ID A5N870_CLOK5 Unreviewed; 205 AA.
AC A5N870;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Predicted hydrolase {ECO:0000313|EMBL:EDK33501.1};
GN OrderedLocusNames=CKL_1459 {ECO:0000313|EMBL:EDK33501.1};
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:EDK33501.1, ECO:0000313|Proteomes:UP000002411};
RN [1] {ECO:0000313|EMBL:EDK33501.1, 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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR EMBL; CP000673; EDK33501.1; -; Genomic_DNA.
DR RefSeq; WP_012101851.1; NC_009706.1.
DR AlphaFoldDB; A5N870; -.
DR STRING; 431943.CKL_1459; -.
DR KEGG; ckl:CKL_1459; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_040940_5_2_9; -.
DR Proteomes; UP000002411; Chromosome.
DR GO; GO:0010945; F:coenzyme A diphosphatase activity; IEA:InterPro.
DR CDD; cd03426; CoAse; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR045121; CoAse.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR12992:SF11; MITOCHONDRIAL COENZYME A DIPHOSPHATASE NUDT8; 1.
DR PANTHER; PTHR12992; NUDIX HYDROLASE; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EDK33501.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002411}.
FT DOMAIN 20..152
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 205 AA; 24170 MW; C666CE431962832E CRC64;
MIKKIEDIFK ERKPHIMGEF SKSAVMIPLC ESGEEISVLF EMRALNLKHQ PGDICFPGGR
LEKGEIPVCA AVRETMEELN LSKEDIKLIG QMDYVVTPYN FIMYPFVCKL NREDIFPSQS
EVDHIFKVPL QFFIENKPLL YEIPIVSQPG KRFPYRLIRN GRKYKFRRGT VKQYFYNYEK
YTIWGFTALI IKRFVDIIVS NDHNK
//