ID Q5FPV7_GLUOX Unreviewed; 479 AA.
AC Q5FPV7;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Glutamate synthase [NADPH] small chain {ECO:0000313|EMBL:AAW61589.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:AAW61589.1};
GN OrderedLocusNames=GOX1851 {ECO:0000313|EMBL:AAW61589.1};
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633 {ECO:0000313|EMBL:AAW61589.1, ECO:0000313|Proteomes:UP000006375};
RN [1] {ECO:0000313|EMBL:AAW61589.1, ECO:0000313|Proteomes:UP000006375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H {ECO:0000313|EMBL:AAW61589.1,
RC ECO:0000313|Proteomes:UP000006375};
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
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DR EMBL; CP000009; AAW61589.1; -; Genomic_DNA.
DR RefSeq; WP_011253370.1; NZ_LT900338.1.
DR AlphaFoldDB; Q5FPV7; -.
DR STRING; 290633.GOX1851; -.
DR KEGG; gox:GOX1851; -.
DR eggNOG; COG0493; Bacteria.
DR HOGENOM; CLU_000422_3_1_5; -.
DR Proteomes; UP000006375; Chromosome.
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 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; IPR006006; GltD-like.
DR InterPro; IPR009051; Helical_ferredxn.
DR NCBIfam; TIGR01318; gltD_gamma_fam; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AAW61589.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006375}.
FT DOMAIN 24..134
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 149..456
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 479 AA; 52123 MW; 8918F7944974756F CRC64;
MAERMLQFVT HPQVLPEKRD AAERRQDFGE IYRGFARSRA EEQASRCSQC GIPFCSVHCP
LGNNIPDWLK LTAEDRLEEA YEMSSATNTF PEICGRICPQ DRLCEGNCVI NKGFESVTIG
AVERFITENA FEQGWVKPAL PDRDLGRSVG IVGSGPAGLA CAERLRAQGY EVHVYERQDR
VGGLLTYGIP SFKLEKHVVA RRHALLEEQG IVFHLSTPVG SGEGETSLED LRARHDAVFL
ATGVYRSRDV KVPGAGLEGV VDAIDFLTAS NRRGYDEDPG EDAALHAKGR RVVVIGGGDT
AMDCVRTSIR QGAERVTCVY RRDRANMPGS RQEVYNAEEE GAHFEWLGSP EAFLGDSSVS
GVRVLKMRLG APDASGRRSI EGTGQHDVIE GDLVIKALGF DPEDLPGQFN EPELAVTRWG
TLTVPPGGFE TSLPGVFAGG DIVRGASLVV WAIKDGRDAA DAIHHYLTET VTGSLEAAE
//
