ID A0A0E3SR88_METMT Unreviewed; 496 AA.
AC A0A0E3SR88;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 05-FEB-2025, entry version 32.
DE RecName: Full=Archaeal glutamate synthase [NADPH] {ECO:0000256|PIRNR:PIRNR006429};
DE EC=1.4.1.13 {ECO:0000256|PIRNR:PIRNR006429};
GN ORFNames=MCMEM_0725 {ECO:0000313|EMBL:AKB84778.1};
OS Methanococcoides methylutens MM1.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=1434104 {ECO:0000313|EMBL:AKB84778.1, ECO:0000313|Proteomes:UP000033048};
RN [1] {ECO:0000313|EMBL:AKB84778.1, ECO:0000313|Proteomes:UP000033048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM1 {ECO:0000313|EMBL:AKB84778.1,
RC ECO:0000313|Proteomes:UP000033048};
RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT "Methanogenic archaea and the global carbon cycle.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + NADP(+) = L-glutamine + 2-oxoglutarate + NADPH
CC + H(+); 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|PIRNR:PIRNR006429};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|PIRNR:PIRNR006429};
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716, ECO:0000256|PIRNR:PIRNR006429}.
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DR EMBL; CP009518; AKB84778.1; -; Genomic_DNA.
DR RefSeq; WP_048204950.1; NZ_CP009518.1.
DR AlphaFoldDB; A0A0E3SR88; -.
DR STRING; 1434104.MCMEM_0725; -.
DR GeneID; 24893239; -.
DR KEGG; mmet:MCMEM_0725; -.
DR PATRIC; fig|1434104.5.peg.782; -.
DR HOGENOM; CLU_023342_0_1_2; -.
DR OrthoDB; 2837at2157; -.
DR Proteomes; UP000033048; Chromosome.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02808; GltS_FMN; 1.
DR CDD; cd00730; rubredoxin; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR024188; GltB.
DR InterPro; IPR043578; GltB_archl_type.
DR InterPro; IPR002932; Glu_synthdom.
DR InterPro; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR024935; Rubredoxin_dom.
DR PANTHER; PTHR43819; ARCHAEAL-TYPE GLUTAMATE SYNTHASE [NADPH]; 1.
DR PANTHER; PTHR43819:SF1; ARCHAEAL-TYPE GLUTAMATE SYNTHASE [NADPH]; 1.
DR Pfam; PF01645; Glu_synthase; 1.
DR Pfam; PF00301; Rubredoxin; 1.
DR PIRSF; PIRSF500061; GOGAT_lg2_archl; 1.
DR PIRSF; PIRSF006429; GOGAT_lg_2; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF57802; Rubredoxin-like; 1.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR006429};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR006429};
KW FMN {ECO:0000256|PIRNR:PIRNR006429};
KW Glutamate biosynthesis {ECO:0000256|PIRNR:PIRNR006429};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|PIRNR:PIRNR006429};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR006429,
KW ECO:0000313|EMBL:AKB84778.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033048};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..53
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50903"
SQ SEQUENCE 496 AA; 54387 MW; B2429C0EAE6879B8 CRC64;
MTEYRCDVCG AFEYDDSRGD SNTGVKPGTK PEDFPDDWRC PICGADKDHQ KPVEKKEVEE
ITSQEIVTCP KCGRKSKVTV SEFEKIDISG YLGEWKRTSD TTELYMEDIH KISVSGESIL
EPMRTKQDVL SWNDILIKGA QLAKIPLNED ETVNTKTTIG PKAKTPLVIE TPVFITHMSY
GALSKEIKQS LAMGSAAVKT AMCSGEGGIL KESMEKAHKY IFEYVPNRYS VTEDNLKKVD
AIEIKIGQSA KAGMGGHLPA EKVTQELSEI RGFPEGTDIV SPAHFDDIRN KDDLKAKVKW
LRETSGGKPI GIKVAAGNIE ADLEVAVYAE PDFITIDGRP GATAAALKFV KNSTSIPTIF
ALYRARKFLD EKGIKDISLI ITGGLRVSSD FAKALALGAD AIAIGTAALM ACACQQYRQC
DTGKCPVGVT TQDPELRARL KIDISAKKLE NFLRVSTQEL ENFARLTGND DVHKLSINDL
CTTNSEISNH TQIEHV
//