ID Q1GR75_SPHAL Unreviewed; 480 AA.
AC Q1GR75;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 24-JAN-2024, entry version 94.
DE RecName: Full=glutamate synthase (NADPH) {ECO:0000256|ARBA:ARBA00012079};
DE EC=1.4.1.13 {ECO:0000256|ARBA:ARBA00012079};
GN OrderedLocusNames=Sala_2138 {ECO:0000313|EMBL:ABF53847.1};
OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS (Sphingomonas alaskensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=317655 {ECO:0000313|EMBL:ABF53847.1, ECO:0000313|Proteomes:UP000006578};
RN [1] {ECO:0000313|EMBL:ABF53847.1, ECO:0000313|Proteomes:UP000006578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13593 / LMG 18877 / RB2256
RC {ECO:0000313|Proteomes:UP000006578};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(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; CP000356; ABF53847.1; -; Genomic_DNA.
DR RefSeq; WP_011542423.1; NC_008048.1.
DR AlphaFoldDB; Q1GR75; -.
DR STRING; 317655.Sala_2138; -.
DR KEGG; sal:Sala_2138; -.
DR eggNOG; COG0493; Bacteria.
DR HOGENOM; CLU_000422_3_1_5; -.
DR OMA; QSHCPLH; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000006578; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
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,
KW ECO:0000313|EMBL:ABF53847.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006578}.
FT DOMAIN 25..136
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 151..453
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 480 AA; 52131 MW; C777CAE4FB6AC968 CRC64;
MVSERMLQFV GREQSYPDKR SPEERARDFR EIAERYSAPD ADAQAARCSQ CGVPYCSVHC
PLHNHIPDWL RLTAEGRLRE AYELSNATST MPEICGRICP QDRLCEGNCV IEFSGHGAVT
IGSVEKYITD TAWAEGWVEP LRVGPATGQS VGVIGAGPAG LTAAEYLRAA GHDVHVYDRH
DRAGGLLTYG IPGFKLEKDV VMRRIDRLAA GGIQFHLGFE VGKDATLDGL RQKHDAILIA
TGVYKAREIN VPGNEAEGVI AALDYLVASN RKGFGDAVPA FDDGRLNAAG KHVVVIGGGD
TAMDCVRTAV RQGARSVKCL YRRDRENMPG SQREVANAEE EGVEFVWLSA PESFTADRHV
KEVAVAGMRL GAPDASGRRS PEVDPGRRFD VPADMVIKAL GFDPEELPHL FGAPDLSVTR
WGTLRVDHQT MMTSLPGVFA AGDIVRGASL VVWGIRDGRD VSDQMAKWLK AKAKSEKKAA
//