ID K6TVQ3_9CLOT Unreviewed; 697 AA.
AC K6TVQ3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, 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 ORFNames=A370_01555 {ECO:0000313|EMBL:EKQ56780.1};
OS Clostridium sp. Maddingley MBC34-26.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1196322 {ECO:0000313|EMBL:EKQ56780.1, ECO:0000313|Proteomes:UP000001325};
RN [1] {ECO:0000313|EMBL:EKQ56780.1, ECO:0000313|Proteomes:UP000001325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Maddingley MBC34-26 {ECO:0000313|Proteomes:UP000001325};
RX PubMed=23405323;
RA Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Bradbury M.I.,
RA Midgley D.J., Hendry P.;
RT "Draft Genome Sequence of Clostridium sp. Maddingley, Isolated from Coal-
RT Seam Gas Formation Water.";
RL Genome Announc. 1:E00081-12(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKQ56780.1}.
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DR EMBL; ALXI01000057; EKQ56780.1; -; Genomic_DNA.
DR AlphaFoldDB; K6TVQ3; -.
DR STRING; 1196322.A370_01555; -.
DR PATRIC; fig|1196322.3.peg.1514; -.
DR eggNOG; COG0209; Bacteria.
DR Proteomes; UP000001325; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
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; 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; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF17975; RNR_Alpha; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
PE 3: Inferred from homology;
KW 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000001325}.
FT DOMAIN 5..105
FT /note="Ribonucleotide reductase alpha helical"
FT /evidence="ECO:0000259|Pfam:PF17975"
FT DOMAIN 319..496
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 697 AA; 80308 MW; C565F3F7BB325118 CRC64;
MSEILSEAFL SKYKELENTP LSAIGEFVYL RTYSRYLDDK KRRENWFETV LRTTKYNIEL
GIDFKKKHGF HINLQDEIKE AELLFDNLFN LRTFTSGRTL YMGGTDIVKE YPLSNYNCSF
TMIEEFHDFV DIFYLLMVGS GVGVRIDKEL IIKMPKIRKI SVAGEYSEGV HKYMPKEYME
DTKLILDKDE PSTATIKIGD SKEGWCNALE TYFKLVTLPE YINIKKVVFD YSYVRPEGER
LKRFGGRASG HKSLKRMFEK INKVCSNLID GSLKSIDVLD IATIISENVV SGGVRRSAMM
IICDEDDKDV INAKSNLYKI VSGNWIENLE VSHRKMSNNS VLYKERPSLD KIKQILNSIK
INGEPGFING AEAKKRKRTF KGCNPCGEIL LNSHQCCNLS TNNLVSFVDK DNELDVKHLE
EVLKLSTRVA IRMTLVNVEL PNWNEVMQSD RIVGISLTGM MDMLNKTNMD YNSLGKLLKH
LREVVRNEGT RYSNELGISA PELMTTIKPE GSLSTLPCVS SGIHYSHSNY YIRRVRISVS
DPLYKMIEKL KCYPIFNENG QNDENCTTKV IEFPIKAPEG KTKYDVGAIE QLELYKLSMM
NWTDHNTSIT VHVKDDEWDD VADWLYNNFD YVVGITFLPL MDETYPLLPY ESISREEYEK
RLKNIKPIDY ELLAELDDDE EHEIIDKECA NGVCPVR
//
