ID G0W3F6_NAUDC Unreviewed; 2152 AA.
AC G0W3F6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN Name=NDAI0A01860 {ECO:0000313|EMBL:CCD22344.1};
GN OrderedLocusNames=NDAI_0A01860 {ECO:0000313|EMBL:CCD22344.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD22344.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD22344.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE580267; CCD22344.1; -; Genomic_DNA.
DR RefSeq; XP_003667587.1; XM_003667539.1.
DR STRING; 1071378.G0W3F6; -.
DR GeneID; 11494400; -.
DR KEGG; ndi:NDAI_0A01860; -.
DR eggNOG; KOG0399; Eukaryota.
DR HOGENOM; CLU_000422_8_2_1; -.
DR OMA; WDGPAAM; -.
DR OrthoDB; 20503at2759; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000000689; Chromosome 1.
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; 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; 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; 1.
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; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 2.
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:UP000000689}.
FT DOMAIN 53..461
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT ACT_SITE 53
FT /note="For GATase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-1"
FT BINDING 1192
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1198
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1203
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
SQ SEQUENCE 2152 AA; 238737 MW; 9BC0842875CC0205 CRC64;
MQLKSEPFDL LEDAYEGGSY NIDQLTHENT KSWANVIPDK CGLYDPDYER DACGVGFVAN
IKGEPSHKII SDAKFLLVNM THRGAVSTDG NGDGAGILVG IPHEFMKREF KLDLNIDIPE
RGKYAVGNVF FQKIDNEDQD SLKRQEKVDA LNKNKKIFED LANSLKLNVL GWRNVPVDTT
ILGSVAKSRE PTILQPMIVP LNDTEEFNET EFNTNLYLLR KQASNTIGIE NWFYACSLNN
KTIVYKGQLT PAQVYSYYPD LTNAYFQSHL ALVHSRFSTN TFPSWDRAQP LRWLAHNGEI
NTLRGNKNWM HSREGSMYSE TFKDQLDKLY PIIEEGGSDS AALDNVLELL TTNGNLSLPE
AIMMLVPEAY HEDMDSDLKA WYDWAACLME PWDGPALLTF TDGRYCGAAL DRNGLRPCRY
YITSDDRVIC ASEVGVIPID NALVIEKGKL KPGDLFLADT ETGELVDTKK LKLQIAKKKD
FKSWLSKVIK LDDLLEKTKN YIPTEFVPKE GIPSFKVQQD PRILANGYTF EQVSLLLTPM
ALTGKEALGA MGNDSPLACL NRDPVLLYDY FRQLFAQVTN PPIDPIREAN VMSLECFVGP
QGNLLDINQS QCERLLLRSP ILFWEEFQAL KQIDKAYPSW SVGEIDITFS KSAGLLGYTA
TIERITKEAS AAIEAGNKII FISDRKLGED RVSISSLIAV STIHHHLIRN RQRSQTALIL
ETAEAKEIHH FCTLLGYGCD GIFPYLVMET LVRMNREGLI RNVDDDDHNT DDKTLLSNYK
HAVDAGIMKV MSKMGISTLA SYKGAQIFEA LGLDNSVIDL SFPGTASRIK GVTFEYLAQD
AFSFHERGYP SRKTANRSVT LPEAGEYHWR DGGYKHVNDP TAIASLQDSV RNKNDASWEL
YVKKEMEAIK DCTLRGLLEL DYDNSTAIPI EQVEPWTEIA RRFASGAMSY GSISMEAHST
LAIAMNRLGA KSNCGEGGED AERSIVSPNG DTMRSAIKQV ASARFGVTSY YLSDADEIQI
KIAQGAKPGE GGELPAHKVS KEIAKTRHST PNVGLISPPP HHDIYSIEDL KQLIYDLKCA
NPRAGISVKL VSEVGVGIVA SGVAKAKADH ILISSHDGGT GAARWTSVKY AGLPWELGLA
ETHQTLVLND LRRNVVVQTD GQLRTGFDLA VAILLGAESF TLATIPLIVM GCVMLRRCHL
NSCAVGIATQ DPYLRSKFQG QPEHVINFFY YLIQDLRMIM AKLGFRTVDE MVGHSEKLKK
RADANAKAFN IDLSPILTPA HEIRPGVPTK FTKKQDHKLH TRLDNKLIDE AEVTLDRGLP
VNIDAQIINT DRALGATLSY RVSKRFGENG LPQDTIVVNI EGSAGQSFGA FLAPGITFIL
DGDANDYVGK GLSGGIIVVR PPKGSKFKSD ENVIVGNTCL YGATSGTVFI SGGVGERFGV
RNSGATVVVE RIKGNNAFEY MTGGRAIVLS QMESLNAFSG ATGGIAYCLV SDYEAFTTKI
NKDTVELENL QDPVEIAFVK NLIQEHFHYT KSELAEKILA NFNHYLKNFV KVIPTDYKKV
LDKEAADKAK EKATATANYL KNFKALQSAP NDSIDATNGE INDLMRSRKA NKAIVSHKST
LNEPEVVDLE DAVPDPEQLE KNAEKIEKLR GFMKYARRHE TYRSPSTRVK DWKEFVKPIS
KKDAKYQTAR CMDCGTPFCS ADTGCPLSNV IPKFNELVFK NQWKLALDKL LETNNYPEFT
GRVCPAPCEG ACTLGISENP VGIKSIERII IDNGFKEGWI KPCPPEIRTD KRIAVIGSGP
AGMACADQLN KAGHNVTVYE RADRCGGLLM YGIPNMKLEK SIVDRRFDIL RAEGIEFICN
TEIGKDISME ELQNEYDAVV YAIGSTIPRD LNIKGRDLKN IDFAMELLED NTKALLNNDL
ETIRKEVEGK KVVVIGGGDT GNDCLGTSVR HGAKSVINFE LLPCPPNERA RDNPWPQWPR
IMRVDYGHSE VKEHYGNDPR EYCIFAKEFI GNENNEVKAI KTVRVEWKKS ESGVWQMVEI
PNTEETFEAD LVLLSMGFVG PELIEDANVT KTSKGTIMTD NDASYHVAGN VYAAGDCRRG
QSLIVWAIQE GRKCAHSIDI DLMGSTKLPC NGGIVKRDFN LLEDLAAEVA YA
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