AGLUS_DEHM1
ID AGLUS_DEHM1 Reviewed; 500 AA.
AC Q3Z7F6;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Archaeal-type glutamate synthase [NADPH] {ECO:0000303|PubMed:11230537, ECO:0000312|EMBL:AAW39579.1};
DE EC=1.4.1.13 {ECO:0000250|UniProtKB:Q58746};
DE AltName: Full=Archaeal-type NADPH-GOGAT {ECO:0000250|UniProtKB:Q58746};
GN Name=gltB {ECO:0000303|PubMed:11230537}; OrderedLocusNames=DET1128;
OS Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS (Dehalococcoides ethenogenes (strain 195)).
OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=243164;
RN [1] {ECO:0000312|EMBL:AAW39579.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX PubMed=15637277; DOI=10.1126/science.1102226;
RA Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA Zinder S.H., Heidelberg J.F.;
RT "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT ethenogenes.";
RL Science 307:105-108(2005).
RN [2] {ECO:0000305}
RP PHYLOGENETIC STUDY.
RX PubMed=11230537; DOI=10.1093/oxfordjournals.molbev.a003812;
RA Nesbo C.L., L'Haridon S., Stetter K.O., Doolittle W.F.;
RT "Phylogenetic analyses of two 'archaeal' genes in thermotoga maritima
RT reveal multiple transfers between archaea and bacteria.";
RL Mol. Biol. Evol. 18:362-375(2001).
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:0000250|UniProtKB:Q58746};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q58746};
CC -!- SIMILARITY: Belongs to the glutamate synthase family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000027; AAW39579.1; -; Genomic_DNA.
DR RefSeq; WP_010936821.1; NC_002936.3.
DR AlphaFoldDB; Q3Z7F6; -.
DR SMR; Q3Z7F6; -.
DR STRING; 243164.DET1128; -.
DR EnsemblBacteria; AAW39579; AAW39579; DET1128.
DR KEGG; det:DET1128; -.
DR PATRIC; fig|243164.10.peg.1060; -.
DR eggNOG; COG0069; Bacteria.
DR HOGENOM; CLU_023342_1_1_0; -.
DR OMA; CAWGIAT; -.
DR OrthoDB; 151647at2; -.
DR Proteomes; UP000008289; 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; 3.20.20.70; -; 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 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 PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S; Amino-acid biosynthesis; Flavoprotein; FMN; Glutamate biosynthesis;
KW Iron; Iron-sulfur; Metal-binding; NADP; Oxidoreductase; Reference proteome;
KW Repeat.
FT CHAIN 1..500
FT /note="Archaeal-type glutamate synthase [NADPH]"
FT /id="PRO_0000420607"
FT DOMAIN 7..38
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 40..69
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 24
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 28
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
SQ SEQUENCE 500 AA; 54048 MW; 9E61793CB3DE62EF CRC64;
MKTFLPSKFI VDRIEDRCIK CKVCITQCSF DTHYYDEDDD QIKVRNQNCV GCHRCVTFCP
TNALVVRNNP LEYRQNANWT PEMIEDIFKQ AETGGVLLTG MGMDKAKPIY WDKLLINASQ
VTNPSIDPLR EPMELTTYLG RRPDKAAFDN CGNVEENITP LVKIDVPVMF SAMSYGAISL
NVHRSLAQAA KNMGTMWNTG EGGLHSSLME FKDNTIVQVA SGRYGVQNDY LNSGRIVEIK
IGQGAKPGIG GHLPGEKVSA DVSLTRMIPM GTDAISPAPQ HDIYSIEDLS QLIYALKEAT
HYRVPISVKI AAVHNVSAIA SGIVRAGADI VTIDGMRGAT GAAPKVIRDN VGIPIELALA
AVDSRLREEG IRNQASLVIS GGIRNSGDVF KAIALGADAV NIGTAALVAL GCHLCQQCHT
GKCAWGICTS DLALTKRINP EIGAKRLTNL LRGWSLEIKD MLGGLGVNAI ESLRGNRLHL
RGVGLSAEEL KILGVRAAGE
