ID A5N992_CLOK5 Unreviewed; 447 AA.
AC A5N992;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDK33873.1};
GN OrderedLocusNames=CKL_1831 {ECO:0000313|EMBL:EDK33873.1};
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:EDK33873.1, ECO:0000313|Proteomes:UP000002411};
RN [1] {ECO:0000313|EMBL:EDK33873.1, 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};
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic
CC sulfatase-maturating enzyme family. {ECO:0000256|ARBA:ARBA00023601}.
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DR EMBL; CP000673; EDK33873.1; -; Genomic_DNA.
DR RefSeq; WP_012102228.1; NC_009706.1.
DR AlphaFoldDB; A5N992; -.
DR STRING; 431943.CKL_1831; -.
DR KEGG; ckl:CKL_1831; -.
DR eggNOG; COG0641; Bacteria.
DR HOGENOM; CLU_009273_3_0_9; -.
DR Proteomes; UP000002411; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR026412; rSAM_Cxxx_rpt.
DR InterPro; IPR023867; Sulphatase_maturase_rSAM.
DR NCBIfam; TIGR04115; rSAM_Cxxx_rpt; 1.
DR PANTHER; PTHR43273; ANAEROBIC SULFATASE-MATURATING ENZYME HOMOLOG ASLB-RELATED; 1.
DR PANTHER; PTHR43273:SF8; RADICAL SAM PROTEIN-RELATED; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF13186; SPASM; 1.
DR SFLD; SFLDG01072; dehydrogenase_like; 1.
DR SFLD; SFLDG01384; thioether_bond_formation_requi; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
PE 3: Inferred from homology;
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 58..226
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|Pfam:PF04055"
FT DOMAIN 305..378
FT /note="4Fe4S-binding SPASM"
FT /evidence="ECO:0000259|Pfam:PF13186"
SQ SEQUENCE 447 AA; 51805 MW; 73D7E1471E811034 CRC64;
MIKPKNGYYL DRRDFEQWQD SISPLIESYE KCNGICNDCE TYKDTKNPDL KVKNITFVVT
EKCNLNCSYC YEQHKTGRRM SKSVAKKAID FLFNEEKING YYSFKTSPAV ILEFIGGEPL
LEIDLMDYIV EYFKFRAFQL DSPWATNYMI SMTTNGVLYD SPEVQEFLKK NLGKVSLGIT
IDGNKKLHDT CRKFYDGSGS YDIVEKSIKD AVRKGYTNST KITLSPQNVM YLNEAIQNVW
NLGIKAAYTN CVFEEGWQIK DAKILYSQMK QLADFLLKDK NYSKYYCSLF DDSIGQPLKE
DRNWCGGNGQ MLAIAPDGKC FPCIRFMKYS LNNQKEQPIG DIYKGLDRKE ENMWLNKLKD
ITMSSQCQYE DNKKCLDCKI ASGCALCTGY NYDKFGDPNH KATFICEMHK ARVLANVYYW
NKLYQKLNLN KIFKSNIPKK KVNSYGM
//
