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Database: UniProt
Entry: A0A1I1YLK6_9FIRM
LinkDB: A0A1I1YLK6_9FIRM
Original site: A0A1I1YLK6_9FIRM 
ID   A0A1I1YLK6_9FIRM        Unreviewed;       463 AA.
AC   A0A1I1YLK6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=glutamate synthase (NADPH) {ECO:0000256|ARBA:ARBA00012079};
DE            EC=1.4.1.13 {ECO:0000256|ARBA:ARBA00012079};
GN   ORFNames=SAMN05216245_102207 {ECO:0000313|EMBL:SFE18880.1};
OS   Succiniclasticum ruminis DSM 9236.
OC   Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC   Succiniclasticum.
OX   NCBI_TaxID=1123323 {ECO:0000313|EMBL:SFE18880.1, ECO:0000313|Proteomes:UP000198896};
RN   [1] {ECO:0000313|EMBL:SFE18880.1, ECO:0000313|Proteomes:UP000198896}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9236 {ECO:0000313|EMBL:SFE18880.1,
RC   ECO:0000313|Proteomes:UP000198896};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + L-glutamine
CC         + NADPH; Xref=Rhea:RHEA:15501, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:58359; EC=1.4.1.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001895};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC       pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+)
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00037898}.
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DR   EMBL; FONL01000002; SFE18880.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1YLK6; -.
DR   STRING; 1123323.SAMN05216245_102207; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000198896; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR006004; SudA-like.
DR   NCBIfam; TIGR01316; gltA; 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; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198896}.
FT   DOMAIN          30..62
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   463 AA;  49966 MW;  5D949E4CB7AF64BD CRC64;
     MLKVNRHAMP EQPAEIRRRN FEEVALGYDE ATAIEEAKRC LNCPKPRCVE GCPVNIYIPK
     FVHAVSEGDF ASAIKIIKEK SSLPAVCGRV CPQEKQCESR CVLGIKGEPV AIGRLERFVA
     DYAREHGLDK VDPSEVAAKN GKKVAIVGSG PSGLACAGVL AQKGYDVTIF EVLHAAGGVL
     MYGIPQFRLP KEIVQHEIEG LKQMGVHVQT NAIIGRTFTI DELMKEEGFD AVYIATGAGL
     PHFMHIPGEQ FNGVYAANEF LTRVNLMKAY TFPRAATPVF IGKKVAVVGG GNVAMDAART
     AMRLGAEHVY IVYRRGEDEL PARKEEVGHA KEEGIEFCLL NNPVRIVGNE QGWVTGLECV
     KMELGEPDAS GRRSPVAIKD SNYVLEVDEV IMAIGQGPNP LIHQTTPDLE VNRRGNIVAD
     ENGATSMPGV YAGGDIVTGA ATVISAMGAG KRAAAAIDEY LMK
//
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