ID W6YKM3_COCMI Unreviewed; 2143 AA.
AC W6YKM3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN ORFNames=COCMIDRAFT_10233 {ECO:0000313|EMBL:EUC39732.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC39732.1};
RN [1] {ECO:0000313|EMBL:EUC39732.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC39732.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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; KI964265; EUC39732.1; -; Genomic_DNA.
DR RefSeq; XP_007693748.1; XM_007695558.1.
DR STRING; 930090.W6YKM3; -.
DR GeneID; 19118059; -.
DR KEGG; bor:COCMIDRAFT_10233; -.
DR eggNOG; KOG0399; Eukaryota.
DR HOGENOM; CLU_000422_8_2_1; -.
DR OrthoDB; 20503at2759; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000054032; 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}.
FT DOMAIN 57..466
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT ACT_SITE 57
FT /note="For GATase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-1"
FT BINDING 1188
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1194
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1199
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
SQ SEQUENCE 2143 AA; 236781 MW; 7DABDBBFBA56EB70 CRC64;
MGRVSFAEDT KLPQETQIEE EQTSVFAYQD GPENKSWAGA LPLKQGLYDP ELEKDACGVG
FAAHIKGKAS HKIVSDARSL LCNMTHRGAV GSDARDGDGA GVMTSIPHRF FLKEFEREQG
YKLPKLGQYA TGNLFFKPDP SILDETKTMF EDVADQLDLR VLGWRTVPRD STLLGPAALS
REPIILQPFV VLKTAYGDGR EPKADFQQKY DNAYFERQLY VMRKRATHVI GLHNWFYICS
LSNKNIVYKG QLSPVQVYEY YHDLLNVDYE GHFALVHSRF STNTFPSWDR AQPLRWAAHN
GEINTLRGNK NWMRAREGVM KSSLFGEELD LLYPIVEDGG SDSAAFDNVL ELLTINGVLS
LPEAVMLMVP EAWQGNNTMD PAKAAFYEWA ACMMEPWDGP ALFTFSDGRY CGANLDRNGL
RPCRYYITDD DRIVCASEVG TISIEPERVV QKGRLQPGRM LLVDTVAGRI VDDAELKKSV
AERNDFRRWI EKNLLTLPKI VQSVGEKGID LSHSLTETKL HEDPRLRAFG YSLEQVSLLL
GPMAADSKEA LGSMGNDAPL ACLATQPRLL YEYFRQLFAQ VTNPPIDPIR EAIVMSLEAY
VGPQGNLLEM DESQCGRLLL PSPILTLEEF KAMTNAHTLY REWTVKSIDI TFPKSEGIEG
YMNALDRICE AATEGIQAGD NILVLTDRAT SVDRVAVSAC LATGMVHHHL VRNKWRSSAA
LVVETGEARE VHHMCVLVGY GADAVCPYLA IECILKMHRE GIIRKNLTPE QLIQNYKHSC
DGGILKVMSK MGISTLQSYK GAQIFEALGL DDSVVDRCFT GTASRIKGMT FELIAADAFA
LHEKGYPSRP IVEVPGLSET GEYHWRDGGE PHVNDPTAMA NLQDAVRTKN DKSYEAYSIA
EYERIKDCTL RGLLDFNFDD RAPIPIDQVE PWTDIVRRFV TGAMSYGSIS MESHSTLAVA
MNRLGGKSNT GEGGEDPERS LRMENGDTMR SAIKQIASGR FGVTSNYLAD ADELQIKMAQ
GAKPGEGGEL PGHKVSGSIA KTRHSTPGVG LISPPPHHDI YSIEDLKQLI YDLKCSNPRA
RVSVKLVSET GVGIVASGVA KAKADHILIS GHDGGTGASR WTGIKYAGLP WELGLAETHQ
TLVLNDLRGR VIVQTDGQIK TGRDVAIACL LGAEEWGFAT TPLIAMGCIF MRKCHLNTCP
VGIATQDPEL RKKFAGTPEH VINFFYYVAN ELRAIMAKLG FRTINDMVGR CEFLRIRDDL
RTAKTENIDL SLILTPAHTL RPGVATFNVR KQDHRLHVRL DNKLIAESEL ALEKGLPARI
ECDVVNTDRA LGATLSYHIS KRYGEAGLPS DTIHVNIRGS AGQSFGAYLA PGVTLELEGD
ANDYVGKGLS GGRLIIYPPR NAVYRAEENV LIGNVCLYGA TQGTCFFRGI AAERFCVRNS
GATAVVEGVG DHGCEYMTGG RVLVLGSTGR NFAAGMSGGI AYVLDIHKDF EQKVNQEMVE
LSPIEEPEEI AFVRGLIEDH HHYTGSELAA RILLDFTRAL SRFVKVMPID YKRVLLEEKA
RLAEEKRNKY PLPLLAGNAV RNAHEESRTK EAEAEAKEKK KSSGLLDIEE SVTDAKAEKK
KALVLDKTRG FMKYQRRSEK YRNPKTRTRD WAELSQRLNE DELKYQTARC MDCGVPFCQS
DTGCPISNII PKWNELVFRS QWRDALNRLL MTNNFPEFTG RVCPAPCEGA CVLGINEDPV
GIKSIECAII DRGFEKGWMV PTPPQVRSGK TVAIIGSGPA GMACADQLNK AGHLVTVFER
ADRVGGLLMY GIPNMKLDKK VVQRRVDFMA AEGVNFKTGV TVGEEGHPNL ERLRKDFDAV
VFATGATVAR DLPIPNRNLE GIHFAMQFLH KNTKSLLDSE LADNAYISAK DKHVVVIGGG
DTGNDCIGTS VRHGAKSVVN FELLPQPPPE RARDNPWPQW PRIFRTDYGH NEVKTHMGKD
PREYCVMSKE FVDDGNGKVK GINTIRVAWT KSSSGGWDMK QVDGSEQFFP ADLVLLSMGF
LGPEQRVMSD IVELDGRKNI KTPPGHYNTN LPGVFAAGDC RRGQSLIVWG INEGRQCARD
VDSFLNGYGS SLPVTGGIVQ RPPYEAVLKA GHGHAEKLAA VAA
//
