ID N1PYD3_DOTSN Unreviewed; 2143 AA.
AC N1PYD3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN ORFNames=DOTSEDRAFT_69369 {ECO:0000313|EMBL:EME47415.1};
OS Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS fungus) (Mycosphaerella pini).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX NCBI_TaxID=675120 {ECO:0000313|EMBL:EME47415.1, ECO:0000313|Proteomes:UP000016933};
RN [1] {ECO:0000313|Proteomes:UP000016933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT but also signatures of common ancestry.";
RL PLoS Genet. 8:E1003088-E1003088(2012).
RN [2] {ECO:0000313|EMBL:EME47415.1, ECO:0000313|Proteomes:UP000016933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB446536; EME47415.1; -; Genomic_DNA.
DR STRING; 675120.N1PYD3; -.
DR EnsemblFungi; EME47415; EME47415; DOTSEDRAFT_69369.
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; UP000016933; 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; 1.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like 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; 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:UP000016933}.
FT DOMAIN 61..470
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 969..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1589..1620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 61
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 2143 AA; 236574 MW; 2EB566D63C879EB0 CRC64;
MGRVSFADDV KNEATIDEID EPQEEHVNIY PYQNTPENKS WAGALPLKQG LYDPELEKDA
CGVGFAAHIK GKASHKIVTD ARNLLCNMTH RGAVGSDARD GDGAGVMTSV PHKFFVKNFE
KEQGIKLPEI GKYAAGNIFF KPEEDALKET LDKFEDIADQ LDLRVLGWRE VPKDSTLLGP
AAKSREPIIL QPFVVMKSWY GSGKEPASDF NDKFEEQAFE RQLYVLRKRA THVVGLHNWF
YICSLSNKNM VYKGQLSPVQ VYDYYHDLVN VDYEGHFALV HSRFSTNTFP SWDRAQPLRW
AAHNGEINTL RGNKNWMRAR EGVLKSDLFG DELEALYPII EDGGSDSAAF DNVLELLMIN
GVLSLPEAVM LMVPEAWQGN DSIDDKKQAF YEWAACMMEP WDGPALFTFS DGRYCGANLD
RNGLRPCRYY VLDDDRIICA SEVGTIAIDP STVVQKGRLQ PGRMLLVDTR AGRIIDDAEL
KETVANRQDF RSWMDSQLLV LPDILKTLLE KGTDLSLQLT EAKVQEDPRL KAFGYSLEQV
SLLLAPMAAD SKEALGSMGN DAPLACLAQQ PRLLFEYFRQ LFAQVTNPPI DPIRESVVMS
LGSYVGPQGN LLEMNKEQAH RLYLPSPMLS VEEFNALTNV TQLYSDWTVA TIDITFPKAD
GIAGYYDALD RICEAASQAI ENGDNIIILS DRKTSAERVA ISSLLATGMV HHHLVRNRWR
AQAALVVETA EAREVHHMCV LVGYGADAIC PYLAIECILK LHREGLIRKK ISPEDLIGNY
KHSCDGGILK VMSKMGISTL QSYKGAQIFE ALGIDDAVVD RCFTGTATRI RGMTFELIAQ
DAFALHEKGY PSRDIHEIPG LAETGEYHWR DGGEPHVNDP VSIANIQDAV RMKNDKSYEA
YSRSEYEQIK NCTLRGLLDF DFDAFNPIPV EQVEPWTEIV RRFVTGAMSY GSISMESHST
LAVAMNRLGG KSNTGEGGED PERSLPMDNG DTMRSAIKQI ASGRFGVTSN YLADADELQI
KMAQGAKPGE GGELPGHKVS GPIAKTRHST PGVGLISPPP HHDIYSIEDL KQLIYDLKCS
NPRARVSVKL VSETGVGIVA SGVAKAKADH ILISGHDGGT GASRWTGIKY AGLPWELGLA
ETHQTLVLND LRGRVVVQTD GQLRTGRDVA LACLLGAEEF GFATAPLIAM GCIMMRKCHL
NTCPVGIATQ DPELRKKFKG TPEHVINFFY YISNELRAIM AKFGFRTVNE MVGHTEALKV
REDLRNAKTE NIDLSLILTP AHTLRSGVAT YNVRKQDHKL HVRLDNKLIA ESELALEKGL
PCRIECDIVN TDRAMGATLS YQISKRYGEK GLPQDTIHAN IRGSAGQSFG AYLAPGVTLE
LEGDANDYVG KGLSGGRLII YPPRSAVFKA EENVIIGNVC LYGATMGTCF FRGVAAERFA
VRNSGVTAVV EGVGDHGCEY MTGGRVVVLG STGRNFAAGM SGGIAYVLDL HNDFEGKVNQ
EMVELSSLED PHEIAFLRGL IEDHHHYTGS ELAARILLDF NRALPHFVKV LPTDYKRVME
EEAKKAEEAK KAEYPLPILP GNAVRNLHEQ SRENDQAKEH KKASLGDLEE SLPDGAAEKK
RSALVLDKTK GFMKYQRRSE KYRQAKTRTR DWGELNSRLT EDELKYQTAR CMDCGVPFCQ
SDTGCPISNI IPKWNELVFA NRWQDALNRL LMTNNFPEFT GRVCPAPCEG ACVLGINEDP
VGIKSVECAI IDRGFEMGWM VPNPPKFRSG KKVAIVGSGP AGLAAADQLN KVGHEVTVYE
RSDRIGGLLM YGIPNMKLDK NVVQRRVDFM AAEGITFKPS TFIGQEGFPS FSDIRKASDA
VVLATGSTVP RDLKIPNREL GGIHFAMQFL HKNTKSLLDS ELADNAYISA KGKNVIVIGG
GDTGNDCIGT SVRHGAKSVI NFELLPQPPA QRAADNPWPQ WPRIYRVDYG HTEVKTHMGR
DPREYCIMSK DFVGDDEGNV KGVNIKRLEW TKNSNGGWDM KEIEGSEEFF PAELVLISMG
FLSPEERVTE GLIELDGRKN FKTPPGKYTT NVEGVFAAGD CRRGQSLIVW GINEGRQSAR
DVDSYLTGVG TQLPVTGGIV KRPPYELLSK ANGGPSQLIT AAA
//
