ID A0A0N0U2S3_9HYME Unreviewed; 1619 AA.
AC A0A0N0U2S3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN ORFNames=WN51_08078 {ECO:0000313|EMBL:KOX67708.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX67708.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX67708.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX67708.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX67708.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) 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|ARBA:ARBA00001927};
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; KQ435989; KOX67708.1; -; Genomic_DNA.
DR STRING; 166423.A0A0N0U2S3; -.
DR OrthoDB; 20503at2759; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000053105; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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; 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; 3.40.50.720; 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; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR InterPro; IPR006982; Glu_synth_centr_N.
DR InterPro; IPR002932; Glu_synthdom.
DR InterPro; IPR006005; Glut_synth_ssu1.
DR InterPro; IPR009051; Helical_ferredxn.
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; PF04898; Glu_syn_central; 1.
DR Pfam; PF01645; Glu_synthase; 1.
DR Pfam; PF01493; GXGXG; 1.
DR Pfam; PF07992; Pyr_redox_2; 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; SSF51971; Nucleotide-binding domain; 1.
PE 3: Inferred from homology;
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291};
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053105}.
FT DOMAIN 52..335
FT /note="Glutamate synthase central-N"
FT /evidence="ECO:0000259|Pfam:PF04898"
FT DOMAIN 398..766
FT /note="Glutamate synthase"
FT /evidence="ECO:0000259|Pfam:PF01645"
FT DOMAIN 849..1035
FT /note="Glutamate synthase alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01493"
FT DOMAIN 1161..1255
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 1269..1590
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 1619 AA; 178225 MW; 6F5CE2C50BF000F3 CRC64;
MEELRAADVE YKKTSSAVEN GSIVDNVIAK KNVMNDANPI SAVNRVWGGD KRLSLYGYTL
ETINLLLLPM MQSKKESLGS MGNDAPLACL SQFQPLIYEY FKQLFAQVTN PPIDPFREKI
VMSMLCPIGP ESNILEPNEL QVHRLFLSQP ILSLEDLEII KRTNYRGWKT KIIDATYPVQ
DGPSGLVNTL NRVSEEANQA AKQGYQFLVL SDRQGGPERV PVSSLLVLGA VHHYLIEERQ
RMKVGLIIET AEAREVHHIC LLLGYGADAI CPYLVFEMAR NLRMDGVLDS SLTDNALCAN
YAEAMERGIA KVMAKMGIST LQSYKGAQIF EAVGLCDEVI DKCFKGTHSR IGGVTFDILA
KEAFERHQIT YWKKPMDMLV IRNPGMYHWR SGGEKHINDP DSIANLQDYV NSKNWNAYEK
YRKSTMEMVR ACTLRGQLEL VERAEKSIPI EEVEPASEIV KRFATGAMSF GSISIEAHTT
LAIAMNRISG KSNTGEGGEN ADRYLNQDPE FNKRSAIKQV ASGRFGVTSS YLANADDLQI
KMSQGAKPGE GGELPGYKVT AEIAATRHSV PGVGLISPPP HHDIYSIEDL AELIYDLKCA
NPNARISVKL VSEVGVGVVA SGVAKGKAEH IVISGHDGGT GASTWTGIKS AGLPWELGIA
ETHQILTLNN LRSRVIVQAD GQMRTGFDVV VAALLGADEF GFSTAPLISM GCTMMRKCHL
NTCPVGIATQ DPTLRKKFEG KPEHVINFFF ALAEEVRSYM ASLGLNKFQD LIGRTDLLKV
RENISIEKAK TLKLDNILRN ALELRPGVNI QGGSMKQDFQ LENRLDNRVI ELAMGVLKGK
QNRVDIELNI NNECRAFAAT LSYHISKLYG EDGLSEGSIN IKMKGSAGQS FCAFMTKGVH
VTLEGDANDY VGKGLCGGEI IIYPPKDSTF KSDTNVIVGN VCLYGATSGK AYFRGIAAER
FSVRNSGAIV VVEGVGDHGC EYMTGGCAVV LGLTGRNFAA GMSGGIAYVL DVDGSFKSKC
NPEMVELLPL NKQEDIAYVK KLLEEFVEKT GSLVAQDLLT LWPEPTTRFV KVFPYEYQRA
LKQVEETKQA ETIVNGSSQT VNAQVKDIED TIADIEIEQH KLDKIRGFMK YRRQTEAYRP
VENRIDDWDE IYNFQRVRKG LRVQAARCME CGVPFCQSSH GCPLGNIIPK WNDLVFQSNW
KEALNQLLQT NNFPEFTGRV CPAPCEGACV LGISEPAVTI KNIECAIIDH AFEQGWIVPH
PPTTRTGRRI AVVGSGPAGL AAAHQLNKAG HLVTVYERND RIGGLLQYGI PTMKLSKQVV
QRRVSLLAAE GITFKTGIDV GKDISAKELQ EEYDATLICT GATWPRDLQI PGRHLEGIHF
AVSFLEHWQK KQMGNDAPLD MRLMAKDRDV IIIGGGDTGC DCIATSLRQG AKTITTFEIL
PEPPSNRAHD NPWPQFPRVF KVDYGHEEVS LKFGRDPRQF STLSKEFLDD GNSHVSGIKT
VSVSWTMENG RWKMEEIPGT EKTYKCDLVL LAMGFLGPEK YVATELNTTM DERGNFKTPV
GKYETSLNGV YAAGDCRRGQ SLVVWAITEG RQAAREIDLA LMGETGLPVA GGVVTGVVG
//