ID A0A0R0EJ07_SOYBN Unreviewed; 2018 AA.
AC A0A0R0EJ07;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN Name=100784900 {ECO:0000313|EnsemblPlants:KRG94150};
GN ORFNames=GLYMA_19G065600 {ECO:0000313|EMBL:KRG94150.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRG94150.1};
RN [1] {ECO:0000313|EMBL:KRG94150.1, ECO:0000313|EnsemblPlants:KRG94150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRG94150};
RC TISSUE=Callus {ECO:0000313|EMBL:KRG94150.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRG94150}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRG94150};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRG94150.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRG94150.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00024267};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|PIRSR:PIRSR000187-2};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000256|PIRSR:PIRSR000187-2};
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. {ECO:0000256|ARBA:ARBA00004944}.
CC -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC {ECO:0000256|ARBA:ARBA00004802}.
CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
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DR EMBL; CM000852; KRG94150.1; -; Genomic_DNA.
DR RefSeq; XP_006604057.1; XM_006603994.2.
DR EnsemblPlants; KRG94150; KRG94150; GLYMA_19G065600.
DR GeneID; 100784900; -.
DR Gramene; KRG94150; KRG94150; GLYMA_19G065600.
DR OrthoDB; 20503at2759; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000008827; Chromosome 19.
DR ExpressionAtlas; A0A0R0EJ07; baseline and differential.
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; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR01317; GOGAT_sm_gam; 1.
DR PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
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; 2.
DR PIRSF; PIRSF000187; GOGAT; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding 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 3: Inferred from homology;
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291, ECO:0000256|PIRSR:PIRSR000187-2};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000187-
KW 2}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827}.
FT DOMAIN 1..320
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 839..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1474..1495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1475..1489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1063
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1069
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1074
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
SQ SEQUENCE 2018 AA; 222238 MW; D8B44324D62FA483 CRC64;
MSFPLLPYAK VAESLGHTVL GWRSVPIDNT GLGKSALQTE PVIEQVFLTP SAQSKIDLER
QMYILRKLCM AAITSALNLQ NDGIADFYIC SLSSRTVVYK GQLTPAQLRD YYFADLGNER
FTSYMALIHS RFSTNTFPSW DRAQPMRVLG HNGEINTLRG NVNWMKAREG LLKCKELGLS
ENELKKLLPI VDANSSDSGA FDGVLEFLLH SGKSLPEAVM MMIPEAWQND KNMDSQRKAF
YEYFSALMEP WDGPALISFT DGHYLGATLD RNGLRPGRFY VTHSGRVIMA SEVGVVDIPP
EDVCRKGRLN PGMMLLVDFV KHTVVNDDAL KEQYSLARPY EDWLKRQKIE LKDIVNSVHE
SERVPPPIAG VAPLSNDDAD MENMGIHGLL VPLKAFGYTV ESLEMLLLPM AKDGVEALGS
MGNDTPLAVM SKREKLTFEY FKQMFAQVTN PPIDPIREKI VTSMQCMVGP EGDLTEITEE
QCHRLSLKGP LLSTEEMEAI KKMNYRGWRS KVIDITYSKE CGKRGLDEAL DRMCAEAHDA
INEGYTTLVL SDRAFSKKRI SVSSLLAVGA VHQHLVKTLE RTRVALIVES AEPRKVHHFC
TLVGFGADAI CPYLAIDAIW RLQVDGKIPP KASGEFHSKD ELVKKYFKAS NYGMMKVLAK
MGISTLASYK GAQIFEALGL SSEVIEKCFA GTPSRVEGAT FEMLACDAFQ LHELAFPSWV
FSPGSAEALA LPNPGDYHWR KGGEVHLNDP LAMAKLQEAA RTNSVDAYKQ YSKLIHELNK
ACNLRGLLKF KETAVKIPID EVEPASEIVK RFCTGAMSYG SISLEAHTAL AMAMNKIGGK
SNTGEGGEQP SRMEPLPDGS MNPKRSAIKQ VASGRFGVSS YYLTNADELQ IKMAQGAKPG
EGGELPGHKV IGDIAVTRNS TSGVGLISPP PHHDIYSIED LAQLIHDLKN ANPAARISVK
LVSEAGVGII ASGVVKGHAD HVLISGHDGG TGASRWTGIK NAGLPWELGL AETHQTLVAN
DLRGRTVLQT DGQLKTGRDV AIATLLGAEE FGFSTAPLIT LGCIMMRKCH KNTCPVGIAT
QDPVLREKFA GEPEHVINFF FMVAEEMREI MSQLGFRRVN EMVGRSDMLE VDKEVVKSNE
KLENIDLSLL LRPAAELRPE ASQYCVQKQD HGLDMALDNK LISLSSAALE KGLPVYIETP
IYNVNRAVGT MLSHEVTKLY HLAGLPNDTI HIRFTGSAGQ SFGAFLCPGI TLELEGDSND
YVGKGLSGGK IVVYPPKESN FDPKENIVIG NVALYGATRG EAYFNGMAAE RFCVRNSGAK
AVVEGVGDHG CEYMTGGTVV VLGKTGRNFA AGMSGGIAYV LDVDGKFQSR CNLELVDLDK
VEEEEDILTL RMLIQQHQRH TNSRLAKEVL DDFENLLPKF IKVFPREYKR VLASMKSEET
SKDAVVHAAK HEQDDEAQAV EKDAFEELKK LATASLNEKP SQAESPKRPS QVTGAIKHRG
FVSYEREGVQ YRDPNVRMTD WKEVMEETKP GPLLKTQSAR CMDCGTPFCH QENSGCPLGN
KIPEFNELVY QNRWHEALER LLETNNFPEF TGRVCPAPCE GSCVLGIIEN PVSIKSIECA
IIDKAFEEGW MVPRPPVQRT GKRVAIVGSG PSGLAAADQL NKMGHTVTVY ERADRIGGLM
MYGVPNMKTD KVDIVQRRVN LMAEEGIDFV VSANVGHDPL YSLDRLREEN DAIVLAVGAT
KPRDLPVPGR ELSGVHFAME FLHANTKSLL DSNLEDGNYI SAKGKKVVVI GGGDTGTDCI
GTSIRHGCSS VVNLELLPQP PPTRAPGNPW PQWPRIFRVD YGHQEAAAKF GKDPRSYEVL
TKRFIGDENG VLKGLEVIRV CWEKDATDKF QFKEIEGSEE IIEADLVLLA MGFLGPESTI
AEKLGVDRDN MSNFKAGYGH FSTNVKGVFA AGDCRRGQSL VVWAISEGRQ AAAQVDNYLV
KEDKDHRNQD GLVKRQQGLY KKQHGSSKHT VMTYRWLL
//
