ID   GLTD_CERSP              Reviewed;         413 AA.
AC   O08340;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Putative glutamate synthase [NADPH] small chain;
DE            EC=1.4.1.13;
DE   AltName: Full=Glutamate synthase subunit beta;
DE            Short=GLTS beta chain;
DE   AltName: Full=NADPH-GOGAT;
GN   Name=gltD;
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=601;
RX   PubMed=12219208;
RA   Lu T., Wu Y.Q., Song H.Y.;
RT   "The nucleotide Sequence of gltD gene encoding the small subunit of
RT   Rhodobacter sphaeroides glutamate synthase.";
RL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 29:294-302(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + L-glutamine
CC         + NADPH; Xref=Rhea:RHEA:15501, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:58359; EC=1.4.1.13;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC       pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+)
CC       route): step 1/1.
CC   -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC   -!- SUBUNIT: Aggregate of 4 catalytic active heterodimers, consisting of a
CC       large and a small subunit. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Glutamine binds to the large subunit and transfers the
CC       amido group to 2-oxo-glutamate that apparently binds to the small
CC       subunit. {ECO:0000250}.
CC   -!- CAUTION: Lacks the 4Fe-4S ferredoxin-type domain found in GltD
CC       orthologs. {ECO:0000305}.
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DR   EMBL; Y12481; CAA73084.1; -; Genomic_DNA.
DR   PIR; JE0142; JE0142.
DR   AlphaFoldDB; O08340; -.
DR   SMR; O08340; -.
DR   PRIDE; O08340; -.
DR   UniPathway; UPA00045; -.
DR   UniPathway; UPA00634; UER00689.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0097054; P:L-glutamate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1060.10; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR006006; GltD-like.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   PANTHER; PTHR42783:SF1; PTHR42783:SF1; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Glutamate biosynthesis; Iron; Iron-sulfur;
KW   Metal-binding; NADP; Oxidoreductase.
FT   CHAIN           1..413
FT                   /note="Putative glutamate synthase [NADPH] small chain"
FT                   /id="PRO_0000386547"
FT   BINDING         33
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         37
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         43
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         47
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   413 AA;  44407 MW;  A177838E418A2254 CRC64;
     MAKEPMLQFV KMARETPEKR PRSLRSQDFH EICGRICPQD RLCEGNCVIE QSGHGTVTIG
     AVEKYITDTA WENGWVVPGK PAYERSESVG IIGAGPGGLA AADALRRAGL QVTVYDRYDR
     AGGLLTYGIP GFKLEKDVVA RRVEQLEQAG VQFVLNCNVG EDLSFDAIRG QHDAVLIATG
     VYKQRDLAAP GVGSAGVVQA LSYLTASNRR SFGDEVDDDG LDASGKRVVV IGGGDTAMDC
     VRTAIRQGAT SVKCLYRRDR ANMPGSQREV ANAEEEGVEF VWLSAPRGFI AGDAVEGVIV
     QKMRLGEPDA TGRQMPEIIE GADYVEPADL AIMALGFEPE DLPTLWGVPD LTVTRWGTIK
     ADFRTHATSL PGVYAVGDIV RGASLVVWAI RDGRDAAQSI LDYLAQPAVV AAE