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Database: UniProt
Entry: U5E5G2_NOCAS
LinkDB: U5E5G2_NOCAS
Original site: U5E5G2_NOCAS 
ID   U5E5G2_NOCAS            Unreviewed;       489 AA.
AC   U5E5G2;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Glutamate synthase small subunit {ECO:0000313|EMBL:GAD85007.1};
GN   Name=gltD {ECO:0000313|EMBL:GAD85007.1};
GN   ORFNames=NCAST_25_04300 {ECO:0000313|EMBL:GAD85007.1};
OS   Nocardia asteroides NBRC 15531.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1110697 {ECO:0000313|EMBL:GAD85007.1, ECO:0000313|Proteomes:UP000017048};
RN   [1] {ECO:0000313|EMBL:GAD85007.1, ECO:0000313|Proteomes:UP000017048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 15531 {ECO:0000313|EMBL:GAD85007.1,
RC   ECO:0000313|Proteomes:UP000017048};
RX   PubMed=24884595; DOI=10.1186/1471-2164-15-323;
RA   Komaki H., Ichikawa N., Hosoyama A., Takahashi-Nakaguchi A., Matsuzawa T.,
RA   Suzuki K., Fujita N., Gonoi T.;
RT   "Genome based analysis of type-I polyketide synthase and nonribosomal
RT   peptide synthetase gene clusters in seven strains of five representative
RT   Nocardia species.";
RL   BMC Genomics 15:323-323(2014).
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:GAD85007.1}.
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DR   EMBL; BAFO02000025; GAD85007.1; -; Genomic_DNA.
DR   RefSeq; WP_022566565.1; NZ_VBUS01000001.1.
DR   AlphaFoldDB; U5E5G2; -.
DR   STRING; 1824.SAMN05444423_101288; -.
DR   eggNOG; COG0493; Bacteria.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000017048; 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; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000017048}.
FT   DOMAIN          28..131
FT                   /note="Dihydroprymidine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF14691"
FT   DOMAIN          146..460
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   489 AA;  53260 MW;  EDD0C39DF8D2A459 CRC64;
     MADPQGFLKH TSRELPTRRP VELRLLDWKE VYEDKFSHDT LQKQASRCMD CGIPFCHNGC
     PLGNLIPEWN DLVYKGAWRE GIDRLHATNN FPEFTGRLCP APCEASCVLG INQQPVTIKQ
     VEVELIENAF DEGWVTPVYP TRLTGKKVAV VGSGPAGLAA AQQLTRAGHT VTVFERDDRI
     GGLMRYGIPE FKMEKSVIDR RLAQMEAEGT IFKTGVNVGV DITAEQLRER FDAVVLAGGA
     TIARDLPIPG RELDGIHQAM EFLPLANRVQ LGDDITDENG LPPIHAKGKK VVIIGGGDTG
     ADCLGTSHRH GAESVHQFEI MPRPPEERAG STPWPTYPLM YRVSSAHEEG GERVFSVNTE
     RFVGKDGKVT GLEAHEVKMA NGRFEKVEGT DFTLEADLVL LAMGFVGPQK PGLLTDLGVG
     YDGRGNVQRD KNWATNIPGV FVAGDMGRGQ SLIVWAIAEG RAAAASVDKF LEGETALPAP
     IPPTAVAQR
//
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