ID A0A1W1WM15_SULTA Unreviewed; 840 AA.
AC A0A1W1WM15;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=SAMN00768000_3270 {ECO:0000313|EMBL:SMC07219.1};
OS Sulfobacillus thermosulfidooxidans (strain DSM 9293 / VKM B-1269 / AT-1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Clostridiales Family XVII. Incertae Sedis; Sulfobacillus.
OX NCBI_TaxID=929705 {ECO:0000313|EMBL:SMC07219.1, ECO:0000313|Proteomes:UP000192660};
RN [1] {ECO:0000313|Proteomes:UP000192660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9293 {ECO:0000313|Proteomes:UP000192660};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reduction of ribonucleotides to
CC deoxyribonucleotides. May function to provide a pool of
CC deoxyribonucleotide precursors for DNA repair during oxygen limitation
CC and/or for immediate growth after restoration of oxygen.
CC {ECO:0000256|RuleBase:RU364064}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000206,
CC ECO:0000256|RuleBase:RU364064};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922,
CC ECO:0000256|RuleBase:RU364064};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC family. {ECO:0000256|ARBA:ARBA00007405, ECO:0000256|RuleBase:RU364064}.
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DR EMBL; FWWY01000001; SMC07219.1; -; Genomic_DNA.
DR RefSeq; WP_020374806.1; NZ_FWWY01000001.1.
DR AlphaFoldDB; A0A1W1WM15; -.
DR STRING; 28034.BFX07_06695; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000192660; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR NCBIfam; TIGR02504; NrdJ_Z; 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; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|RuleBase:RU364064};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|RuleBase:RU364064};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634,
KW ECO:0000256|RuleBase:RU364064};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364064};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064};
KW Reference proteome {ECO:0000313|Proteomes:UP000192660}.
FT DOMAIN 87..141
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 147..628
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 782..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 840 AA; 94151 MW; BE4A976BB51A0177 CRC64;
MELSTGFSSE LSWKIFLDRY TLKDPNRNFQ VGDLAIALVE PHPKWPKKDV GIVREILPDG
HLSIELLTGP QKGDLIERRV VDCDRPIEKT IDEVARRIAR GVAKVEKPKV RQDVEDSFAK
EIAALHFVPG GRIWAGAGTD QKLTYFNCYV IPSPRDSREG IVETLGQMIE IMSRGGGVGI
NISSLRPARA AVRGVNGRSS GAVSWMDLYS RATGLVEQGG SRRGALMLQI EDWHPDIWRF
IDVKKTPGMV ENANISVRIS DSFMQAVKND DDWDLVFPDT TDPDYDTLWD GNLENWKKAD
KPIIVYETVK ARKIWNEIIK GAWQAAEPGI VFDERHEKDS NSWYFNPLIS TNPCAEQPLP
AWGVCTLGHI NLSAFYDRET NDVNWDGLRT TIRMGVRFLD DIVDATPYFF QQNYDNQQKE
RRIGLGTMGL GELLIRLGLR YGSPESLDFI DKLYKFIAVE SYLYDVELAK EKGPFPAFNA
ELYLQSGFIK RLPESVRQAI REHGVRNVTI LTQAPTGTVG TMVGTSTGIE PYYALTYFRQ
SRLGYDEQYV PVAAEWKEAH PGMELPSYFV GAMDLTPEEH VYVQAAIQRW TDSSISKTAN
APSTYTVEDT ARLYELAYDL GCKGVTIYRD QSRTEQVLHL SEESSPKNDA VNATTPENMP
PMADDVEVYP VPQLINGRTY RKETPAGTAR VVINEVDGNP FEVFMLLGRA GSEVQSFMES
LGRVISLYLR SNGNLTPRRR LELVAEQLKG IGGANQMGFG PGRVLSVVDA IGQLLESHLR
QRPGEEAAAI TSPSPNTRKT EERDNRHTSL HLDLCPQCDA PTLVYEEGCQ HCQSCGYSKC
//
