ID A0A1D7YH30_9ACTN Unreviewed; 487 AA.
AC A0A1D7YH30;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:AOR34903.1};
GN Name=gltD {ECO:0000313|EMBL:AOR34903.1};
GN ORFNames=BFF78_31055 {ECO:0000313|EMBL:AOR34903.1};
OS Streptomyces fodineus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1904616 {ECO:0000313|EMBL:AOR34903.1, ECO:0000313|Proteomes:UP000094960};
RN [1] {ECO:0000313|Proteomes:UP000094960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW1S1 {ECO:0000313|Proteomes:UP000094960};
RA Kim M.-K., Kim S.B.;
RT "Streptomyces puniciscabiei strain:TW1S1 Genome sequencing and assembly.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR EMBL; CP017248; AOR34903.1; -; Genomic_DNA.
DR RefSeq; WP_069781446.1; NZ_CP017248.1.
DR AlphaFoldDB; A0A1D7YH30; -.
DR KEGG; spun:BFF78_31055; -.
DR Proteomes; UP000094960; Chromosome.
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; IPR017896; 4Fe4S_Fe-S-bd.
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.
DR PROSITE; PS51379; 4FE4S_FER_2; 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}.
FT DOMAIN 38..69
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 487 AA; 52825 MW; E9F9BF405848E0BD CRC64;
MADPKGFLNH GREVAQTRPV GDRVKDWNEV YVPGSLLPII SKQASRCMDC GIPFCHNGCP
LGNLIPEWND YAYREDWAAA QERLHATNNF PEFTGRLCPA PCESACVLGI NQPPVTIKNV
EVSIIDKAWD AGTVAPQIPE RLSGKTVAVI GSGPAGLAAA QQLTRAGHTV AVYERADRVG
GLLRYGIPEF KMEKRHINRR IEQMRAEGTR FRTGVEIGRD INARDLKKRY DAIVIAAGAT
TARDLPVPGR ELKGIYQAME YLPLANKVQE GDYVTAPISA EGKHVVVIGG GDTGADCVGT
AHRQGAASVT QLEIMPRPND ERHPTNQPWP TFPILYKVTS AHEEGGERIY SASTTHFEGD
EDGNVQWLHL AEVEFVDGKL TQKPGTERKI PAQLVTLAMG FTGTDRDNGL VEQFGLDLDA
RGNIARDADF QTNVPGVFVA GDAGRGQSLI VWAIAEGRSA ARGVDRFLTG ASDLPAPIRP
TDRALAV
//
