ID C7LX68_DESBD Unreviewed; 466 AA.
AC C7LX68;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=glutamate synthase (NADPH) {ECO:0000256|ARBA:ARBA00012079};
DE EC=1.4.1.13 {ECO:0000256|ARBA:ARBA00012079};
GN OrderedLocusNames=Dbac_0617 {ECO:0000313|EMBL:ACU88741.1};
OS Desulfomicrobium baculatum (strain DSM 4028 / VKM B-1378 / X)
OS (Desulfovibrio baculatus).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfomicrobiaceae; Desulfomicrobium.
OX NCBI_TaxID=525897 {ECO:0000313|EMBL:ACU88741.1, ECO:0000313|Proteomes:UP000002216};
RN [1] {ECO:0000313|EMBL:ACU88741.1, ECO:0000313|Proteomes:UP000002216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4028 / VKM B-1378 / X {ECO:0000313|Proteomes:UP000002216};
RX PubMed=21304634; DOI=10.4056/sigs.13134;
RA Copeland A., Spring S., Goker M., Schneider S., Lapidus A., Del Rio T.G.,
RA Tice H., Cheng J.F., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavrommatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.C., Meincke L.,
RA Sims D., Brettin T., Detter J.C., Han C., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lucas S.;
RT "Complete genome sequence of Desulfomicrobium baculatum type strain (X).";
RL Stand. Genomic Sci. 1:29-37(2009).
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}.
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DR EMBL; CP001629; ACU88741.1; -; Genomic_DNA.
DR RefSeq; WP_015772841.1; NC_013173.1.
DR AlphaFoldDB; C7LX68; -.
DR STRING; 525897.Dbac_0617; -.
DR KEGG; dba:Dbac_0617; -.
DR eggNOG; COG0493; Bacteria.
DR HOGENOM; CLU_000422_3_3_7; -.
DR OMA; QSHCPLH; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000002216; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; 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 InterPro; IPR006004; SudA-like.
DR NCBIfam; TIGR01316; gltA; 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 Reference proteome {ECO:0000313|Proteomes:UP000002216}.
FT DOMAIN 20..129
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 143..451
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 466 AA; 50001 MW; 0BBFE66C26A2A827 CRC64;
MGAANQKSRQ AMPEQDPHVR ARNFEEVPLG YTPEMAIAEA SRCLQCKNPL CVQGCPVGVA
IPEFIKHIAD GKFDLAIGKI WERNSLPAVC GRVCPQEVQC EGNCILGRKG EAVAIGNLER
FAADWERANH ACELPSREKA TGKKVAVVGS GPSGLTVAGD LILKGHEVTI FEAFHKPGGV
LVYGIPEFRL PKEIVASEVS CLQAQGARIE CDVVVGRTET VDELFEQGFD AVYLGVGAGL
PRFMNIPGEN MIGVLSANEY LTRANLMKAY LFPQVDTPIP HGRNVVVLGA GNVAMDSART
AMRLGAEKVS IVYRRSRAEM PARSAEIHHA EEEGLHFELL SNPVRYLGDE KGRLTGIECV
RMELGEPDAS GRRRPVVVPG SEFVIECDLA IVAIGSGANP LLTRSTPDLP LGKSGYIMAN
PETGKTGKKA VWAGGDIVTG AATVILAMGA GRKAADSIHE YLTWGW
//