ID E5VLS6_9FIRM Unreviewed; 610 AA.
AC E5VLS6;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=glutamate synthase (NADPH) {ECO:0000256|ARBA:ARBA00012079};
DE EC=1.4.1.13 {ECO:0000256|ARBA:ARBA00012079};
GN ORFNames=HMPREF0996_01988 {ECO:0000313|EMBL:EFV16200.1};
OS Lachnospiraceae bacterium 5_1_63FAA.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=658089 {ECO:0000313|EMBL:EFV16200.1, ECO:0000313|Proteomes:UP000005278};
RN [1] {ECO:0000313|EMBL:EFV16200.1, ECO:0000313|Proteomes:UP000005278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5_1_63FAA {ECO:0000313|EMBL:EFV16200.1,
RC ECO:0000313|Proteomes:UP000005278};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C.,
RA Allen-Vercoe E., Ambrose C., Strauss J., Daigneault M., Haas B.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium strain 5_1_63FAA.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFV16200.1}.
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DR EMBL; ACTS01000043; EFV16200.1; -; Genomic_DNA.
DR AlphaFoldDB; E5VLS6; -.
DR HOGENOM; CLU_000422_3_4_9; -.
DR Proteomes; UP000005278; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
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; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF140490; Nqo1C-terminal domain-like; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 2.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 37..82
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT sulphur binding"
FT /evidence="ECO:0000259|SMART:SM00928"
SQ SEQUENCE 610 AA; 66330 MW; C29D22E8D6A58079 CRC64;
MSRLELRSPN QAQLVVEGLY KDLERRIESS PPGLCPVDMS RAFLEICHAQ SCGKCVPCRV
GLGQLKNLIT DVLDGKATIR TLTEIHETAK SIMESADCAI GYEAANMVYK GAIGFKDDYV
EHIMYHRCLS TLKQPVPCVS RCPARVDIPG YIALVREGRY EDAIRLIRKD NPFPTTCGFI
CEHPCEALCR RNMIDDAVNI RGLKRMAADA AGYVAPPECA ESTGKNIAVV GGGPGGLSAA
YFLQLMGHQV TVYEMLPKLG GMLRYGIPNY RLPKERLDDD IQAILDTGVK VDCGKAIGKD
YSIVDLKEKY DAVLITIGAS TDKKLGLEGE DAKGVISAVQ FLRNVGYGTQ ESLEGKEVAV
IGGGNVSMDA VRTSVRFGAK KVSIVYRRRV ADMTALPDEI SGAEAEGVEI KTLMAPSRIE
KDEEGNVKGI WVTPQMISNI KGGRASVKPT GEDDVFIPCQ TLIVAIGQDI EYQHFEEAGV
PVQRGKINVE KFGGFEEMPG VFAGGDCATG PSTVISAIAA GKVIAANIDE YLGYHHEITA
DVEIPEPKLE DKPACGRVNL TEREAGERVK DFEGVENCMT EKEACQEAGR CLRCDHFGYG
IFKGGRDTKW
//