ID A0AA38IIJ4_9CUCU Unreviewed; 1965 AA.
AC A0AA38IIJ4;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=Glutamate synthase [NADH] {ECO:0000256|ARBA:ARBA00068518};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN ORFNames=Zmor_013887 {ECO:0000313|EMBL:KAJ3654716.1};
OS Zophobas morio.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Zophobas.
OX NCBI_TaxID=2755281 {ECO:0000313|EMBL:KAJ3654716.1, ECO:0000313|Proteomes:UP001168821};
RN [1] {ECO:0000313|EMBL:KAJ3654716.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=QUZm001 {ECO:0000313|EMBL:KAJ3654716.1};
RX PubMed=37002914; DOI=10.1093/g3journal/jkad079;
RA Kaur S., Stinson S.A., diCenzo G.C.;
RT "Whole genome assemblies of Zophobas morio and Tenebrio molitor.";
RL G3 (Bethesda) 13:jkad079-jkad079(2023).
CC -!- FUNCTION: Forms L-glutamate from L-glutamine and 2-oxoglutarate.
CC Represents an alternative pathway to L-glutamate dehydrogenase for the
CC biosynthesis of L-glutamate. Participates with glutamine synthetase in
CC ammonia assimilation processes. The enzyme is specific for NADH, L-
CC glutamine and 2-oxoglutarate. {ECO:0000256|ARBA:ARBA00057049}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + NAD(+) = L-glutamine + 2-oxoglutarate + NADH +
CC H(+); 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:ARBA00048867};
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 -!- SUBUNIT: Homotrimer. {ECO:0000256|ARBA:ARBA00011233}.
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:KAJ3654716.1}.
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DR EMBL; JALNTZ010000004; KAJ3654716.1; -; Genomic_DNA.
DR Proteomes; UP001168821; 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:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0019676; P:ammonia assimilation cycle; IEA:UniProtKB-ARBA.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd00713; GltS; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR FunFam; 1.10.1060.10:FF:000006; Glutamate synthase (NADPH/NADH); 1.
DR FunFam; 3.20.20.70:FF:000031; Glutamate synthase 1 [NADH]; 1.
DR FunFam; 3.20.20.70:FF:000017; Glutamate synthase [NADH], amyloplastic; 1.
DR FunFam; 3.40.50.720:FF:000113; Glutamate synthase [NADH], amyloplastic; 1.
DR FunFam; 3.50.50.60:FF:000022; Glutamate synthase [NADH], amyloplastic; 1.
DR FunFam; 2.160.20.60:FF:000001; Glutamate synthase, large subunit; 1.
DR FunFam; 3.60.20.10:FF:000001; Glutamate synthase, large subunit; 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; IPR051394; Glutamate_Synthase.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR NCBIfam; TIGR01317; GOGAT_sm_gam; 1.
DR NCBIfam; NF008730; PRK11750.1; 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; 1.
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:UP001168821}.
