ID A0A1X7MVS3_9LACT Unreviewed; 732 AA.
AC A0A1X7MVS3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN ORFNames=SAMN04488700_0875 {ECO:0000313|EMBL:SMH28240.1};
OS Carnobacterium iners.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1073423 {ECO:0000313|EMBL:SMH28240.1, ECO:0000313|Proteomes:UP000193435};
RN [1] {ECO:0000313|EMBL:SMH28240.1, ECO:0000313|Proteomes:UP000193435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG26642 {ECO:0000313|EMBL:SMH28240.1,
RC ECO:0000313|Proteomes:UP000193435};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
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:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
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DR EMBL; FXBJ01000002; SMH28240.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7MVS3; -.
DR STRING; 1073423.SAMN04488700_0875; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000193435; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd01679; RNR_I; 1.
DR Gene3D; 1.10.1650.20; -; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR026459; RNR_1b_NrdE.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013554; RNR_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR NCBIfam; TIGR04170; RNR_1b_NrdE; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR Pfam; PF08343; RNR_N; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000193435}.
FT DOMAIN 569..591
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
FT COILED 338..365
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 732 AA; 83037 MW; FBCF66FE88C02C36 CRC64;
MLNQKKLIKS PETYFYLNNL VNIPVNGEIP LHRDQEALKA YFEEEIIPNT LLFDSLEEKL
TFMIENNYID VAILNLYTQA KNNEYDNAFI KSLFKKIYAA NFKFKSFMGA YKFYSQYALK
TNDNLKYLER FEDRVAFNAL YLGNGDKQLA MQLAEELISQ RYQPATPTFL NAGKKKRGEM
ISCFLIDIGD SMLSIGRGVN SALQLSRIGG GVGVNLSNIR SAGDPIKGIL NASSGVLPVM
KLLEDSFSYS NQLGQRNGAG VVYLNVFHPD ILGFLSTKKE NADEKIRVKT LSLGLVVPDK
YYELIKTNKP MYLFSPYSVE KEYGVPFSYV DLTAEYDNMV ANSAIKKTQV NARELEQEIS
RLQQESGYPY ILNIDTANKT NPVDGKIIMS NLCSEILQPQ EPSKLNNDLS YEQTGTDISC
NLGSSNIMNM MKSPDFAKSV NLAVRALTTV TDLSDVLEVP TVSKGNSFYH TIGLGAMGLH
TALSLYEIEY GSKESFEFTE AYFIALNYHS LVASNEIAKE REEVFFKFEK SNYADGSYFE
TYLKSEFVIK NEKVKEIFSA IQLPTVADWE NLKDAVIEYG LYHRNRLAVA PNGSISYINE
TSASLHPITQ LIENRQEKTV GSIFYPAPFL SNKTLKYYNS AYDYDQRKII DVYAVAQKHI
DQGMSLTLFM RSKLPEGLYE WKAGASPKLT TRDLNRLRNY AWTKGIKSLY YIRTYTEDDE
FIMANTCESC MI
//
