GLTB_MAIZE
ID GLTB_MAIZE Reviewed; 1616 AA.
AC P23225;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Ferredoxin-dependent glutamate synthase, chloroplastic;
DE EC=1.4.7.1;
DE AltName: Full=Fd-GOGAT;
DE Flags: Precursor;
GN Name=GLSF;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 97-109 AND 790-802.
RC STRAIN=cv. Golden cross Bantam T51; TISSUE=Leaf;
RX PubMed=1989968; DOI=10.1016/s0021-9258(18)52204-3;
RA Sakakibara H., Watanabe M., Hase T., Sugiyama T.;
RT "Molecular cloning and characterization of complementary DNA encoding for
RT ferredoxin-dependent glutamate synthase in maize leaf.";
RL J. Biol. Chem. 266:2028-2035(1991).
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;
CC Note=Binds 1 [3Fe-4S] cluster.;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
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 -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC -!- TISSUE SPECIFICITY: Mostly in green tissues and lesser in non-
CC photosynthetic tissues.
CC -!- SIMILARITY: Belongs to the glutamate synthase family. {ECO:0000305}.
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DR EMBL; M59190; AAA33463.1; -; mRNA.
DR PIR; A38596; A38596.
DR RefSeq; NP_001105693.1; NM_001112223.1.
DR AlphaFoldDB; P23225; -.
DR SMR; P23225; -.
DR STRING; 4577.GRMZM2G036609_P02; -.
DR MEROPS; C44.003; -.
DR PaxDb; P23225; -.
DR PRIDE; P23225; -.
DR GeneID; 542710; -.
DR KEGG; zma:542710; -.
DR MaizeGDB; 40403; -.
DR eggNOG; KOG0399; Eukaryota.
DR OrthoDB; 126283at2759; -.
DR BRENDA; 1.4.7.1; 6752.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00691.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P23225; baseline and differential.
DR GO; GO:0009570; C:chloroplast stroma; 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 1: Evidence at protein level;
KW 3Fe-4S; Amino-acid biosynthesis; Chloroplast; Direct protein sequencing;
KW FAD; Flavoprotein; FMN; Glutamate biosynthesis; Glutamine amidotransferase;
KW Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..97
FT /note="Chloroplast"
FT CHAIN 98..1616
FT /note="Ferredoxin-dependent glutamate synthase,
FT chloroplastic"
FT /id="PRO_0000011616"
FT DOMAIN 98..497
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT ACT_SITE 98
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 1176..1233
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 1229
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1235
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 1240
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1616 AA; 175173 MW; 67724CBFA0AEB053 CRC64;
MATLPRAAPP TPAALLPLPR AAPPLLLAGR AAAARRSRLR ARGPSAAARR SWVVASAASS
SSRAVVGGVA RREAPPAPQK PTQQAADLNH ILSERGACGV GFVANLKNMS SFDIVRDALM
ALGCMEHRGG CGADSDSGDG AGLMSAVPWD LFDDWASKQG LALFDRRNTG VGMVFLPQDE
KSMEEAKAAT EKVFVDEGLE VLGWRPVPFN VSVVGRNAKE TMPNIQQIFV KVAKEDNADD
IERELYISRK LIERAAKSFS WADELYFCSL SSRTIVYKGM LRSEVLGQFY LDLQNELYKS
PFAIYHRRFS TNTSPRWPLA QPMRLLGHNG EINTIQGNLN WMRSRETTLK SPVWRGREHE
ICPFGDPKAS DSANLDSTAE LLLRSGRSPA EALMILVPEA YKNHPTLSIK YPEVTDFYDY
YKGQMEAWDG PALLLFSDGR TVGATLDRNG LRPARYWRTS DDFVYVASEV GVIPMDESKV
VMKGRLGPGM MITVDLQTGQ VLENTEVKKT VASASPYGTW LQECTRLIKP VNFLSSTIMD
NETVLRHQQA FGYSSEDVQM VIESMASQGK EPTFCMGDDI PLAVLSQRPH LLYDYFKQRF
AQVTNPAIDP LREGLVMSLE VNIGKRGNIL EVGPENADQV ALSSPVLNEG ELETLLNDSK
LKPKVLSTYF DIRKGLDGSL DKTIQALCEE ADAAVRSGSQ LLVLSDRSEA PEPTRPAIPI
LLAVGAIHQH LIQNGLRMSA SIVADTAQCF STHHFACLIG YGASAVCPYL ALETCRQWRL
SNKTLNLMRN GKMPTVTIEQ AQRNFIKAVK SGLLKILSKM GISLLSSYCG AQIFEIYGLG
QEVVDLAFCG SVSKIGGLTL DELGRETLSF WVKAFSEDTA KRLENFGFIQ SRPGGEYHAN
NPEMSKLLHK AIREKRDNAY TVYQQHLASR PVNVLRDLLE LKSDRAPIPI GKVESATSIV
ERFCTGGMSL GAISRETHEA IAIAMNRIGG KSNSGEGGED PIRWNPLTDV VDGYSPTLPH
LKGLQNGDTA TSAIKQVASG RFGVTPTFLV NADQIEIKIA QGAKPGEGGQ LPGKKVSAYI
ARLRNSKPGV PLISPPPHHD IYSIEDLAQL IYDLHQINPK AKVSVKLVSE AGIGTVASGV
SKANADIIQI SGHDGGTGAS PISSIKHAGG PWELGLTETN QTLIQNGLRE RVVLRVDGGF
RSGQDVLIAA AMGADEYGFG SVAMIATGCV MARICHTNNC PVGVASQREE LRARFPGVPG
DLVNYFLFVA EEVRAALAQL GYEKLDDIIG RTDLLKPKHI SLVKTQHIDL GYLLSNAGLP
EWSSSQIRSQ DVHTNGPVLD ETILADPEIA DAIENEKEVS KAFQIYNVDR AVCGRVAGVI
AKKYGDTGFA GQLNITFNGS AGQSFGCFLT PGMNIRLVGE ANDYVGKGMA GGELVVVPVD
KTGFVPEDAT IVGNTCLYGA TGGQVFVRGK AGERFAVRNS LCQAVVEGTG DHCCEYMTGG
CVVVLGKAGR NVAAGMTGGL AYILDEDDTL VPKVNKEIVK MQRVNAPAGQ MQLKGLIEAY
VEKTGSEKGI AILREWEAYL PLFWQLVPPS EEDSPEACAE FERVLAKQAT TQLSAK
