ID A5N548_CLOK5 Unreviewed; 392 AA.
AC A5N548;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Predicted Fe-S oxidoreductase {ECO:0000313|EMBL:EDK32429.1};
GN OrderedLocusNames=CKL_0375 {ECO:0000313|EMBL:EDK32429.1};
OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=431943 {ECO:0000313|EMBL:EDK32429.1, ECO:0000313|Proteomes:UP000002411};
RN [1] {ECO:0000313|EMBL:EDK32429.1, ECO:0000313|Proteomes:UP000002411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680
RC {ECO:0000313|Proteomes:UP000002411};
RX PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA Hagemeier C., Thauer R.K., Gottschalk G.;
RT "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT metabolic features.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP000673; EDK32429.1; -; Genomic_DNA.
DR RefSeq; WP_011988944.1; NC_009706.1.
DR AlphaFoldDB; A5N548; -.
DR STRING; 431943.CKL_0375; -.
DR KEGG; ckl:CKL_0375; -.
DR eggNOG; COG0535; Bacteria.
DR HOGENOM; CLU_009273_4_0_9; -.
DR Proteomes; UP000002411; 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 CDD; cd21123; SPASM_MftC-like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR InterPro; IPR034479; AhbC-like.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR023930; NirJ1.
DR InterPro; IPR017200; PqqE-like.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR04085; rSAM_more_4Fe4S; 1.
DR NCBIfam; TIGR04054; rSAM_NirJ1; 1.
DR PANTHER; PTHR11228:SF7; PQQA PEPTIDE CYCLASE; 1.
DR PANTHER; PTHR11228; RADICAL SAM DOMAIN PROTEIN; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF13186; SPASM; 1.
DR PIRSF; PIRSF037420; PQQ_syn_pqqE; 1.
DR SFLD; SFLDF00543; alternative_heme_biosynthesis; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
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:UP000002411};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 33..247
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 392 AA; 44279 MW; DCE9C4963A98BC0C CRC64;
MLGITKLLCE SENFGDRLRY ASGAGSEKSG AAKGKGPVVV WNCTNSCNLK CRHCYADSQN
KKFEEELDSK EAKYLIEDLA ELKVPVLLIS GGEPLMREDL FELLNYAKNY NIRSTISTNG
TLIDKRTAKD LKLNGVSYVG ISLDGIGTNH DKFRGVIGSF NKSLEGIRNC VEIGQKVGLR
FTINKSNYHQ LEDIFYLIKE EKIPRVCFYH LAYSGRGNAM AREDITFEQK RQALDIIMDR
AVRFGKDVEI LTVGNHADAV YLYLQVKKKY PHLRDRIWDL IQTNGGNRSG MALANIDFKG
HVHADQFTQQ HSFGNIRERK FSDIWKNPSN PLAVGLRNRK SLLKGRCSSC KWLNVCNGNL
RVRAEAATGD FWNSDPSCYL TDKEIGIFNI VK
//
