GLUT1_ARATH
ID GLUT1_ARATH Reviewed; 2208 AA.
AC Q9LV03; Q0WL27; Q56W62; Q8LPH2;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 143.
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 Name=GLT1; OrderedLocusNames=At5g53460; ORFNames=MYN8.7;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 913-1715 AND 1729-2208.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1867-2208.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=11844111; DOI=10.1046/j.1365-313x.2002.01218.x;
RA Lancien M., Martin M., Hsieh M.H., Leustek T., Goodman H., Coruzzi G.M.;
RT "Arabidopsis glt1-T mutant defines a role for NADH-GOGAT in the non-
RT photorespiratory ammonium assimilatory pathway.";
RL Plant J. 29:347-358(2002).
RN [6]
RP INDUCTION BY CADMIUM.
RC STRAIN=cv. Columbia;
RX PubMed=16502469; DOI=10.1002/pmic.200500543;
RA Sarry J.-E., Kuhn L., Ducruix C., Lafaye A., Junot C., Hugouvieux V.,
RA Jourdain A., Bastien O., Fievet J.B., Vailhen D., Amekraz B., Moulin C.,
RA Ezan E., Garin J., Bourguignon J.;
RT "The early responses of Arabidopsis thaliana cells to cadmium exposure
RT explored by protein and metabolite profiling analyses.";
RL Proteomics 6:2180-2198(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
CC -!- FUNCTION: Involved in glutamate biosynthesis. Required for non-
CC photorespiratory ammonium assimilation. Probably involved in primary
CC ammonium assimilation in roots. {ECO:0000269|PubMed:11844111}.
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:18431481}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots and at low levels in
CC leaves. {ECO:0000269|PubMed:11844111}.
CC -!- INDUCTION: Induced by cadmium. {ECO:0000269|PubMed:16502469}.
CC -!- DISRUPTION PHENOTYPE: Defect in growth and glutamate biosynthesis under
CC non-photorespiratory conditions. {ECO:0000269|PubMed:11844111}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97323.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB020754; BAA97323.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96358.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96359.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96360.1; -; Genomic_DNA.
DR EMBL; AY099795; AAM20646.1; -; mRNA.
DR EMBL; AK222185; BAD95320.1; -; mRNA.
DR EMBL; AK230382; BAF02180.1; -; mRNA.
DR RefSeq; NP_001190529.1; NM_001203600.1.
DR RefSeq; NP_001190530.1; NM_001203601.1.
DR RefSeq; NP_200158.2; NM_124725.5.
DR AlphaFoldDB; Q9LV03; -.
DR SMR; Q9LV03; -.
DR BioGRID; 20672; 2.
DR IntAct; Q9LV03; 1.
DR STRING; 3702.AT5G53460.1; -.
DR iPTMnet; Q9LV03; -.
DR MetOSite; Q9LV03; -.
DR PaxDb; Q9LV03; -.
DR PRIDE; Q9LV03; -.
DR ProteomicsDB; 230406; -.
DR EnsemblPlants; AT5G53460.1; AT5G53460.1; AT5G53460.
DR EnsemblPlants; AT5G53460.2; AT5G53460.2; AT5G53460.
DR EnsemblPlants; AT5G53460.3; AT5G53460.3; AT5G53460.
DR GeneID; 835427; -.
DR Gramene; AT5G53460.1; AT5G53460.1; AT5G53460.
DR Gramene; AT5G53460.2; AT5G53460.2; AT5G53460.
DR Gramene; AT5G53460.3; AT5G53460.3; AT5G53460.
DR KEGG; ath:AT5G53460; -.
DR Araport; AT5G53460; -.
DR TAIR; locus:2178461; AT5G53460.
DR eggNOG; KOG0399; Eukaryota.
DR HOGENOM; CLU_000422_8_2_1; -.
DR InParanoid; Q9LV03; -.
DR OMA; TVFRLQH; -.
DR OrthoDB; 126283at2759; -.
DR PhylomeDB; Q9LV03; -.
DR BioCyc; ARA:AT5G53460-MON; -.
DR BRENDA; 1.4.1.14; 399.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR PRO; PR:Q9LV03; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LV03; baseline and differential.
DR Genevisible; Q9LV03; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
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: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; IDA:TAIR.
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; IDA:TAIR.
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; 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; SSF56235; SSF56235; 1.
DR SUPFAM; SSF69336; SSF69336; 1.
