araport; AT2G41220; -.
DR TAIR; AT2G41220; GLU2.
DR eggNOG; KOG0399; Eukaryota.
DR HOGENOM; CLU_000422_8_2_1; -.
DR InParanoid; Q9T0P4; -.
DR OMA; CISKGTK; -.
DR OrthoDB; 20503at2759; -.
DR PhylomeDB; Q9T0P4; -.
DR BioCyc; ARA:AT2G41220-MONOMER; -.
DR BRENDA; 1.4.7.1; 399.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00691.
DR PRO; PR:Q9T0P4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9T0P4; baseline and differential.
DR Genevisible; Q9T0P4; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016041; F:glutamate synthase (ferredoxin) activity; ISS:TAIR.
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:SF138; FERREDOXIN-DEPENDENT GLUTAMATE SYNTHASE 2, CHLOROPLASTIC; 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 1: Evidence at protein level;
KW 3Fe-4S; Amino-acid biosynthesis; Chloroplast; FAD; Flavoprotein; FMN;
KW Glutamate biosynthesis; Glutamine amidotransferase; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..107
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 108..1629
FT /note="Ferredoxin-dependent glutamate synthase 2,
FT chloroplastic"
FT /id="PRO_0000011615"
FT DOMAIN 108..507
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT REGION 1599..1629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 108
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 1186..1243
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 1239
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1245
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1250
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT CONFLICT 86
FT /note="S -> P (in Ref. 1; AAC78552)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1629 AA; 177752 MW; 83B02D81807F2DC7 CRC64;
MALQSPGATG ASSSVSRLLS SAKLSSTKTI FSVDFVRSYC ISKGTKRRNE LSGFRGYSPL
LKSSLRSPFS VKAILNSDRA AGDASSSFSD LKPQVAYLED IISERGACGV GFIANLENKA
THKIVNDALI ALGCMEHRGG CGSDNTSGDG SGLMTSIPWD LFNEWAEKQG IASFDRTHTG
VGMLFLPRDD NIRKEAKKVI TSIFEKEGLE VLGWRDVPVE ASIVGHNAKQ TMPNTEQVFV
RIVKDDKVDD VERELYICRK LIERAVASES WASELYFSSL SNQTIVYKGM LRSEVLGLFY
PDLQNDLYKS PFAIYHRRFS TNTSPRWHLA QPMRFLGHNG EINTIQGNLN WMTSREASLR
SPVWHGREND IRPISNPKAS DSANLDSAAE LLIRSGRTPE ESLMILVPEA YKNHPTLMIK
YPEAVDFYDY YKGQMEPWDG PALVLFSDGK TVGACLDRNG LRPARYWRTS DNVVYVASEV
GVLPMDESKV TMKGRLGPGM MISVDLENGQ VYENTEVKKR VASYNPYGKW VSENLRNLKP
SNYLSSAILE TDETLRRQQA FGYSSEDVQM VIESMAAQGK EPTFCMGDDT PVAVLSQKPH
MLYDYFKQRF AQVTNPAIDP LREGLVMSLE VNIGKRGNIL EVGPQNVSQV VLSGPVLNER
ELEGLLGDPL LKSQILPTFF DIRRGIEGSL KKGLLKLCEA ADEAVRNGSQ VLVLSDRSDN
PEPTRPAIPM LLAVGAVHQH LIQNGLRMSA SIIADTAQCF STHHFACLIG YGASAICPHL
ALETCRQWRL SNKTVNMMRN GKMPTVTMEQ AQKNYRKAVN TGLLKVLSKM GISLFSSYCG
AQIFEIYGLG NEVVEFSFRG SASQIGGLTL DELARETLTF WVRAFSEDTA KRLENFGFIQ
FRPGGEYHGN NPEMSKLLHK AVREKSETAY AVYQQHLANR PITVFRDLLE FKSDRNPIPV
GKVEPASSIV ERFCTGGMSL GAISRETHET IAIAMNRLGG KSNSGEGGED PIRWKPLTDV
VDGYSSTLPH LKGLRNGDTA TSAIKQVASG RFGVTPTFLV NADQLEIKVA QGAKPGEGGQ
LPGKKVSAYI ARLRNSKPGV PLISPPPHHD IYSIEDLAQL IFDLHQVNPK AKVSVKLVSE
TGIGTVASGV AKANADIIQI SGYDGGTGAS PISSIKHAGG PWELGLAETQ KTLIGNGLRE
RVIIRVDGGF KSGVDVLIAA AMGADEYGFG TLAMIATGCI MARICHTNNC PVGVASQREE
LRARFPGLPG DLVNFFLYIA EEVRGILAQL GYEKLDDIIG RTDLLKARDI SLVKTHLDLS
YLLSSVGLPK RSSTSIRKQE VHSNGPVLDD TLLQDPEIMD AIENEKTVHK TMSIYNVDRS
VCGRIAGVIA KKYGDTGFAG QLNLTFTGSA GQSFACFLTP GMNIRLVGEA NDYVGKGMAG
GEVVILPVES TGFRPEDATI VGNTCLYGAT GGLLFVRGKA GERFAVRNSL AQAVVEGTGD
HCCEYMTGGC VVILGKVGRN VAAGMTGGLA YILDEDNTLL PKMNKEIVKI QRVTSPVGQT
QLKSLIQAHV EKTGSSKGAM IVEEWDKYLA MFWQLVPPSE EDTPEANSDH ILKTTTGDEE
QVSSTLAEK
//
