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Database: UniProt
Entry: Q034U4_LACP3
LinkDB: Q034U4_LACP3
Original site: Q034U4_LACP3 
ID   Q034U4_LACP3            Unreviewed;       477 AA.
AC   Q034U4;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   24-JAN-2024, entry version 103.
DE   RecName: Full=glutamate synthase (NADPH) {ECO:0000256|ARBA:ARBA00012079};
DE            EC=1.4.1.13 {ECO:0000256|ARBA:ARBA00012079};
GN   OrderedLocusNames=LSEI_2555 {ECO:0000313|EMBL:ABJ71278.1};
OS   Lacticaseibacillus paracasei (strain ATCC 334 / BCRC 17002 / CCUG 31169 /
OS   CIP 107868 / KCTC 3260 / NRRL B-441) (Lactobacillus paracasei).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=321967 {ECO:0000313|EMBL:ABJ71278.1, ECO:0000313|Proteomes:UP000001651};
RN   [1] {ECO:0000313|EMBL:ABJ71278.1, ECO:0000313|Proteomes:UP000001651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 334 / BCRC 17002 / CCUG 31169 / CIP 107868 / KCTC 3260 /
RC   NRRL B-441 {ECO:0000313|Proteomes:UP000001651};
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA   Kozyavkin S., Weimer B., Mills D.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000423; ABJ71278.1; -; Genomic_DNA.
DR   RefSeq; WP_003596237.1; NC_008526.1.
DR   RefSeq; YP_807720.1; NC_008526.1.
DR   AlphaFoldDB; Q034U4; -.
DR   STRING; 321967.LSEI_2555; -.
DR   PaxDb; 321967-LSEI_2555; -.
DR   KEGG; lca:LSEI_2555; -.
DR   PATRIC; fig|321967.11.peg.2496; -.
DR   HOGENOM; CLU_000422_3_1_9; -.
DR   OMA; DCVGTAH; -.
DR   Proteomes; UP000001651; Chromosome.
DR   GO; GO:0016040; F:glutamate synthase (NADH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; 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; 2.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 2.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABJ71278.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001651}.
FT   DOMAIN          23..142
FT                   /note="Dihydroprymidine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF14691"
FT   DOMAIN          157..329
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          379..457
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   477 AA;  52416 MW;  F0FEEA907ACAE200 CRC64;
     MADPKGFLKY LRQDDPMRPI MQRIKDFNVM ELDLDMAERR KQAARCMNCG IPFCHHGVFF
     GGGRAVSGCP NDNLIPEWND LVYRDQDKRA FERLSRSNML PDMTGRVCPA PCEVSCVQAL
     NGAGITIRNN EKFIIEQAFK HGWVVDSGKP LHRTGKKIAV VGSGPAGIAA AWRLNQLGHA
     VTLFERDDRF GGFLMYGIPN MKLPKDVVQR RIDTLTKVGI ELVANTEVGK DITADELKKT
     FDRVVICTGA REARDLKVPG RELSGIMQAT DFLKAATQTV LKDGPAANDQ LKGKHVLVLG
     GGDTGNDCIG TAIRQGCADI TQLEITPALP AERRPQNQWP EWPMVLKTGY GQKEAKALFG
     DITAYASTVT AFFGKDGQVK EAEISQVDHF KPVAGTEKKI KADLVVLAMG FTGAEQWLFD
     QFGITAKNDN FTTNDTQIYV AGDCRRGPSL VIWGIHEGRM CAEGVDASLR TLASETL
//
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