ID C3MGG1_SINFN Unreviewed; 453 AA.
AC C3MGG1;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Glutamate synthase [NADPH] large chain {ECO:0000313|EMBL:ACP26233.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:ACP26233.1};
GN Name=gltB2 {ECO:0000313|EMBL:ACP26233.1};
GN OrderedLocusNames=NGR_c24760 {ECO:0000313|EMBL:ACP26233.1};
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394 {ECO:0000313|EMBL:ACP26233.1, ECO:0000313|Proteomes:UP000001054};
RN [1] {ECO:0000313|EMBL:ACP26233.1, ECO:0000313|Proteomes:UP000001054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
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DR EMBL; CP001389; ACP26233.1; -; Genomic_DNA.
DR RefSeq; WP_012708991.1; NC_012587.1.
DR RefSeq; YP_002826986.1; NC_012587.1.
DR AlphaFoldDB; C3MGG1; -.
DR STRING; 394.NGR_c24760; -.
DR KEGG; rhi:NGR_c24760; -.
DR PATRIC; fig|394.7.peg.5298; -.
DR eggNOG; COG0493; Bacteria.
DR HOGENOM; CLU_000422_3_3_5; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000001054; Chromosome.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
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; IPR009051; Helical_ferredxn.
DR PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:ACP26233.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT DOMAIN 20..129
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 142..431
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 453 AA; 48160 MW; C82937ABD74615AD CRC64;
MGTTQSGILY GRLPLAEYEA NFSDLHPPLD KHEALVAADR CYFCHDAPCM TACPTSIDIP
LFIRQIATGN PIGSAKTIFD QNILGGMCAR VCPTETLCEQ ACVRNTAEER PVEIGRLQRY
STDIAMRENK QFYARAAATG RRIAVVGAGP AGLACAHRLA VEGHDVVIYD AREKSGGLNE
YGIAAYKTVD DFAQREVDYV LSIGGIEVRH GEALGRDFSL ADLTEEYDAV FLGLGLAGVN
ALRVEGENAE GVEDAVDFIA ALRQSKTKAD IPVGRRVVVL GGGMTAIDAA VQAKLLGAEE
VTICYRRGKE HMNASEFEQD LASSKGVTIR HWLQPKRIAV KDGKVAGIEL EYTTLEDGKL
TTTGETGIIA AEQIFKAIGQ TFQASGLGAL QMESGRIVVD AAGRTSLAKV WAGGDCVLGG
EDLTVSAVAM GRDCAESINR AFAADAPLAS AVA
//
