ID A0A0C7N405_9SACH Unreviewed; 2150 AA.
AC A0A0C7N405;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 36.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN ORFNames=LALA0_S01e05556g {ECO:0000313|EMBL:CEP60211.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP60211.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP60211.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP60211.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LN736360; CEP60211.1; -; Genomic_DNA.
DR STRING; 1245769.A0A0C7N405; -.
DR HOGENOM; CLU_000422_8_2_1; -.
DR OrthoDB; 20503at2759; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000054304; 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; 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:UP000054304}.
FT DOMAIN 57..464
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 1194
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1200
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
FT BINDING 1205
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|PIRSR:PIRSR000187-2"
SQ SEQUENCE 2150 AA; 236897 MW; 316CCE9EB9E9EEA2 CRC64;
MLQSDKFDVL EEAYDGGLPL SDDLSGFGSS STKTQFWADS IPQKQGLYDP EYERDACGVG
FVANIKGTPS HKIVSDARYL LCNMTHRGAV SSGGNGDGAG ILVGIPHEFM RREFKLELDI
DVPARHQYAV GNFFFKKDSS DSLEVGKRVF EEIATSLGLT VLGWRSVPRD SSLLGAVALS
REPAILQPLV VLTAAYQEQG QISDEEFKSK YDVEFQTLLY GLRKKSTSAI GIQNWFYACS
LNTKTIVYKG QLTPTQVYQY YHDLTNAHFE SHMALVHSRF STNTFPSWDR AQPLRWIAHN
GEINTLRGNK NSMRSREGVM SSDTFKENLE QLYPIIEEGG SDSAALDNVL ELLVINGALS
LPEAIMMMVP EAYHKDMDSN LKAWFDWAAC LMEPWDGPAL LNFTDGRYCG AMLDRNGLRP
CRYYITSDDR VICASEVGVI QVDNSLIVQK GKLKPGDMLL VDTELGQMVD TKKMKSQFAK
KQDFKSWLSK LIKVEDLLVK TEKFTPKTFL SEEHASLKAQ QDPRLLALGY TFEQVSMVLV
PMALGSKEAL GSMGNDAPLA CLNEDPVLLY DYFRQLFAQV TNPPIDPIRE ANVMSLECYV
GPQGNLLEVH PSQCDRLLLK SPILHWKEYE AIKNIEKAHP AWSTANIDIT FEKSQGLLGY
TAALDRITQD ASDAIDQGKR ILMLSDRKLG AHRVPLSSLI AVGAIHHHLI RNKQRSQVAL
ILETGEAREV HHFCVLLGYG CDAIFPYLAM ETLVRMNQEG LVRNVDNEDL VIDDSTLLEN
YKHAVDGGIL KVMSKMGIST LASYKGAQIF ESLGIDNTVV DLCFAGTASR IQGVTFEYIA
QDAFSMHERG FPSRKTISKS VNLPESGEYH WRDGGAKHIN DPTAIASLQD SVRNKNEDAW
EMYVKKEMES IRDCTLRGLL ELNFEDATPI PLEQVEPWTE IARRFATGAM SYGSISMEAH
STLAVAMNRL GAKSNCGEGG EDSERSIVHA NGDTMRSAIK QVASARFGVT SHYLSDADEI
QIKIAQGAKP GEGGELPAHK VSADIAKTRH STPYVGLISP PPHHDIYSIE DLKQLIYDLK
CSNPRAGISV KLVSEVGVGI VASGVAKAKA DHILVSGHDG GTGASRWTGI KYAGLPWELG
LAETHQTLVL NDLRRNVVVQ TDGQLRTGFD IAVAVLLGAE SFTLATVPLI AMGCIMLRKC
HLNACAVGIA TQDPLLREKF KGQPEHVINF FYYLIQDLRK IMAKLGFRTI DEMVGHSEKL
KKRDNVNTKA INIDLSPILT PAHVIRPGVA TKFTKKQDHK LHTRLDNKLI DEAEVTLDRG
LPINIDASII NTDRALGATL SYRISKKFGE EGLPQDTVVV NIEGSAGQSF GAFLASGVTF
ILDGDANDYV GKGLSGGRLV IRPPSGSSFK SDENVIVGNT CFYGATSGTA FISGVAGERF
CVRNSGATIV VERIKGNNAF EYMTGGRAVV LSQMESLNAF SGATGGIAYC LTSDYDDFAG
KINMETIELQ SLVDTVEIAF VKNLIQEHYN YTKSELAARI LGNFNHYLKN FVKVIPTDYR
KVLEKAAAEK VKQKEANTAK FLKRFNSGTD LKADATNGEV DGIRDSRIKA ATVSHKATLT
EPKVQDLEDA IQNADQLEKN VEKIEKTRGF MLYKIRHEKY RGTKSRTKDW KELSSCLTKK
DAKYQTARCM DCGVPFCTAD TGCPISNVIP KFNELVFKNQ WKLALDKLLE TNNFPEFTGR
VCPAPCQGSC TLGIIDDPVG IKSIERLIID NGFKEGWITP QIPEFRTGRN VAVIGSGPAG
LACADQLNRA GHSVTVFERA DRCGGLLMYG IPNMKLDKSI VQRRIDLMAA EGVSFINNVE
IGKDVTTEDL KSAHDAVVYA IGSTIPRDLK IPGRSLKNID FAMSLLTANT KALLEKDLEI
IRQQIAGKKV IVIGGGDTGN DCLGTSVRHG AASVLNFELL PQPPNERSKD NPWPQWPRVM
RVDYGHAEVK EHYGRDPREY CILSKEFIGN EDGEVKAIKT VRVEWKKSES GVWQMVEVPG
SEEVFEADIV LLSMGFMGPE LFEDPDIVKT KRGTIGTLND ASYSVDGGKI FTAGDCRRGQ
SLIVWAIQEG RKCATSVDSF LMGSTNLPGN GGIVKRDYRL LEELASTVDA
//
