ID F6B2M4_DESCC Unreviewed; 709 AA.
AC F6B2M4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Glutamate synthase (NADPH) {ECO:0000313|EMBL:AEF93853.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:AEF93853.1};
GN OrderedLocusNames=Desca_0979 {ECO:0000313|EMBL:AEF93853.1};
OS Desulfotomaculum nigrificans (strain DSM 14880 / VKM B-2319 / CO-1-SRB)
OS (Desulfotomaculum carboxydivorans).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=868595 {ECO:0000313|EMBL:AEF93853.1, ECO:0000313|Proteomes:UP000009226};
RN [1] {ECO:0000313|Proteomes:UP000009226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14880 / VKM B-2319 / CO-1-SRB
RC {ECO:0000313|Proteomes:UP000009226};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Stams A., Plugge C., Muyzer G.,
RA Kuever J., Parshina S., Ivanova A., Nazina T., Woyke T.;
RT "Complete sequence of Desulfotomaculum carboxydivorans CO-1-SRB.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP002736; AEF93853.1; -; Genomic_DNA.
DR RefSeq; WP_013809955.1; NC_015565.1.
DR AlphaFoldDB; F6B2M4; -.
DR STRING; 868595.Desca_0979; -.
DR KEGG; dca:Desca_0979; -.
DR eggNOG; COG0493; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_3_4_9; -.
DR Proteomes; UP000009226; 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 Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF140490; Nqo1C-terminal domain-like; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AEF93853.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009226}.
FT DOMAIN 615..646
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 709 AA; 76531 MW; 1DA13417B53970ED CRC64;
MTGNDCKVKQ TANLINAFLT AENYCSVCRR HFKQILDHLA RIQTGSGSRP DLLEIRDLAS
KVTGLCQCGG GKSVAEQVMA NLQAFRDEFI IHIENHVCPA GECPQLVLAP CQAACPAGLD
IPNYVALVGM QQYEEALARI REDVPLPGSL GRICEHPCER ACRRGQVDKP ISICALKGLA
YDKSNQQPGD LLAPPARKFK ERVAVIGAGP AGLSAAYFLA QRGYGVTIFE AMPEPGGMLA
YGIPPYRLPR QVLRDEIARI KALGVEIKVN TPVSNIQALK KEGFDAIFLG TGAWQGSIPI
ANDEEFKGVF DGVTFLRTVN QQLLQNNGTP EIDLTGKQVV VVGGGNVAID AARVSLRLGA
EEVKIIYRRT REEMPALVEE IVDAEHEGVK FDFLVSPVGL GGQNGWVAYI ECLKNELSEP
DASGRRKPVP IAGSAYRIAA DVVIFATGQQ PDLSILHGTG AEVARNRIVV NPLTLETSLP
GVFAGGDAVT GPASAIKAMA AGKQAAASIH AFLRGEVPTA SIKFPVKRPS IPPRKITAEQ
KAQASQVNFH ELYMAEKKDS FAEIMQGISE AAAMAEANRC LRCDLCIACG QCVDSCHNRI
GAAALQLGYI KDAHGETDFA RPGDKCIGCG TCSVNCPTGA ITQEDRNGFR EMRMCGSLMS
RLELVNCQVC GQPFATEKHL DYINSKDKQV CPACSRQVWS RNVYGRWRQ
//