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Database: UniProt
Entry: A0A0W7YZP4_9BURK
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Original site: A0A0W7YZP4_9BURK 
ID   A0A0W7YZP4_9BURK        Unreviewed;       491 AA.
AC   A0A0W7YZP4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=glutamate synthase (NADPH) {ECO:0000256|ARBA:ARBA00012079};
DE            EC=1.4.1.13 {ECO:0000256|ARBA:ARBA00012079};
GN   Name=gltD {ECO:0000313|EMBL:KUF40636.1};
GN   ORFNames=AS359_03750 {ECO:0000313|EMBL:KUF40636.1};
OS   Comamonas kerstersii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=225992 {ECO:0000313|EMBL:KUF40636.1, ECO:0000313|Proteomes:UP000053300};
RN   [1] {ECO:0000313|EMBL:KUF40636.1, ECO:0000313|Proteomes:UP000053300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12322-1 {ECO:0000313|EMBL:KUF40636.1,
RC   ECO:0000313|Proteomes:UP000053300};
RA   Ming D., Wang M., Hu S., Zhou Y., Jiang T.;
RT   "Complete genome sequence of a multi-drug resistant strain Acidovorax sp.
RT   12322-1.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00001895};
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. {ECO:0000256|ARBA:ARBA00037898}.
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:KUF40636.1}.
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DR   EMBL; LPXH01000027; KUF40636.1; -; Genomic_DNA.
DR   RefSeq; WP_058880018.1; NZ_LPXH01000027.1.
DR   AlphaFoldDB; A0A0W7YZP4; -.
DR   STRING; 225992.B5M06_07775; -.
DR   Proteomes; UP000053300; 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; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053300}.
FT   DOMAIN          37..68
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   491 AA;  53509 MW;  13527531665ECC8A CRC64;
     MGKTTGFLEY DRIEEGYLPV AERVKNYKEF VIALTPEQAK IQGARCMDCG TPFCNNGCPI
     NNIIPDFNDL VYRGDWASAI EVLHSTNNFP EFTGRICPAP CEAACVANIN RAPIGIKSIE
     HAIIDRAWEE GWVKPQPPVR LTGKKVAVVG AGPAGLAAAQ QLVRAGHDVT LFEKNDQVGG
     LLRYGIPDFK LDKANIDRRV EQLVAEGLKI RTGVLVAGKD GLGKDSKVTN WAKETISPEQ
     LMEEFDAVLL TGGAEQSRDL PVPGRDLKGV HFAMEFLPQQ NKATREGKYK GQIRADGKHV
     VVIGGGDTGS DCVGTSNRHG AVSVTQLELM PMPPEQENKP LVWPYWPLKL RTSSSHEEGC
     VREFAIGTKE FIGEKGQLTG VKTVRLEWKD GKMTEVPGSE QIIKADLVFL AMGFVSPVQA
     VLDAFGVEKD QRGNAKASTD LVGGYATSVP KLFAAGDMRR GQSLVVWAIR EGRQAARAVD
     EFLMGETTLP R
//
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