ID E5AXE7_RHIRD Unreviewed; 400 AA.
AC E5AXE7;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Glutamate synthase small subunit {ECO:0000313|EMBL:CBX26090.1};
DE Flags: Fragment;
GN Name=gltD {ECO:0000313|EMBL:CBX26090.1};
OS Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS radiobacter).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=358 {ECO:0000313|EMBL:CBX26090.1};
RN [1] {ECO:0000313|EMBL:CBX26090.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CFBP 2517 {ECO:0000313|EMBL:CBX26090.1};
RA Costechareyre D., Bahena-Ramirez M., Muller D., D'Angelo-Picard C.,
RA Nesme J., Bertolla F., Daubin V., Nesme X.;
RT "Circular and linear chromosome multilocus analysis of the Agrobacterium
RT tumefaciens / biovar 1 species complex.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR EMBL; FR695176; CBX26090.1; -; Genomic_DNA.
DR AlphaFoldDB; E5AXE7; -.
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; 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}.
FT DOMAIN 2..106
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 121..378
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CBX26090.1"
FT NON_TER 400
FT /evidence="ECO:0000313|EMBL:CBX26090.1"
SQ SEQUENCE 400 AA; 43377 MW; D44052EC6C88EAE0 CRC64;
HFREFTIPMS DAEVQKQAAR CMDCGIPYCH GPTGCPVHNQ IPDWNDLVYN NNWEEAIRNL
HSTNNFPEFT GRVCPAPCEE ACTLNLEDAP VAIKTVEQAI ADKAYELGFI VPKPATIHTG
KKVAIIGSGP SGMAAAQQLG RAGHEVHVYE RESKPGGLLR YGIPDFKMEK NFIDRRVEQI
KGEGVTFHCG VNVGVDVTVE ALLADHDAVL YCGGSETPRT AGIGGADFNG VYDAMPYLVQ
QNRRVGRENI DSIGWPADPI LAGGKHVVVV GGGDTASDCV GTAFRQGAVK VTQLDIRPMP
PEKEDKLAVW PFWATKMRTS SSQAEGAVRE FQVATLEFVG EDGVLTGVKC CQVDDRRKPI
AGTEFIIKAD LAFIAIGFSG PFTDSVLKEM DGKLSLNTDR
//