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Database: UniProt
Entry: A0A0B1PD66_UNCNE
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ID   A0A0B1PD66_UNCNE        Unreviewed;      2116 AA.
AC   A0A0B1PD66;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   13-SEP-2023, entry version 36.
DE   RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE            EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN   ORFNames=EV44_g4391 {ECO:0000313|EMBL:KHJ34609.1};
OS   Uncinula necator (Grape powdery mildew).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Erysiphe.
OX   NCBI_TaxID=52586 {ECO:0000313|EMBL:KHJ34609.1, ECO:0000313|Proteomes:UP000030854};
RN   [1] {ECO:0000313|EMBL:KHJ34609.1, ECO:0000313|Proteomes:UP000030854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=c {ECO:0000313|Proteomes:UP000030854};
RX   PubMed=25487071;
RA   Jones L., Riaz S., Morales-Cruz A., Amrine K.C., McGuire B., Gubler W.D.,
RA   Walker M.A., Cantu D.;
RT   "Adaptive genomic structural variation in the grape powdery mildew
RT   pathogen, Erysiphe necator.";
RL   BMC Genomics 15:1081-1081(2014).
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}.
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:KHJ34609.1}.
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DR   EMBL; JNVN01000790; KHJ34609.1; -; Genomic_DNA.
DR   STRING; 52586.A0A0B1PD66; -.
DR   HOGENOM; CLU_000422_8_2_1; -.
DR   OMA; TVFRLQH; -.
DR   OrthoDB; 20503at2759; -.
DR   UniPathway; UPA00045; -.
DR   UniPathway; UPA00634; UER00690.
DR   Proteomes; UP000030854; Unassembled WGS sequence.
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:UP000030854}.
FT   DOMAIN          60..463
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   REGION          962..985
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        54
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000187-1"
FT   BINDING         1186
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT   BINDING         1192
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT   BINDING         1197
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
SQ   SEQUENCE   2116 AA;  234153 MW;  9492A68FA467F1C8 CRC64;
     MAYRDDFNDR QAQLDAEKLE YHEYVCLEPN SSSWAGALPS KQGLYDPELE KDACGVGFTC
     NIKGVASHKI VSDARNLLCN MTHRGAVGSD ARDGDGAGVM TSIPHKFFIK NFERETNVKL
     PLQGQYAVGN LFFKPDEETL QKSKIQLEKI AETLGLRVLG WRQVPKDSTL LGPAAASREP
     VILQPFVVLR SAYDLSNSPQ DIDPVDFDER HFERQLFILR KRATHAVGLQ NWFYICSLSN
     KNIVYKGQLS PSQVYDYFYD LVNADYEVHF ALVHSRFSTN TFPSWDRAQP LRWVAHNGEI
     NTLRGNKNWM RAREGLMASE VFGDDLESLY PIIEEGGSDS AAFDNVLELL TINGVLSLPE
     AIMLMVPEAW EGNALMDPAK TAFYEWAACL MEPWDGPALF TFSDGRYCGA NLDRNGLRPC
     RFYITDDDRI ICASEVTTLN INPEKIIHKG RLQPGKMLLV DTLAGRIIDD GELKKTVSMR
     YDFGSWVQKE LLLLPKIHEN LVNQTSMDLS SHLNELSIQE DPMLAAFGYS FEQVSLLLAP
     MASDEKEALG SMGNDAPLAC LAKEPRLLYE YFRQLFAQVT NPPIDPIREA MVMSLSSYVG
     PQGNLLKMDA SQCRRLSLRS PILSIPELNS LKNITKIHKD WTVKVIDLTF PKCEGTDGYI
     KHLDEICRQA TAAIEHQDKI ILLSDRATCA DRLPVSALLA CGMVHHHLVT NRWRSLAALI
     VETAEAREVH HMCVLLGYGA DAINPYLAME CIMKLNREGL IKKKLDDQTL IRNYKYSADG
     GILKVMSKMG ISTLASYKGA QIFEALGIDD TVVNRCFKGT ATRIKGVTFD LIAADAFRFH
     EKGFPSRQTI GIKGLIESGE YHWRDGGQPH INDPTSIANI QDAVRTKNDK SYEAYSISEY
     EQIKSCTLRG MLDFKFDEST PVPINQVEPW TEIVRRFCTG AMSYGSISME AHSTLAIAMN
     RLGGKSNTGE GGEDPERSER MSNGDTMRSA IKQVASGRFG VTSNYLADSD ELQIKMAQGA
     KPGEGGELPG HKVSKSIART RHSTPGVGLI SPPPHHDIYS IEDLKQLIYD LKCSNPRARI
     SVKLVSETGV GVVASGVAKA KADHILISGH DGGTGASRWT GIKYAGLPWE LGLAETHQTL
     VLNDLRGRVI VQTDGQLRTG RDVAIACLLG AEEWGFATTP LIAMGCVFMR KCHLNTCPVG
     IASQDPELRK KFQGTPEHVI NFFYYIANEL RAIMAKLGFR TINEMVGHAE RLRVRDDLRT
     SKTENIDLSL ILTPAHKLRP GVATFNVRKQ DHRLYLRLDN KLISEAELTL DKGLPSRIEC
     DIMNTDRAMG TSLSYQVSKR YGEEGLPIDT IHVNIKGSAG QSFGAFLAPG ITLELEGDAN
     DYVGKGLSGG RLIIYPPRAA IFKAEENMLI GNVCLYGATS GTCYFRGIAA ERFAVRNSGA
     TAVVEGVGDH GCEYMTGGRI LVLGSTGRNF AAGMSGGIAY ILDINQDFVT KLNHDMVEIS
     GLDNPSEIAF VRGLIEDHHH YTGSELAARI LVDFNRALPR FVKVLPIDYK RVIAEEAAKA
     AEAKRAAFEM PNLPGIQLRE KHDVKKSTSS ILDIEETVGD AATVKSKSLV LDKTRGFMRY
     QRRSEKYRST KSRVRDWAEL SQRLDEDELK YQAARCMDCG VPFCQSDTGC PISNIIPKWN
     ELVFQDQWRD ALNRLLMTNN FPEFTGRVCP APCEGACVLG INEDPVGIKS IECAIIDRGF
     DMGWLVPNPP KIRTGKTVAI IGSGPAGLAC ADQLNKAGHL VTVYERSDRP GGLLMYGIPN
     MKLDKKIVTR RTNLLAAEGI VFKTGITVGE DITLMKLKDE NDAVVIATGA TVARDLNIKN
     RSLEGIHFAM EFLHANTKSL LDSGLTDGAY ISAKDKDVIV IGGGDTGNDC IGTSVRHGAK
     SVTNFELLPQ PKSERTRDNP WPQWPRVYRV DYGHAEVKQH MGHDPREYCV MSQEFVDDGT
     GKVKGINTHR VEWTKSATGG WDMTKVEGSE KFFPADLVLL SMGFLGPDAR ILDDKITKDG
     RSNIKTPLGK YHTNVEGIFA AGDCRRGQSL IVWGINEGRQ SAREIDIWLE GCTRLPVAGG
     IIKQTAQQVL HSIKVV
//
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