ID W7MH49_GIBM7 Unreviewed; 2113 AA.
AC W7MH49;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN ORFNames=FVEG_09511 {ECO:0000313|EMBL:EWG50221.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG50221.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG50221.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7600 {ECO:0000313|EMBL:EWG50221.1}, and M3125 / FGSC 7600
RC {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [2] {ECO:0000313|EMBL:EWG50221.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=7600 {ECO:0000313|EMBL:EWG50221.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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; DS022254; EWG50221.1; -; Genomic_DNA.
DR EMBL; DS022254; EWG50222.1; -; Genomic_DNA.
DR RefSeq; XP_018756412.1; XM_018898510.1.
DR RefSeq; XP_018756413.1; XM_018898511.1.
DR STRING; 334819.W7MH49; -.
DR EnsemblFungi; FVEG_09511T0; FVEG_09511T0; FVEG_09511.
DR GeneID; 30067159; -.
DR KEGG; fvr:FVEG_09511; -.
DR VEuPathDB; FungiDB:FVEG_09511; -.
DR eggNOG; KOG0399; Eukaryota.
DR HOGENOM; CLU_000422_8_0_1; -.
DR OMA; WDGPAAM; -.
DR OrthoDB; 20503at2759; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000009096; 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:UP000009096}.
FT DOMAIN 54..463
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 961..982
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 1184
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1190
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1195
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
SQ SEQUENCE 2113 AA; 233641 MW; CD12E8F06782E224 CRC64;
MGLNEEFDDR HIQTEAEQQP YIPYEYQTEN NDSWAGALPV KQGLYDPSYE KDACGVGFAC
HIKGKPSHKI VSDARNLLCN MTHRGAVGSD ARDGDGAGVM TSIPHRFFIK NFEKEEDIKL
PPLGQYAVGN LFFKPDEETL QESKRQLEDV AESLGLRVLG WRRPPVDSTL LGPAAKSREP
IIAQPFVVLA SAYGTGNAPE MTDPEKFDER LFERQLYILR KRATQSIGLH NWFYLCSLSN
KNIVYKGQLA PVQVYSYYHD LVNADYEAHF ALVHSRFSTN TFPSWDRAQP LRWAAHNGEI
NTLRGNKNWM RAREGVMQSD IFKEELEQMY PVVEDGGSDS AAFDNVLELL TINGVLSLPE
AVMLMVPEAW QGNQHMDPKK AAFYEWAACQ MEPWDGPALF TFADGRYCGA NLDRNGLRPC
RFYVMDDDRI ICASEVGTIP VEPETVIQKG RLQPGRMLLV DTQAGRIIDD KELKEAVSSR
YDFRAWLDSE LITLPKVVEI MEQALDLAPK LDDKAIQADP LLLSYGYTHE QVSLLLAPMA
ADEKEALGSM GNDAPLACLT QAPRLLYDYF RQLFAQVTNP PIDPIRESIV MSLECYVGPQ
GNLLEMDASQ CGRLLLPSPI LSIEEFNAVK NMSNKYSEWT VKTIDLTFPK NQGIQGYIKH
LDEICNEASA AIESRDRVIV LSDRNTSADR VPVSAVLASA MVHHHLVSNK WRSMVALVVE
TAEAREVHHM CVLLGYGADA INPYLAMECI LKLNREGLIK KKTTNETLIR NYKHSCDGGI
LKVMSKMGIS TLASYKGAQI FEILGLDETV VERCFRGTAS RIQGMTFELI AEEAFRFHER
GFPTRETILP SGLPESGEYH WRDGGEPHVN DPTSIANIQD AVRTKNDKSY EAYSRSEYEQ
IKNCTLRGLL DFKFEDCTPV PIDQVEPWTD IVRRFCTGAM SYGSISMESH STLAVAMNRL
GGKSNTGEGG EDPERSQRMP NGDTMRSAIK QVASGRFGVT SAYLADSDEL QIKMAQGAKP
GEGGELPGHK VSKSIARTRH STPGVGLISP PPHHDIYSIE DLKQLIYDLK CSSPRSRVSV
KLVSEVGVGI VASGVAKAKA DHILISGHDG GTGASRWTGI KYAGLPWELG LAETHQTLVL
NDLRGRVVVQ TDGQLKTGRD VALACLLGAE EWGFATAPLI AMGCVFMRKC HLNTCPVGIA
TQDPELRKKF TGTPEHVINF FYYVANELRA IMAQLGFRTI NEMVGHVEVL KMRDDLRTNK
TANIDLSLLL TPAHKLRPGV ATFNVRKQDH KLHVRLDNKL ISESELTLDK GLPSRIECDI
VNTDRAMGTS LSYHISKRYG EAGLPMDTVH VNIKGSAGQS FGAFLAPGVT LELEGDANDY
VGKGLSGGRL IIYPPRSAVF KSEENILIGN TCLYGATTGT CFFRGVAAER FAVRNSGATA
VVEGVGDHGC EYMTGGRVVV LGSTGRNFAA GMSGGIAYIL DVHGDFHSKL NGEMVEASGL
EDPAEIAFVR GLIEDHHHYT GSERAARILV DFNRALPRFI KILPVDYKRV LEEEAAKAAE
AKRAEYNLPA VSGVQHKKSE KVAKLQDLEE AVGDNAAEKK RALVLDKTRG FKMYKRRQEK
YRPVNSRLKD WAELSSRLDE DELKYQSARC MDCGVPFCQS ETGCPISNII PKWNELVFQN
QWKDALNRLL MTNNFPEFTG RVCPAPCEGA CVLGINEDPV GIKSIECAII DRGFEMGWMV
PQPPKVRTGK TVAIIGSGPA GLAAADQLNR AGHLVTVYER ADRLGGLLMY GIPNMKLDKR
IVKRRTDFMA SEGIIFKTGV AVGEEGHPSL NDLRASNSAV VIATGATVAR DLPIKGRQLD
GIHYAMEFLH KNTKSLLDSE LADNTYISAK GKDVVVIGGG DTGNDCIGTS LRHGAKSVTN
FELLPQPPPE RANDNPWPQW PRIYRVDYGH TEVRQHTGKD PREYCIMSEE FMDDGSGKVK
GINTIRVEWT KSPSGGWDMK KVEGSQQFFP ADLVLLAMGF LGPEARVLGD EIEKDARKNV
KTAPGKYSTN LEGVFAAGDA RRGQSLIVWG INEGRQAARE IDLYLEKYTN LPVTGGITKR
TAQEIFSQIK VEA
//
