ID   A0A1I2DTH5_9BACI        Unreviewed;       490 AA.
AC   A0A1I2DTH5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Glutamate synthase (NADPH/NADH) small chain {ECO:0000313|EMBL:SFE83521.1};
GN   ORFNames=SAMN05192532_104282 {ECO:0000313|EMBL:SFE83521.1};
OS   Alteribacillus iranensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacillus.
OX   NCBI_TaxID=930128 {ECO:0000313|EMBL:SFE83521.1, ECO:0000313|Proteomes:UP000199516};
RN   [1] {ECO:0000313|EMBL:SFE83521.1, ECO:0000313|Proteomes:UP000199516}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23995 {ECO:0000313|EMBL:SFE83521.1,
RC   ECO:0000313|Proteomes:UP000199516};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR   EMBL; FONT01000004; SFE83521.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2DTH5; -.
DR   STRING; 930128.SAMN05192532_104282; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000199516; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster 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:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
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; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 2.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199516}.
FT   DOMAIN          25..140
FT                   /note="Dihydroprymidine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF14691"
FT   DOMAIN          154..476
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   490 AA;  54619 MW;  6E520AE304F26C8F CRC64;
     MGKATGFMEY DRQSATYRDP SERLNDWREI SVLPPEEKIT QQAARCMDCG VPFCQNGSEL
     AGMATGCPVY NLIPEWNELV YQGKWKEAYE RLSKTNPFPE FTGRACPAPC EGGCVASLYE
     SSVTIKNIEW AIIDKAFEEG WVTPPKPKKR TGKKAAIIGS GPAGLACASE LNKQGHTVTV
     FERSDRLGGL LTYGIPKMKI EQHVVDRRVN LLKEAGIHFK TNVEVGKEYP VEKLKTEFDA
     VIVCTGATKA RNIELDGRHF KGIHFAMDYL HSNTKSMLDS NFRDENYISA EGKDVIVIGG
     GDTATDCVST ALRHQCKSLV QFDIYPKRPE DRTQANPWPQ FPVIHKLDYG QEEAKSKFGS
     DPRSYATSTI EFLGDDTGYI SGVRSVEVKT IFNEKGEKKR EPILGSDKVW PAQLVFLAVG
     FEGPEQHLLE QMNIRVTERS NVDVQEGSYQ TSQDGVFAAG DARRGQSLIV WAIQEGKEAA
     EACHDYMMNN
//