ID B5VF99_YEAS6 Unreviewed; 1159 AA.
AC B5VF99;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
DE Flags: Fragment;
GN ORFNames=AWRI1631_40680 {ECO:0000313|EMBL:EDZ73395.1};
OS Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=545124 {ECO:0000313|EMBL:EDZ73395.1, ECO:0000313|Proteomes:UP000008988};
RN [1] {ECO:0000313|EMBL:EDZ73395.1, ECO:0000313|Proteomes:UP000008988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1631 {ECO:0000313|EMBL:EDZ73395.1,
RC ECO:0000313|Proteomes:UP000008988};
RX PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL FEMS Yeast Res. 8:1185-1195(2008).
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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDZ73395.1}.
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DR EMBL; ABSV01000327; EDZ73395.1; -; Genomic_DNA.
DR AlphaFoldDB; B5VF99; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000008988; Unassembled WGS sequence.
DR GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
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; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 2.160.20.60; Glutamate synthase, alpha subunit, C-terminal 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; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR InterPro; IPR002932; Glu_synthdom.
DR InterPro; IPR006005; Glut_synth_ssu1.
DR InterPro; IPR009051; Helical_ferredxn.
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; PF01645; Glu_synthase; 1.
DR Pfam; PF01493; GXGXG; 1.
DR Pfam; PF07992; Pyr_redox_2; 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; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 2.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 3..253
FT /note="Glutamate synthase"
FT /evidence="ECO:0000259|Pfam:PF01645"
FT DOMAIN 333..520
FT /note="Glutamate synthase alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01493"
FT DOMAIN 675..784
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 799..1120
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDZ73395.1"
SQ SEQUENCE 1159 AA; 127481 MW; E529D25AE073623F CRC64;
RSAIKQVASA RFGVTSYYLS DADEIQIKIA QGAKPGEGGE LPAHKVSKDI AKTRHSTPNV
GLISPPPHHD IYSIEDLKQL IYDLKCANPR AGISVKLVSE VGVGIVASGV AKAKADHILV
SGHDGGTGAA RWTSVKYAGL PWELGLAETH QTLVLNDLRR NVVVQTDGQL RTGFDIAVAV
LLGAESFTLA TVPLIAMGCV MLRRCHLNSC AVGIATQDPY LRSKFKGQPE HVINFFYYLI
QDLRQIMAKL GFRTIDEMVG HSEKLKKRDD VNAKAINIDL SPILTPAHVI RPGVPTKFTK
KQDHKLHTRL DNKLIDEAEV TLDRGLPVNI DASIINTDRA LGSTLSYRVS KKFGEDGLPK
DTVVVNIEGS AGQSFGAFLA SGITFILNGD ANDYVGKGLS GGIIVIKPPK DSKFKSDENV
IVGNTCFYGA TSGTAFISGS AGERFGVRNS GATIVVERIK GNNAFEYMTG GRAIVLSQME
SLNAFSGATG GIAYCLTSDY DDFVGKINKD TVELESLCDP VEIAFVKNLI QEHWNYTQSD
LAARILGNFN HYLKDFVKVI PTDYKKVLLK EKAEAAKAKA KATSEYLKKF RSNQEVDDEV
NTLLIANQKA KEQEKKKSIT ISNKATLKEP KVVDLEDAVP DSKQLEKNSE RIEKTRGFMI
HKRRHETHRD PRTRVNDWKE FTNPITKKDA KYQTARCMDC GTPFCLSDTG CPLSNIIPKF
NELLFKNQWK LALDKLLETN NFPEFTGRVC PAPCEGACTL GIIEDPVGIK SVERIIIDNA
FKEGWIKPCP PSTRTGFTVG VIGSGPAGLA CADMLNRAGH TVTVYERSDR CGGLLMYGIP
NMKLDKAIVQ RRIDLLSAEG IDFVTNTEIG KTISMDELKN KHNAVVYAIG STIPRDLPIK
GRELKNIDFA MQLLESNTKA LLNKDLEIIR EKIQGKKVIV VGGGDTGNDC LGTSVRHGAA
SVLNFELLPE PPVERAKDNP WPQWPRVMRV DYGHAEVKEH YDRDPREYCI LSKEFIGNDE
GEVTAIRTVR VEWKKSQSGV WQMVEIPNSE EIFEADIILL SMGFVGPELI NGNDNEVKKT
RRGTIATLDD SSYSIDGGKT FACGDCRRGQ SLIVWAIQEG RKCAASVDKF LMDGTTYLPS
NGGIVQRDYK LLKELASQV
//
