ID A9QPA6_9BACT Unreviewed; 478 AA.
AC A9QPA6;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=glutamate synthase (NADPH) {ECO:0000256|ARBA:ARBA00012079};
DE EC=1.4.1.13 {ECO:0000256|ARBA:ARBA00012079};
GN ORFNames=MBMO_EB00055B11g063 {ECO:0000313|EMBL:ABX59274.1};
OS uncultured marine bacterium EB000_55B11.
OC Bacteria; environmental samples.
OX NCBI_TaxID=480665 {ECO:0000313|EMBL:ABX59274.1};
RN [1] {ECO:0000313|EMBL:ABX59274.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18028413; DOI=10.1111/j.1462-2920.2007.01471.x;
RA Rich V.I., Konstantinidis K., DeLong E.F.;
RT "Design and testing of 'genome-proxy' microarrays to profile marine
RT microbial communities.";
RL Environ. Microbiol. 10:506-521(2008).
RN [2] {ECO:0000313|EMBL:ADI19955.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20695878; DOI=10.1111/j.1462-2920.2010.02314.x;
RA Rich V.I., Pham V.D., Eppley J., Shi Y., DeLong E.F.;
RT "Time-series analyses of Monterey Bay coastal microbial picoplankton using
RT a 'genome proxy' microarray.";
RL Environ. Microbiol. 13:116-134(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU221239; ABX59274.1; -; Genomic_DNA.
DR EMBL; GU474935; ADI19955.1; -; Genomic_DNA.
DR AlphaFoldDB; A9QPA6; -.
DR GO; GO:0051539; F:4 iron, 4 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; 3.
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; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 25..136
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 151..458
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 478 AA; 52434 MW; D3A4F72B1F995E9E CRC64;
MAVNKMLKFV HVSRDMPTKR MPKLRNKDYN EVYQEFAAEK AEEQSSRCSQ CGVPFCQTHC
PLHNNIPDWL RLTAEGRLKE AYELSQDTNT FPEICGRICP QDRLCEGNCV IEQSGHETVT
IGSVEKYITD TAWEKGWVKA ITPKVERSES VGIIGAGPAG LAAADRLRKM GIQVTIYDRY
DRAGGLLTYG IPGFKLEKDV VMRRNDLLSE GGVNFELNTN IGIDISFHDI RSKHDAILIG
TGVYKARELS GIGSSNKGIV KALDYLTASN RSNMGDHVPE IENGELNAKG KRIVVIGGGD
TAMDCVRTAI RQGAKSVKCL YRRDKKNMPG SQRETQNAEE EGVEFVWLSA PKGFVGEGEV
SGVVVSKMRL GAPDSSGRQS PEEIVGADYT EDADLVIKAL GFNPENLPTL WDTPELEVTR
WGTIKTDFKT HSTSLPGVYA AGDIVRGASL VVWAIRDGRE AADSILAFLD TQTSIAAE
//