ID D7GQL8_9FIRM Unreviewed; 708 AA.
AC D7GQL8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Anaerobic ribonucleoside-triphosphate reductase {ECO:0000313|EMBL:CBL40093.1};
DE EC=1.17.4.2 {ECO:0000313|EMBL:CBL40093.1};
GN ORFNames=CK3_02300 {ECO:0000313|EMBL:CBL40093.1};
OS butyrate-producing bacterium SS3/4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=245014 {ECO:0000313|EMBL:CBL40093.1, ECO:0000313|Proteomes:UP000008961};
RN [1] {ECO:0000313|EMBL:CBL40093.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL40093.1,
RC ECO:0000313|Proteomes:UP000008961};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Clostridiales sp. SS3/4.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL40093.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL40093.1,
RC ECO:0000313|Proteomes:UP000008961};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FP929062; CBL40093.1; -; Genomic_DNA.
DR AlphaFoldDB; D7GQL8; -.
DR KEGG; bprs:CK3_02300; -.
DR PATRIC; fig|245014.3.peg.501; -.
DR HOGENOM; CLU_002707_2_0_9; -.
DR BioCyc; BBAC245014:G1314-192-MONOMER; -.
DR Proteomes; UP000008961; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR012833; NrdD.
DR NCBIfam; TIGR02487; NrdD; 1.
DR PANTHER; PTHR21075; ANAEROBIC RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR21075:SF0; ANAEROBIC RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE; 1.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF13597; NRDD; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492}; Oxidoreductase {ECO:0000313|EMBL:CBL40093.1}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 708 AA; 80864 MW; 9EF2E3A51EBF9055 CRC64;
MNVIKKDGTI EQFDGQKIVN AVSKSAARAM IELDDTQYHE IVSKVMAIVT ERFPEQVHVA
DMHNIVEQVL DEVNPKIAKS YRDYRNFKKD FVHIMDEVYQ KSQSIRFLGD KENANTDSTL
VATKRCLIFN ELNKRLYRKF FMTNDELQAC KDGYIYIHDQ SARLDTMNCC LCDISSIMSG
GFEMGNVWYN EPKTLDTAFD VLGDIILATA SQQYGGFTVP EVDRILAPYA EKSYKKYCAE
YMEIRNQQTF TQDVKDWAMS KVQRDYEQGF QGIEMKLNTV GSSRGDYPFI TMTFGLATDV
FGKMASKTFL KVHMEGEGKP GFKKPVLFPK LVFLYDENLH GEGGFNEDVF EAGIDCSSKT
MYPDWLSLTG DGYVAEMYKK YGRVISPMGC RAFLSPWFER GGMKPADADD KPVFVGRFNI
GAVSLHLPMI LAKARAESRD FYEVLDYYLE MIRGVHKRTY EYLGEMKAST NPIMYCEGGV
YGGRLKPSEK IKPLLKPMTA SFGITALNEL QRLYNGKSIA EDGEFALEVM QHINQKVTEF
KNEDGWLYAI YGTPAESLCG LQIEQFRKKY GIIENVSDRP YVSNSFHCHV TEDLTPIEKQ
DLEGRFWNMF NGGKIQYVRY PISYNREAVK TLVRRAMQLG FYEGVNLSLA YCDDCGHQEL
EMDVCPVCGS TNLTKIDRMN GYLSYSRVHG DTRLNAAKMA EIAERRSM
//