ID E1QJ31_DESB2 Unreviewed; 423 AA.
AC E1QJ31;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Radical SAM domain protein {ECO:0000313|EMBL:ADK85574.1};
GN OrderedLocusNames=Deba_2210 {ECO:0000313|EMBL:ADK85574.1};
OS Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS / 2st14).
OC Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC Desulfarculaceae; Desulfarculus.
OX NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK85574.1, ECO:0000313|Proteomes:UP000009047};
RN [1] {ECO:0000313|EMBL:ADK85574.1, ECO:0000313|Proteomes:UP000009047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC {ECO:0000313|Proteomes:UP000009047};
RX PubMed=21304732; DOI=10.4056/sigs.1243258;
RA Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL Stand. Genomic Sci. 3:276-284(2010).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP002085; ADK85574.1; -; Genomic_DNA.
DR RefSeq; WP_013259015.1; NC_014365.1.
DR AlphaFoldDB; E1QJ31; -.
DR STRING; 644282.Deba_2210; -.
DR KEGG; dbr:Deba_2210; -.
DR eggNOG; COG2896; Bacteria.
DR HOGENOM; CLU_645348_0_0_7; -.
DR OrthoDB; 9764628at2; -.
DR Proteomes; UP000009047; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR034457; Organic_radical-activating.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR30352:SF23; PYRUVATE FORMATE-LYASE 1-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR30352; PYRUVATE FORMATE-LYASE-ACTIVATING ENZYME; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SFLD; SFLDG01109; Uncharacterised_Radical_SAM_Su; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 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 Reference proteome {ECO:0000313|Proteomes:UP000009047};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 182..421
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 423 AA; 46516 MW; 9097C7B04490379A CRC64;
MSAPRLVYAD AEGKVFDHPE LAMAGSAAGR WQPVEAQDCI PLPEGSELFL LPGRLPVGVG
DDGKFEIVDE HPENPDEKVC AVAAFMAPAH TATLWAAYKT TPGAPNLPLF AYAAVGFMEN
DFVVTGLRID PLPRQDPGRF PPPERLQSAA RRLLRQYKQN RLWQHLGTCA MTYGCPAAKN
LVLGRWEAPL PTSPVCNADC VGCLSFQPDG VFPVTQERIK FTPSPEEVAE VALHHFRNKR
EALVSFGQGC EGEPLLQADL LSKAIRLIRL EEPLGTINLN TNGSRPDQVG RLMTDGLSSI
RVSVNSLIPE RHAAYYRPKG WSLAQAIDSL KAVKRAGGHA SLNLLTMPGL TDRPEEMDAL
CQVIEQTKLD LIQWRNINID PEIYLKALGL GQPKERLGVA AMIDELRRRF PGLKHGYFNP
KIG
//
