ID   A0A238ZVF9_9ACTN        Unreviewed;       486 AA.
AC   A0A238ZVF9;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Glutamate synthase (NADH) small subunit {ECO:0000313|EMBL:SNR87001.1};
GN   ORFNames=SAMN05216252_101573 {ECO:0000313|EMBL:SNR87001.1};
OS   Actinacidiphila glaucinigra.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=235986 {ECO:0000313|EMBL:SNR87001.1, ECO:0000313|Proteomes:UP000198280};
RN   [1] {ECO:0000313|EMBL:SNR87001.1, ECO:0000313|Proteomes:UP000198280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.1858 {ECO:0000313|EMBL:SNR87001.1,
RC   ECO:0000313|Proteomes:UP000198280};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR   EMBL; FZOF01000001; SNR87001.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238ZVF9; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000198280; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198280}.
FT   DOMAIN          41..130
FT                   /note="Dihydroprymidine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF14691"
FT   DOMAIN          146..456
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   486 AA;  52692 MW;  C4F29656E2926D43 CRC64;
     MADPKGFLTT PRETAPTRPV EQRKQDWNEV YVPGGLLPII SKQAGRCMDC GIPFCHNGCP
     LGNLIPEWND YAYREDWKAA SERLHATNNF PEFTGRLCPA PCESACVLGI NQPAVTIKNV
     EVTIIDRAWD SGDVTPQPPD RLSGKTVAVI GSGPAGLAAA QQLTRAGHTV AVYERADRIG
     GLLRYGIPEF KMEKRHINRR IEQMRAEGTK FRTGVEIGRD MDGAKLRKRY DAVVIAAGAT
     AARDLPVEGR ELGGVYQAME YLPLANKVQE GDFVAPPVSA EGKHVVVIGG GDTGADCVGT
     AHRQGARSVT QLEIMPRPSD DRPSHQPWPT MPMTYKVTSA HEEGGERVYA VNTMRFEGDE
     DGNVKALHLV EVEFQDGKFV PQPGTEKVIP AELVTLAMGF TGTDQRNGLV EQLGLELDAR
     GNIARDKDFT TNVDGVFVAG DAGRGQSLIV WAIAEGRSAA RAVDHYLTGA SILPAPIRPT
     DRPLTV
//