ID A0A1I6T3A1_9BACI Unreviewed; 491 AA.
AC A0A1I6T3A1;
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:SFS83732.1};
GN ORFNames=SAMN05421668_11237 {ECO:0000313|EMBL:SFS83732.1};
OS Halolactibacillus miurensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halolactibacillus.
OX NCBI_TaxID=306541 {ECO:0000313|EMBL:SFS83732.1, ECO:0000313|Proteomes:UP000199139};
RN [1] {ECO:0000313|EMBL:SFS83732.1, ECO:0000313|Proteomes:UP000199139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17074 {ECO:0000313|EMBL:SFS83732.1,
RC ECO:0000313|Proteomes:UP000199139};
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; FPAI01000012; SFS83732.1; -; Genomic_DNA.
DR RefSeq; WP_062322498.1; NZ_FPAI01000012.1.
DR AlphaFoldDB; A0A1I6T3A1; -.
DR STRING; 306541.SAMN05421668_11237; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000199139; 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; 2.
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}.
FT DOMAIN 24..138
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 153..471
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 491 AA; 54998 MW; 362A78F9868D7C62 CRC64;
MGKPTGFIDY KREVAKERDH LTRLKDWGEY QGRLTDEQLK TEGARCMNCS IPFCHTGIDI
NKQVSGCPLH NLIPEWNDLV YKERFEEALD RLLMTNNFPE FTGRVCPAPC EGACTVSIHD
DAVGIKNIER AIIDRGFDEG YITARIPKER TGKKVAIIGS GPSGLSAADE LNQQGHTVTI
FEKADRAGGL LMYGIPTMKL DKDIVERRIN LLKEEGIIFN LNTDVGKDIL PEDLKRDFDS
VIVCTGAEAP RDLKIQGREL KGIHFAMDYL TKQTKSYLDK KDTSLSAEGK NVVVIGGGDT
GADCVATAIR QGAKNVRQLA ITPAFPQTRA KGNEWPSYPN VFREDYAHKE AKMIFNREVR
EFLTETHAFI DDGEGHVQAL FTRKIEEIST TEGVRYEKVD RGDDVIPADL VILAIGFVGP
QQSLLDRFGV EMKNNRIDAD YQDFRTNVKN VFAAGDARRG PSLIVWAIQE GREVAKVVHD
YLINQKVKQY A
//