ID A0A0L9U7D8_PHAAN Unreviewed; 1617 AA.
AC A0A0L9U7D8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 28-JAN-2026, entry version 37.
DE RecName: Full=glutamate synthase (ferredoxin) {ECO:0000256|ARBA:ARBA00039085};
DE EC=1.4.7.1 {ECO:0000256|ARBA:ARBA00039085};
GN ORFNames=LR48_Vigan03g210200 {ECO:0000313|EMBL:KOM38720.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
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; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM38720.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
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|ARBA:ARBA00001927};
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. {ECO:0000256|ARBA:ARBA00037928}.
CC -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC {ECO:0000256|ARBA:ARBA00004802}.
CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000256|ARBA:ARBA00004470}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
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DR EMBL; CM003373; KOM38720.1; -; Genomic_DNA.
DR STRING; 3914.A0A0L9U7D8; -.
DR Gramene; KOM38720; KOM38720; LR48_Vigan03g210200.
DR OMA; LKTGWDV; -.
DR UniPathway; UPA00045; -.
DR Proteomes; UP000053144; Chromosome 3.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0019676; P:ammonia assimilation cycle; IEA:TreeGrafter.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd00713; GltS; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR FunFam; 2.160.20.60:FF:000003; Ferredoxin-dependent glutamate synthase, chloroplastic; 1.
DR FunFam; 3.20.20.70:FF:000084; Ferredoxin-dependent glutamate synthase, chloroplastic; 1.
DR FunFam; 3.20.20.70:FF:000127; Ferredoxin-dependent glutamate synthase, chloroplastic; 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; IPR050711; ET-N_metabolism_enzyme.
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 InterPro; IPR002213; UDP_glucos_trans.
DR PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11938:SF133; GLUTAMATE SYNTHASE (NADH); 1.
DR Pfam; PF00310; GATase_2; 2.
DR Pfam; PF04898; Glu_syn_central; 1.
DR Pfam; PF01645; Glu_synthase; 1.
DR Pfam; PF01493; GXGXG; 1.
DR Pfam; PF00201; UDPGT; 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); 2.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 101..543
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 1594..1617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1617 AA; 175793 MW; 51524908E9225A1F CRC64;
MALHSVSSVP HVLRLSEPFP SLHNAHLLLD PVPFRRKPKR RTRKLRAFPA PSPLSHSSVK
AVLHIDRTAA DNSLQASPAS SSSSQPQVAN LEDILSERGA CGVGFIANLE NKGSHEIVKD
ALNALSCMEH RGGCGADNDS GDGSGLMTAV PWDLLDNWAN KQGIASFDKS HTGVGMVFLP
KDAQLLNEAK KVIVNIFRQE GLEVLGWRPV PVNTSVVGYY AKETMPNIQQ VFVKIVKEEN
VDDIERELYI CRKLIEKAVS SESWGNELYF CSLSNQTIVY KGMLRSEVLG LFYSDLQNDL
YKSPFAIYHR RYSTNTSPRW PLAQPMRLLG HNGEINTIQG NLNWMQSREP SLKSPVWRDR
ENEIRPYGNP KASDSANLDS AAELLIRSGR SPEEAMMILV PEAYKNHPTL TIKYPEKVFV
THCGWNSVFE AVCEGVPMAA WPLYAEQKPN KVILVEEMKA LDFYDYYKGQ MEAWDGPALL
LFSDGKTVGA CLDRNGLRPA RYWRTSDNMV YVASEVGVVP VDDSKVVLKG RLGPGMMITV
DLPGGQVYEN TEVKKRVALS NPYGKWIKEN LRSLKPGNFL SASLMDNEAV LRNQQAFGYS
SEDVQMVIES MASQGKEPTF CMGDDIPLAA LSQKPHMLFD YFKQRFAQVT NPAIDPLREG
LVMSLEVNIG KRGNLLEVGP ENASQVMLSS PVLNEGELES LLKDSQLNPQ VLPTFFDITK
GIEGSLEKAL NKLCEAADEA VRNGSQLLVL SDRSDALEPT HPAIPILLAV GTVHQHLILN
GLRTSASIIA DTAQCFSTHQ FACLIGYGAS AVSPYLALET CRQWRLSNKT VNLMRNGKMP
TVSIEQAQKN YCKAVKAGLL KILSKMGISL LSSYCGAQIF EVYGLGKEIV DLAFRGSVSK
IGGLTFDEVA RETLSFWVKA FSEDTAKRLE NFGFIQSRPG GEYHANNPEM SKLLHKAVRQ
KSQSAFSVYQ QYLANRPANV LRDLLEFKSD RAAIPVGKVE PASSIVQRFC TGGMSLGAIS
RETHEAIAIA MNRLGGKSNS GEGGEDPVRW KPLTDVVDGY SPTLPHLKGL QNGDTATSAI
KQVASGRFGV TPTFLANADQ LEIKIAQGAK PGEGGQLPGK KVSMYIARLR NSKPGVPLIS
PPPHHDIYSI EDLAQLIFDL HQVNPRAKVS VKLVAEAGIG TVASGVAKGN ADIIQISGHD
GGTGASPISS IKHAGGPWEL GLTESHQTLI ENGLRERVIL RVDGGFRSGV DVMMAAIMGA
DEYGFGSVAM IATGCVMARI CHTNNCPVGV ASQREELRAR FPGVPGDLVN YFLYVAEESA
GLSKWSSTEI RNQEPHTNGP VLDDGLLADP EIADAIENEK VVNKTVNIYN IDRAVCGRIA
GVIAKKYGDT GFAGQLNITF TGSAGQSFAC FLTPGMNIRL VGEANDYVGK GIAGGELVIT
PVDKTGFEPE DAAIVGNTCL YGATGGQVFV RGRAGERFAV RNSLAEAVVE GTGDHCCEYM
TGGCVVVLGK VGRNVAAGMT GGLAYILDED DTLIPKVNRE IVKIQRVSAP VGQMQLKSLI
EAHVEKTGST KGAAILKDWD KYLSLFWQLV PPSEEDTPEA NAKYDTTTAE QVSFQSA
//
