ID A3CSB6_METMJ Unreviewed; 505 AA.
AC A3CSB6;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Archaeal glutamate synthase [NADPH] {ECO:0000256|PIRNR:PIRNR006429};
DE EC=1.4.1.13 {ECO:0000256|PIRNR:PIRNR006429};
GN OrderedLocusNames=Memar_0333 {ECO:0000313|EMBL:ABN56266.1};
OS Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=368407 {ECO:0000313|EMBL:ABN56266.1, ECO:0000313|Proteomes:UP000002146};
RN [1] {ECO:0000313|EMBL:ABN56266.1, ECO:0000313|Proteomes:UP000002146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35101 / DSM 1498 / JR1
RC {ECO:0000313|Proteomes:UP000002146};
RX PubMed=21304656; DOI=10.4056/sigs.32535;
RA Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT type strain JR1.";
RL Stand. Genomic Sci. 1:189-196(2009).
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 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; CP000562; ABN56266.1; -; Genomic_DNA.
DR RefSeq; WP_011843176.1; NC_009051.1.
DR AlphaFoldDB; A3CSB6; -.
DR STRING; 368407.Memar_0333; -.
DR GeneID; 76730900; -.
DR KEGG; mem:Memar_0333; -.
DR eggNOG; arCOG00619; Archaea.
DR HOGENOM; CLU_023342_1_1_2; -.
DR OrthoDB; 2837at2157; -.
DR Proteomes; UP000002146; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR024188; GltB.
DR InterPro; IPR043578; GltB_archl_type.
DR InterPro; IPR002932; Glu_synthdom.
DR PANTHER; PTHR43819:SF1; ARCHAEAL GLUTAMATE SYNTHASE [NADPH]; 1.
DR PANTHER; PTHR43819; ARCHAEAL-TYPE GLUTAMATE SYNTHASE [NADPH]; 1.
DR Pfam; PF13187; Fer4_9; 1.
DR Pfam; PF01645; Glu_synthase; 1.
DR PIRSF; PIRSF500061; GOGAT_lg2_archl; 1.
DR PIRSF; PIRSF006429; GOGAT_lg_2; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|PIRSR:PIRSR006429-1};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR006429};
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR006429};
KW FMN {ECO:0000256|PIRNR:PIRNR006429};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164,
KW ECO:0000256|PIRNR:PIRNR006429}; Iron {ECO:0000256|PIRSR:PIRSR006429-1};
KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR006429-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR006429-1};
KW NADP {ECO:0000256|PIRNR:PIRNR006429};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR006429,
KW ECO:0000313|EMBL:ABN56266.1}.
FT DOMAIN 12..41
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 42..70
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 24
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 27
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 31
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 60
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
SQ SEQUENCE 505 AA; 54809 MW; DFF1458B17A0508E CRC64;
MSSNFGSMPL RYRISIDREQ CMECGRCVEN CSYGVFRWDG NRILINSRNC TACHRCLTYC
PRDAIMLQEH PCDYRSHPVW TRSVRESIYN QARTGKIILA GMGSVSNLPI IFDHLMLDAC
QVTTPPTDPL REPVELRTYL GKKPSKLEFR QKPNGDVELS TELTPNLMLE TPIMLGHMSY
GALSLNAHVA MARAAKETGT FMGTGEGGLH PGLYPYQDRM IVQVASGRFG VNIDYLERGA
AIELKLGQGA KPGIGGHLPG EKVSADVSRT RMIPEGSDAI SPAPHHDIYG IEDLPQLVNS
VKEATERKKP IFAKIAAVNN NAENVAAVAR SGVDAIAIDG FRGGTGAAPR VFRDHVGIPI
EVAIATADRE LRKQGLRNEV SLIACGSIRE STDVVKAIAL GADAVYIATA ALAAMGCRVC
GNCYQGLCPW GIATQRPDLV ARLDPDVASK QVANLIHAWT LEITELMGAA GINSIESLRG
NRDRLRGYML DEGLLEILDV KSVGA
//