FT DOMAIN 1..348
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT BINDING 1058
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1064
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1069
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
SQ SEQUENCE 1965 AA; 217696 MW; 3C4A66CDB51DDA81 CRC64;
MPLNMRLLAP TMGDEQNIEL PPFGKYATGI FYLDKLHHQE FEAKFASLAE ELDMSVLAWR
TVPTDNSSIG TVAKNTEPFM RQVFVGVKGD APEDELDRRF FILRKRASHT IPSSGKRFYI
CSLSRRTIVY KGQLTSDQLW TYFPDLADPL YDTYLALVHT RFSTNTFPSW ERAHPLRMLA
HNGEINTLRG NVNLMKAREG VMYNEEYGEK LKDLYPVVEP NLSDSGSADC VLEFLVHAGN
RKLPEAVMTM VPEAWHNDPT MSEEKRDYYH WAACIMEPWD GPALISFTDG RFIGAILDRN
GLRPSRFYIT KDNMMIMASE VGVYDVDPSQ VIFKSRLKPG RMLLVDTQEK SVIQDVELKQ
QIARSRPHSE WLKEQITMDE LRQTHLEANR SSKPKYEPSG LGDKRLSLYG YSTETIHMLL
LPMVNNKKEA LGSMGNDVPL ACLSNFAPLL YDYFKQLFAQ VTNPPIDPFR EKVVMSLQCP
IGPEANILRP DPKQVHRLWL KQPVISIVDL EVLKQTTHRN WSAHIIDITF PVESGPVGFL
KKLQSVCEEA HQASKDNQII VLSDRKAGSE RVPISSLLAL GAVHHHLIEM RARMKVALVV
ETAEAREVHH VCVLLGYGAD AICPYLALEL ASSLRDQGVL DTSLTDEVIF QNYAQAMQTG
INKVMAKMGI STLQSYKGAQ IFEAVGLAED VIDKCFRGTH SRIGGVTLET LAQEAFQRHG
NTYCIATDSL ILRDTGNFHW RAGGEKHLNE PASIAALQES AINKNQSAYE KFRESTMESV
RNCMLRGRFD LRTLDEPLPL DEIEPASEIV KRFATGAMSF GSISLEAHQT LAIAMNKVGG
KSNTGEGGED PERYLDPQKR SSIKQVASGR FGVTSSYLAH ADDLQIKMAQ GAKPGEGGEL
PGYKVSAEIA KTRHSVAGVG LISPPPHHDI YSIEDLAELI YDLKCANPRA RISVKLVSEV
GVGVVASGVA KGKAEHIVVS GHDGGTGASS WTGIKNAGLP WELGIAETHQ VLVLNNLRSR
IVLQADGQIR TGFDVVIAAL LGADEIGFST APLIVMGCTM MRKCHLNTCP VGIATQDPIL
RKKFTGQPEH VINYMFMLAE EVRQLMAKLG VRTYQELVGR TDLLKVSEEG SAKAKMLNLN
LILTNALHMR PGVNIKGGSQ VQDFQLENRM DNILIEKAKG VLDGTEKTVD IEMKINNECR
AVTSTLSYHI SCKYDEQGLP DDQHINIRLN GSAGQSFCAF LVNGITVTLE GDANDYVGKG
LSGGTIIIYP PKTSPFESHL NVIVGNVCLY GATSGRAYMR GIASERFAVR NSGAVAVVEG
VGDHGCEYMT GGIVLILGLT GRNFAAGMSG GIAYVWDVDG KFSTKCNPEL VELCKLEDKE
DVDLVKTLLH EFKDLTESVI AEQLINEFDE RRKEFVKVFP YEYQRVLKQK ATEQMVNNVQ
QNHEPKIQDI EDAVTDVAME QKKLDKVRGF MKYPRETGMY RPAEKRMKDW DEIYNFGHVR
KGLRVQAARC MDCGVPFCQS NSHGCPLGNI IPKWNFLVFQ NQWRQALNHL LQTNNFPEFT
GRVCPAPCEG ACVLGISEPS VTIKNIECAI IDHAFENGWI TPQIPQFRTG KQVAVVGSGP
SGLACAHQLN KAGHTVTVFE RNDRVGGLLQ YGIPTMKLSK NVVQRRVDLL AAEGITFKTN
VNVGKDISAK ELSEEYDAVV LCTGATWPRD LPLPGRQLGG IHFAMEFLES WQKKQLGANH
SGPHAKDKNV IIIGGGDTGC DCIATSLRHG AASITTFEIL PEPSPKRTAD NPWPQWPRIF
RVDYGHDEVK VRFGGDPRVF SILTQEFLDN GQGHVSGVKT VNVEWTKDES GRWQMNQVPG
TERVFPADLV LLAMGFLGPE RAIADQLELT LDARSNFNTK EYKTNLPNVF AAGDCRRGQS
LVVWAISEGR QAARRVDEFL NQGQTVLPGP GGIIQPSTNP VACPV
//
