ID A0A0U3QAF1_9ACTN Unreviewed; 487 AA.
AC A0A0U3QAF1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:ALV36301.1};
GN Name=gltD {ECO:0000313|EMBL:ALV36301.1};
GN ORFNames=AS200_32795 {ECO:0000313|EMBL:ALV36301.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV36301.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV36301.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV36301.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR EMBL; CP013743; ALV36301.1; -; Genomic_DNA.
DR RefSeq; WP_058925899.1; NZ_CP013743.1.
DR AlphaFoldDB; A0A0U3QAF1; -.
DR STRING; 1725411.AS200_32795; -.
DR KEGG; scx:AS200_32795; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000068029; 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; 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000068029}.
FT DOMAIN 40..131
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 146..319
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 364..457
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 487 AA; 52897 MW; 6ABDB44D399E496F CRC64;
MADPKGFLNH GREVAKSRPV EERVKDWNEV YVPGSLLPII SKQAGRCMDC GIPFCHNGCP
LGNLIPEWND YAYREDWTAA SERLHATNNF PEFTGRLCPA PCESACVLGI NQPAVTIKNV
EVSIIDKAWD AGTVAAQIPE RLSGKTVAVI GSGPAGLAAA QQLTRAGHTV AVYERADRIG
GLLRYGIPEF KMEKRHINRR IEQMRAEGTR FRTGVEIGRD LKATDLKKRY DAVVIAAGAT
TARDLPVPGR ELKGVYQAME YLPLANKVQE GDYVTAPISA EGKHVVVIGG GDTGADCVGT
AHRQGAASVT QLEIMPRPGE ERNSVTQPWP TFPMLYKVTS AHEEGGERVY SVSTTHFEGD
EDGNVQWLHL TEVEFVEGRL TPKPGTERKI PAQLVTLAMG FTGTDRENGL VEQFGLELDE
RGNIARDADF QTNVPGVFVA GDAGRGQSLI VWAIAEGRSA ARGCDRFLTG ASDLPAPIRP
TDRSLMV
//
