ID A0A0D8I6Z2_9CLOT Unreviewed; 784 AA.
AC A0A0D8I6Z2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase {ECO:0000256|ARBA:ARBA00021063};
DE EC=1.17.4.2 {ECO:0000256|ARBA:ARBA00012275};
GN Name=rtpR {ECO:0000313|EMBL:AKL97095.1};
GN ORFNames=CACET_c36640 {ECO:0000313|EMBL:AKL97095.1}, TZ02_15455
GN {ECO:0000313|EMBL:KJF26050.1};
OS Clostridium aceticum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=84022 {ECO:0000313|EMBL:AKL97095.1, ECO:0000313|Proteomes:UP000035704};
RN [1] {ECO:0000313|EMBL:AKL97095.1, ECO:0000313|Proteomes:UP000035704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1496 {ECO:0000313|EMBL:AKL97095.1,
RC ECO:0000313|Proteomes:UP000035704};
RA Poehlein A., Schiel-Bengelsdorf B., Gottschalk G., Duerre P., Daniel R.;
RT "Genome sequence of Clostridium aceticum DSM 1496.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KJF26050.1, ECO:0000313|Proteomes:UP000032372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1496 {ECO:0000313|EMBL:KJF26050.1,
RC ECO:0000313|Proteomes:UP000032372};
RA Song Y., Hwang S., Cho B.-K.;
RT "Draft genome sequence of Clostridium aceticum DSM 1496, a potential
RT butanol broducer through syngas fermentation.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC triphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC triphosphate; Xref=Rhea:RHEA:12701, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:61557, ChEBI:CHEBI:61560; EC=1.17.4.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001283};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
CC -!- SIMILARITY: Belongs to the class II ribonucleoside-triphosphate
CC reductase family. {ECO:0000256|ARBA:ARBA00005654}.
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DR EMBL; CP009687; AKL97095.1; -; Genomic_DNA.
DR EMBL; JYHU01000020; KJF26050.1; -; Genomic_DNA.
DR RefSeq; WP_044825893.1; NZ_JYHU01000020.1.
DR AlphaFoldDB; A0A0D8I6Z2; -.
DR STRING; 84022.CACET_c36640; -.
DR KEGG; cace:CACET_c36640; -.
DR PATRIC; fig|84022.5.peg.1779; -.
DR OrthoDB; 9763270at2; -.
DR Proteomes; UP000032372; Unassembled WGS sequence.
DR Proteomes; UP000035704; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:InterPro.
DR GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.20.70.20; -; 1.
DR Gene3D; 3.30.1620.10; b-12 dependent (class ii) ribonucleotide reductase, Chain A, Domain 2; 1.
DR Gene3D; 3.90.1390.10; b-12 dependent (class ii) ribonucleotide reductase, chain A, domain 3; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR040763; RNR_alpha_hel.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013345; RTP_Rdtase_AdoCbl-dep.
DR NCBIfam; TIGR02505; RTPR; 1.
DR PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF17975; RNR_Alpha; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492}; Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AKL97095.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000035704}.
FT DOMAIN 2..93
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 784 AA; 90339 MW; EC7E3F35F26ABAA7 CRC64;
MFKVKKRDGR MVDFDSSKII GAIKKAMGET TKGIDEDLSK KIADEIVGKI ENEESPLHVE
EIQDIVEDML MSSDRKDAAK RYIIYRNQRN RSRSVRNKEE NKLLTDAFIS SYKHRFSPMQ
QLGSFVYYRT YARWIPEESR REYWWETVKR AVEYNCSLVP TTRQEAEKLF DNVYNLKQFL
SGRTFWVGNT TVARSYPMAN YNCAFLVIDA FESFKDLFYL LMVGSGVGVR VLKKDVQALP
KVRTDYDIIH KDYAPIPKDL REDNTSLEFA HKNIVKITVG DSKEGWTQAL DFFFKLIYSH
EYRSIKTIII NYDHVRPKGE KLKTFGGTAS GHESLKNMFY KINKVITNSK KASISEKVKL
GAVDCLDIAN IIGENVVVGG VRRTAEMILI DPEDTVSIEA KSNLYKQIEG QWIVDQEIIH
RQMSNNSIYY ESKPSREKLH WLMEKMRYSG EPGWVNAEAG SKRRPSMKGV NPCGEILLDS
KGLCNLTTVN VFAFVQEDGV LDQEGLIEAQ RLSVRASYRM TCVELELPKW DEVQKRDKLL
GCSLTGWQDM VNATGMTKEE EIKLLKTLRN TAHKEAEVYA DAIGEKAPLL VTTIKPEGTL
SQLPTVSSGV HYSHSPYYIR RIRVSADDPL VKVCEELGYP VFPEVGQEWE TCSTKVVEFP
IKAPKGKTKY DVSAIQQLEN YKMFMEHYVD HNCSITVHTK EDEWHQVEEW VWNNWNDIVA
LSFLSLEDHF YKLLPYEAIE EEEYTKRAEA MKGFIPSLIT KYEKQEIETE ITSDDCETGV
CPIR
//
