ID K0KBS3_SACES Unreviewed; 501 AA.
AC K0KBS3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Glutamate synthase (NADH), small subunit {ECO:0000313|EMBL:CCH34068.1};
DE EC=1.4.1.14 {ECO:0000313|EMBL:CCH34068.1};
GN Name=gltD2 {ECO:0000313|EMBL:CCH34068.1};
GN OrderedLocusNames=BN6_68310 {ECO:0000313|EMBL:CCH34068.1};
OS Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS 15066 / NRRL 15764).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH34068.1, ECO:0000313|Proteomes:UP000006281};
RN [1] {ECO:0000313|EMBL:CCH34068.1, ECO:0000313|Proteomes:UP000006281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC {ECO:0000313|Proteomes:UP000006281};
RX PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT comparison to the other completely sequenced Pseudonocardiaceae.";
RL BMC Genomics 13:465-465(2012).
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR EMBL; HE804045; CCH34068.1; -; Genomic_DNA.
DR RefSeq; WP_015104179.1; NC_019673.1.
DR AlphaFoldDB; K0KBS3; -.
DR STRING; 1179773.BN6_68310; -.
DR KEGG; sesp:BN6_68310; -.
DR PATRIC; fig|1179773.3.peg.6897; -.
DR eggNOG; COG0493; Bacteria.
DR HOGENOM; CLU_000422_3_1_11; -.
DR OrthoDB; 9803192at2; -.
DR BioCyc; SESP1179773:BN6_RS32945-MONOMER; -.
DR Proteomes; UP000006281; Chromosome.
DR GO; GO:0016040; F:glutamate synthase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:RHEA.
DR GO; GO:0051536; F:iron-sulfur cluster binding; 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 ECO:0000313|EMBL:CCH34068.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006281}.
FT DOMAIN 38..141
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 155..470
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 501 AA; 53636 MW; 1660D7DD504A8644 CRC64;
MADPYGFLKH DRADAKKRPA DERLGDWGEV YLDLGADTRD KQVRTQASRC MDCGIPFCHS
GSAGCPLGNL IPEWNDLVRR GDWGQASDRL HATNNFPEFT GRLCPAPCEA ACVLAISHDG
GGAVAIKRVE QAIADVSWEQ GLVQPSQAQV TSGKRVAVVG SGPAGLAAAQ QLTRAGHEVT
VYERDDRLGG LLRYGIPEFK LEKKVLDRRL AQLRKEGTKF VTGCEVGVDL TVAELRSRFD
AVVLAVGALR GRDDTSTPGR RLAGVHLAMD HLVPANRACE GDGPPAVDAA GKHVVIIGGG
DTGADCYGTA TRQGAASVVQ LDQYPQPPSR RDDERSPWPV WPWILRTYPA HEEAGERKFA
VAVEEFVGDE HGHVKQIRLR KVRVEKDASG RRAVVPTSEE VEVLPADLVL LAIGFEGVEH
LPLLGGLGIE LTARGTISCG SDWQTQAPGV FVCGDAHRGA SLVVWAIAEG RSVAHAVDSF
LTGSSDLPSP VIPNQLPLAV V
//
