ID M9SLF2_METAX Unreviewed; 472 AA.
AC M9SLF2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Archaeal glutamate synthase [NADPH] {ECO:0000256|PIRNR:PIRNR006429};
DE EC=1.4.1.13 {ECO:0000256|PIRNR:PIRNR006429};
GN ORFNames=MMALV_15450 {ECO:0000313|EMBL:AGI86267.1};
OS Methanomethylophilus alvi (strain Mx1201).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata;
OC Methanomassiliicoccales; Methanomethylophilaceae; Methanomethylophilus.
OX NCBI_TaxID=1236689 {ECO:0000313|EMBL:AGI86267.1, ECO:0000313|Proteomes:UP000012672};
RN [1] {ECO:0000313|EMBL:AGI86267.1, ECO:0000313|Proteomes:UP000012672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mx1201 {ECO:0000313|EMBL:AGI86267.1,
RC ECO:0000313|Proteomes:UP000012672};
RX PubMed=23209209; DOI=10.1128/JB.01867-12;
RA Borrel G., Harris H.M., Tottey W., Mihajlovski A., Parisot N.,
RA Peyretaillade E., Peyret P., Gribaldo S., O'Toole P.W., Brugere J.F.;
RT "Genome sequence of 'Candidatus Methanomethylophilus alvus' Mx1201, a
RT methanogenic archaeon from the human gut belonging to a seventh order of
RT methanogens.";
RL J. Bacteriol. 194:6944-6945(2012).
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|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; CP004049; AGI86267.1; -; Genomic_DNA.
DR RefSeq; WP_015505413.1; NC_020913.1.
DR AlphaFoldDB; M9SLF2; -.
DR STRING; 1236689.MMALV_15450; -.
DR GeneID; 41322296; -.
DR KEGG; max:MMALV_15450; -.
DR eggNOG; arCOG00619; Archaea.
DR eggNOG; arCOG04391; Archaea.
DR HOGENOM; CLU_023342_0_1_2; -.
DR InParanoid; M9SLF2; -.
DR OrthoDB; 57305at2157; -.
DR Proteomes; UP000012672; 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:SF1; ARCHAEAL GLUTAMATE SYNTHASE [NADPH]; 1.
DR PANTHER; PTHR43819; 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 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:AGI86267.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000012672};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..44
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50903"
SQ SEQUENCE 472 AA; 50653 MW; CF7A4C1D9F40D9AC CRC64;
MAKYVCTVCG EIYDEEREGV RFEDLPDDWV CPLCRSPKSA FVLMGAEAPV TESGPAEEGP
SSVADVSDIG YDPKLVRHDG GPMDEIHAMA VTGKSVGEAM DTLLPVPKFD DILILGGQLA
HPPKDDGADV SIRTVIGKKA EHPMVLESPV YISHMSFGAL SGRAKIALAK GATMAGTAMC
SGEGGALYDE MIASDNYIFE YVPNKYSMYD ETFERCAAVE IKIGQGTKPG MGGHLPGAKV
NHVISVMREK PEGKDVLSPS RFPEIGSPKD LKEMVSMLRK RSGGKPIGVK IAAGHIEEDL
EFISKSGCDF ITIDGRGGAT GSSPKYLKDA SSVPTVYALS RARKYMDEHG MKQELVITGG
LRTSKDFVKA IAMGADAVAV ASSALIALGC QRYRACNSGM CPMGIATQDP ELEKRLDIDV
GAQRVANYLN VTAEELRSFT RISGHDDVHE LSLDDLCTTD PEIERITGIR HA
//
