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Database: UniProt
Entry: E6W1X5_DESIS
LinkDB: E6W1X5_DESIS
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ID   E6W1X5_DESIS            Unreviewed;       546 AA.
AC   E6W1X5;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=glutamate synthase (NADPH) {ECO:0000256|ARBA:ARBA00012079};
DE            EC=1.4.1.13 {ECO:0000256|ARBA:ARBA00012079};
GN   OrderedLocusNames=Selin_0764 {ECO:0000313|EMBL:ADU65507.1};
OS   Desulfurispirillum indicum (strain ATCC BAA-1389 / DSM 22839 / S5).
OC   Bacteria; Chrysiogenota; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae;
OC   Desulfurispirillum.
OX   NCBI_TaxID=653733 {ECO:0000313|EMBL:ADU65507.1, ECO:0000313|Proteomes:UP000002572};
RN   [1] {ECO:0000313|EMBL:ADU65507.1, ECO:0000313|Proteomes:UP000002572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1389 / DSM 22839 / S5
RC   {ECO:0000313|Proteomes:UP000002572};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Haggblom M., Rauschenbach I.,
RA   Bini E., Woyke T.;
RT   "Complete sequence of Desulfurispirillum indicum S5.";
RL   Submitted (DEC-2010) 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   -!- SIMILARITY: Belongs to the glutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00009716, ECO:0000256|PIRNR:PIRNR006429}.
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DR   EMBL; CP002432; ADU65507.1; -; Genomic_DNA.
DR   RefSeq; WP_013505395.1; NC_014836.1.
DR   AlphaFoldDB; E6W1X5; -.
DR   STRING; 653733.Selin_0764; -.
DR   KEGG; din:Selin_0764; -.
DR   eggNOG; COG0069; Bacteria.
DR   eggNOG; COG1145; Bacteria.
DR   HOGENOM; CLU_494121_0_0_0; -.
DR   InParanoid; E6W1X5; -.
DR   OrthoDB; 9758182at2; -.
DR   Proteomes; UP000002572; 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:InterPro.
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; IPR002932; Glu_synthdom.
DR   PANTHER; PTHR43819:SF1; ARCHAEAL GLUTAMATE SYNTHASE [NADPH]; 1.
DR   PANTHER; PTHR43819; ARCHAEAL-TYPE GLUTAMATE SYNTHASE [NADPH]; 1.
DR   Pfam; PF13484; Fer4_16; 1.
DR   Pfam; PF01645; Glu_synthase; 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; 2.
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   Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR006429-1};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR006429-
KW   1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR006429-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002572}.
FT   DOMAIN          16..45
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          69..99
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   BINDING         79
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT   BINDING         82
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT   BINDING         85
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT   BINDING         89
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
SQ   SEQUENCE   546 AA;  59484 MW;  63B743E370A176B3 CRC64;
     MATMRVNAIA RDDLFWRINY KHDRCTMCGK CLASCPFRAI EAGVEKRRRV ISDHLTPKPK
     VLFQTVPVIR QVLNHHEACR GCGICEKVCP NEAIAPYFNK DNRLAIKYRS ATADAYKRGG
     RSNLNPMGST LDKITVGRIS QMTDPSLDAQ RHTFDILAPL GRVLPPQSLP LSIKEGRLDI
     TRPLPPLNWM YPIIIGDMSI GALSTRMWEA LSIATAYLNE EAGIPIRMCT GEGGIPGRLL
     RSRYVRYMIL QIASGHFGWN RIVNAMPRMQ DDPAGVLIKI GQGAKPGDGG MLQAKKVARH
     IQEIRGVPKT DLLSPPNHQG LYSIEESVQK MFLSFNSAFQ FRVPVAIKVA ASATSVSVYN
     NLLRDPYNIV GGFFLDGISG GTGAAQDISL DHTGHPIVSK LRDCYLAAVH QGKQGQIPLW
     AGGGMGQGWN LAADAFKMIC LGANGVFTGK LMLQLAGCVG LDNGKCNACN TGLCPVGICT
     QNPILEKRLD IDRVAEGIVN YFIATDQELK KLMAPIGNSS LPVGRSDALI STDTAVAEKL
     NIPYSC
//
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