DR TIGRFAMs; TIGR01317; GOGAT_sm_gam; 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; NAD; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..2208
FT /note="Glutamate synthase 1 [NADH], chloroplastic"
FT /id="PRO_0000395200"
FT DOMAIN 117..521
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT REGION 1040..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 117
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT BINDING 1211..1268
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 1264
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1270
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1275
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1995..2009
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT CONFLICT 998
FT /note="I -> V (in Ref. 3; BAF02180)"
FT /evidence="ECO:0000305"
FT CONFLICT 1440
FT /note="G -> R (in Ref. 3; BAF02180)"
FT /evidence="ECO:0000305"
FT CONFLICT 2188
FT /note="D -> V (in Ref. 4; AAM20646)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2208 AA; 241899 MW; CCE65F1AAF76594D CRC64;
MSAASSSSVL HLRTNQQLLS LRSLKNSTSV ASQLAVTSGV SRRRSCTARC SVKKPVIPES
PFLGTRVRRS GSETLQFWRS DGPGRSAKLR TVVKSSFSAV PEKPLGLYDP SYDKDSCGVG
FVAELSGETT RKTVTDSLEM LIRMTHRGAC GCESNTGDGA GILVGLPHDF YAEAATELGF
VLPSAGNYAV GMFFLPTVES RREESKNVFT KVAESLGHSV LGWRLVPTDN SGLGNSALQT
EPIIAQVFLT PTTKSKADFE QQMYILRRVS MVAIRAALNL QHGAMKDFYI CSLSSRTIVY
KGQLKPDQLK DYYYADLGSE RFTSYMALVH SRFSTNTFPS WDRAQPMRVL GHNGEINTLR
GNVNWMRARE GLLKCNELGL SKKELKKLLP IVDVSSSDSG AFDGVLELLV RAGRSLPEAV
MMMIPEAWQN DKNIDPSRKE FYEYLSALME PWDGPALISF TDGRYLGATL DRNGLRPGRF
YITHSGRVIM ASEVGVVDVP PEDVMRKGRL NPGMMLLVDF EKHIVVDDDA LKQQYSLARP
YGEWLKRQKI ELKDIIESVP EAERIAPSIS GVVPASNDDD SMESMGIHGL LSPLKAFGYT
VEALEMLLLP MAKDGSEALG SMGNDTPLAV MSNREKLCFE YFKQMFAQVT NPPIDPIREK
IVTSMECMIG PEGDLTETTE EQCHRLSLKG PLLKIEEMEA IKKMNYRGWR TKVLDITYAK
ERGTKGLEET LDRICDEANE AIKEGYTLLV LSDRAFSATR VAVSSLMAVG AVHHHLVKTL
ARTQVGLVVE SAEPREVHHF CTLVGFGADA ICPYLAVEAV YRLQVDGKIP PKSNGEFHSK
EELVKKYYKA SNYGMMKVLA KMGISTLASY KGAQIFEALG LSSEVIQKCF AGTPSRVEGA
TFEMLARDGL QLHELAFPTR GYAPGSAEAS ALTNPGNYHW RKNGEIHLND PLAIAKLQEA
ARTNSVAAYK EYSKRINELN KQSNLRGLMK FKDADVKIPL DEVEPASEIV KRFCTGAMSY
GSISLEAHTT LAMAMNKLGG KSNTGEGGEL PSRMEPLADG SRNPKRSSIK QIASGRFGVS
SYYLTNADEL QIKMAQGAKP GEGGELPGHK VIGDIAITRN STAGVGLISP PPHHDIYSIE
DLAQLIHDLK NANPGARISV KLVSEAGVGV IASGVVKGHA DHVLIAGHDG GTGASRWTGI
KNAGLPWELG LAETHQTLVA NDLRGRTVLQ TDGQLKTGRD VAVAALLGAE EFGFSTAPLI
TLGCIMMRKC HKNTCPVGIA TQDPVLREKF AGEPEHVINF FFMLAEEVRE IMSGLGFRTV
TEMIGRADML ELDREVVKNN DKLENIDLSL LLRPAAEIRP GAAQYCVQKQ DHGLDMALDQ
ELIALSKSAL EKSLPVYIET PICNVNRAVG TMLSHEVTKR YHLTGLPKDT IHIKFTGSAG
QSLGAFLCPG IMLELEGDSN DYVGKGLSGG KVVVYPPKGS SFDPKENIVI GNVALYGATS
GEAYFNGMAA ERFSVRNSGA KAVVEGLGDH GCEYMTGGTV VVLGKTGRNF AAGMSGGIAY
VLDVDGKFNT RCNLELVDLD KVEDEEDKMT LKMMIQQHQR HTNSQLAQEV LADFENLLPK
FIKVFPRDYK RVLSAMKHEE VSKQAIERAS EEADETEEKE LEEKDAFAEL KNMAAASSKE
EMSGNGVAAE ARPSKVDNAV KNGGFIAYER EGVKYRDPNV RLNDWNEVME ESKPGPLLTT
QSARCMDCGT PFCHQENSGC PLGNKIPEFN ELVYQNRWQE ALNRLLETNN FPEFTGRVCP
APCEGSCVLG IIENPVSIKS IECAIIDKAF EEGWMVPRPP LKRTGKKVAI IGSGPAGLAA
ADQLNKMGHL VTVYERSDRI GGLMMYGVPN MKTDKIDVVQ RRVDLMTKEG INFVVNANIG
KDPSYSLDGL KEENDAIVLA VGSTKPRDLP VPGRDLSGVH FAMEFLHANT KSLLDSNHED
GNYISAKGKK VVVIGGGDTG TDCIGTSIRH GCTNIVNLEL LPQPPSTRAP GNPWPQWPRV
FRIDYGHQEA TTKFGKDPRT YEVLTKRFIG DDNGNVKGLE LVRVSWEKDE TGRFQFKEIE
GSEEIIEADL VFLAMGFLGP EPTLAEKLGL ECDNRSNFKA EYGRFSTTVE GVFAAGDCRR
GQSLVVWAIS EGRQAADQVD KFLTKTDDDE DAKLQQDLNQ MKHNTITN
