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Database: UniProt
Entry: A9QPA6_9BACT
LinkDB: A9QPA6_9BACT
Original site: A9QPA6_9BACT 
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}.
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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
//
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