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Database: UniProt
Entry: A0A0E3SR88_METMT
LinkDB: A0A0E3SR88_METMT
Original site: A0A0E3SR88_METMT 
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
//
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