ID A0A0W7W828_9MICO Unreviewed; 485 AA.
AC A0A0W7W828;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KUF06740.1};
GN Name=gltD {ECO:0000313|EMBL:KUF06740.1};
GN ORFNames=AUL38_12040 {ECO:0000313|EMBL:KUF06740.1};
OS Leucobacter sp. G161.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=663704 {ECO:0000313|EMBL:KUF06740.1, ECO:0000313|Proteomes:UP000053012};
RN [1] {ECO:0000313|EMBL:KUF06740.1, ECO:0000313|Proteomes:UP000053012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G161 {ECO:0000313|EMBL:KUF06740.1,
RC ECO:0000313|Proteomes:UP000053012};
RA Ge S., Dong X.;
RT "High quality draft genome sequence of Leucobacter sp. G161, a distinct and
RT effective chromium reducer.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KUF06740.1}.
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DR EMBL; LOHP01000064; KUF06740.1; -; Genomic_DNA.
DR RefSeq; WP_059061991.1; NZ_LOHP01000064.1.
DR AlphaFoldDB; A0A0W7W828; -.
DR STRING; 663704.AUL38_12040; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000053012; 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; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; 1.
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:UP000053012}.
FT DOMAIN 27..132
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 146..457
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 485 AA; 51416 MW; 9902F4B90831915D CRC64;
MVDTHGFLKV RERELAPKRP VALRLMDWRE VVERGDAAVI GRQASRCMDC GVSFCHQGCP
LGNLIPEWND LTHRGRSREA IDRLHETNNF PEFTGRACPA PCESACVLGI NQPAVTIKQI
ENHIIDEAFE RGWVTPQPPA RLTGKTVAVV GSGPAGLAAA QQLTRAGHTV AVYERDEAPG
GLLRFGIPDF KLEKALVARR IEQLKAEGTR FRCGVELGTD MSWGELRRRF DAIVIATGAP
VPRELALPGR ELSGIMPAMD FLVAANRVQS GALPSAEHAG SVVDAAGKHV VVIGGGDTGA
DCVGTAHRQG ALSVTSLAIG KQPGVLRPTG QPWPTHPTIF EVSSSHEEGG HREYLASTVE
FVGKSAVTGL RVAETGFTDS GRVPLAGTER LIAADLVLIA LGFTGPEAVD DPAVALTMNS
EGSFERARDF STDHPGVFVA GDAGRGQSLI VWAIAEGRSA AAADRYLTGG TVLPSPVGAF
DRAFA
//
