ID I0L8P0_9ACTN Unreviewed; 511 AA.
AC I0L8P0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Glutamate synthase, small subunit,nucleotide-binding, 4Fe-4S protein, GOGAT {ECO:0000313|EMBL:CCH20187.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:CCH20187.1};
DE EC=1.4.1.14 {ECO:0000313|EMBL:CCH20187.1};
GN Name=gltD {ECO:0000313|EMBL:CCH20187.1};
GN ORFNames=MILUP08_45067 {ECO:0000313|EMBL:CCH20187.1};
OS Micromonospora lupini str. Lupac 08.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1150864 {ECO:0000313|EMBL:CCH20187.1, ECO:0000313|Proteomes:UP000003448};
RN [1] {ECO:0000313|Proteomes:UP000003448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lupac 08 {ECO:0000313|Proteomes:UP000003448};
RX PubMed=22815450; DOI=10.1128/jb.00628-12;
RA Alonso-Vega P., Normand P., Bacigalupe R., Pujic P., Lajus A., Vallenet D.,
RA Carro L., Coll P., Trujillo M.E.;
RT "Genome Sequence of Micromonospora lupini Lupac 08, Isolated from Root
RT Nodules of Lupinus angustifolius.";
RL J. Bacteriol. 194:4135-4135(2012).
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCH20187.1}.
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DR EMBL; CAIE01000037; CCH20187.1; -; Genomic_DNA.
DR RefSeq; WP_007462906.1; NZ_HF570108.1.
DR AlphaFoldDB; I0L8P0; -.
DR STRING; 1150864.MILUP08_45067; -.
DR eggNOG; COG0493; Bacteria.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000003448; Unassembled WGS sequence.
DR GO; GO:0016040; F:glutamate synthase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
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; 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 ECO:0000313|EMBL:CCH20187.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003448}.
FT DOMAIN 24..131
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 145..480
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 511 AA; 53886 MW; 296D5EE1A2348F87 CRC64;
MPDPNGFLRY DRRLPARRPV PVRISDWREV YPPAGEELVR EQATRCMDCG IPFCHDGCPL
GNRIPDWNDL VRTGNWDAAV ESLHATNNFP EFTGRLCPAP CEAACVLGIA GGQPVTIKQV
EVEIADAAAA RGLTPRPVPA PSGRSVAVVG SGPAGLAAAQ QLARAGHAVT VYERDDAIGG
LLRYGIPDFK LEKRHIDARL AQLTAEGVRF RTGVNVGVDV TAEQLRAEHD AVLLAAGALQ
GRDTPETPGR ALRGVHQAMA HLVAANRAVA TATDGGPGVA VTGEGRAARA VLPDGTPIDA
AGKHVVIIGG GDTAADCLGV AHRQGAAGVH QLDLYPQPPQ ERDEARDPWP TWPWVLRSYP
AHEEGGERVF AVAVQEFVDD GTGQVRAVRI AEVTVEKRDG RRVVTVVPGS ERELPADLVL
LAIGFEGTEQ QPLLEQFGVT RNPRGAIDAR DDWQTAADGV FVAGDMHRGA SLIVWAIAEG
RAAAAAIHGY LGGATALPAP VGPAAQPLAA R
//
