ID A0A0M0C1P1_9ARCH Unreviewed; 503 AA.
AC A0A0M0C1P1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Archaeal glutamate synthase [NADPH] {ECO:0000256|PIRNR:PIRNR006429};
DE EC=1.4.1.13 {ECO:0000256|PIRNR:PIRNR006429};
GN ORFNames=AC479_01285 {ECO:0000313|EMBL:KON34306.1};
OS miscellaneous Crenarchaeota group-6 archaeon AD8-1.
OC Archaea; Candidatus Bathyarchaeota; Candidatus Bathyarchaeia.
OX NCBI_TaxID=1685126 {ECO:0000313|EMBL:KON34306.1, ECO:0000313|Proteomes:UP000037259};
RN [1] {ECO:0000313|EMBL:KON34306.1, ECO:0000313|Proteomes:UP000037259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD8-1 {ECO:0000313|EMBL:KON34306.1};
RA Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., Hinrichs K.-U.,
RA Teske A.P.;
RT "New insights into the roles of widespread benthic archaea in carbon and
RT nitrogen cycling.";
RL Submitted (JUN-2015) 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 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}.
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:KON34306.1}.
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DR EMBL; LFWW01000003; KON34306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0C1P1; -.
DR STRING; 1685126.AC479_01285; -.
DR PATRIC; fig|1685126.3.peg.1439; -.
DR Proteomes; UP000037259; Unassembled WGS sequence.
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; PF12838; Fer4_7; 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}.
FT DOMAIN 9..38
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 40..69
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
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 28
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
SQ SEQUENCE 503 AA; 54610 MW; 7A086D0D7914858B CRC64;
MKTYSLPEYV IDRDQDRCIR CKVCVNQCTY DTHYYDEEDD LIRSSEENCV NCQRCVTFCP
TNAITIIKNP NKSRSNVNWT QEAIGDLKKQ AESGVVVLTG MGCDKPHLTY WDRLLLNASQ
VTNPSIDPLR EPMEIRTYLG SKQDRLEIDL KDNKFNLKTK LSPQLLLETP IMFSAMSYGA
ISLNVHEALA RAAVECGTYF NTGEGGLDKR LYKYGKNAIV QVASGRFGVH SEYLSSGAAI
EIKIGQGAKP GIGGHLPGEK VTKHVAKTRM IPIGTDALSP APQHDIYSIE DLRQLIFALK
EATNYKKPIS VKIAAVHNSP AIASGMVRAG ADIIALDGVR GSTGAAPKVI RDNVGIPIEL
AIAKVDQRLR DEKIRNQASI VAAGGIKSSA DVIKAIALGA DAAYIGTAAL VAVGCTICQR
CYTGKCPWGI ATSDSWISKR INPDIATERL VNLLTSWSLE IKDIMGGMGI NAIESLRGNR
LALRGVGLTD TELKILGVKM AGD
//
