ID A0A0M3DBM4_9MICO Unreviewed; 488 AA.
AC A0A0M3DBM4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KKX98888.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:KKX98888.1};
GN Name=gltD {ECO:0000313|EMBL:KKX98888.1};
GN ORFNames=AAY78_04280 {ECO:0000313|EMBL:KKX98888.1};
OS Microbacterium sp. Ag1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1643443 {ECO:0000313|EMBL:KKX98888.1, ECO:0000313|Proteomes:UP000034223};
RN [1] {ECO:0000313|EMBL:KKX98888.1, ECO:0000313|Proteomes:UP000034223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKX98888.1,
RC ECO:0000313|Proteomes:UP000034223};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-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:KKX98888.1}.
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DR EMBL; LBCR01000025; KKX98888.1; -; Genomic_DNA.
DR RefSeq; WP_046747120.1; NZ_LBCR01000025.1.
DR AlphaFoldDB; A0A0M3DBM4; -.
DR GeneID; 69643008; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000034223; Unassembled WGS sequence.
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; 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; 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:KKX98888.1}.
FT DOMAIN 25..132
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 146..455
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 488 AA; 52919 MW; BD5C15EB3A9E0F17 CRC64;
MADPKGFLKV TERELPARRP VPVRIMDWKE VYEPGDKQVL RRQAGRCMDC GVPFCHQGCP
LGNLIPEWND LTWRGEGRAA IERLHATNNF PEFTGRLCPA PCESSCVLGI NQPAVTIKQI
EVSIIDEAFS KGWVEPEPPE RLTGKTVAVV GSGPAGLAAA QQLTRAGHTV AVFERDDRIG
GLLRYGIPDF KMEKTQLESR LRQMQEEGTR FRAGVEIGKD ISWPDLRARY DAVVIATGST
VPRDLAIPGR DLDGVHFAME YLVESNHAVA GDKVTDQISA EGKHVIVIGG GDTGADCIGT
AHRQGALSVT NLAIGKQPGD TRPDHQPWPM MPTLFEVSSA HEEGGERVFL ASTVEFLGND
VGEVRALRVA ETEFVDGRRV PKSGTEREIP ADLILIAMGF TGPEQDGYTE ETLPQVTDRG
AFRRDSSYES TVPGVFVAGD AGRGQSLIVW AIAEGRAAAA NVDRFLMGTT VLPEPVRPSD
VAIGLQPA
//
