ID A0A251WV51_9RHOB Unreviewed; 712 AA.
AC A0A251WV51;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=BVC71_15090 {ECO:0000313|EMBL:OUD08131.1};
OS Marivivens niveibacter.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Marivivens group; Marivivens.
OX NCBI_TaxID=1930667 {ECO:0000313|EMBL:OUD08131.1, ECO:0000313|Proteomes:UP000194664};
RN [1] {ECO:0000313|EMBL:OUD08131.1, ECO:0000313|Proteomes:UP000194664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A06712 {ECO:0000313|EMBL:OUD08131.1};
RA Hu D., Wang L., Shao Z.;
RT "The draft genome sequence of HSLHS2.";
RL Submitted (DEC-2016) 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}.
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:OUD08131.1}.
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DR EMBL; MSPP01000008; OUD08131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251WV51; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000194664; 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 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:UP000194664}.
FT DOMAIN 564..586
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 712 AA; 80588 MW; 92B6324344F78424 CRC64;
MLDHGMKDGE TLDYHALNAM LNLYDENGHI RFEADRMAAR QYFLQHVNQN TVFFHSLDEK
LRYLVEEGYY EAEVLSQYPR EFLTQIWDAA YAAKFRFPTF LGAFKYYTSY TLKTRDGQRY
LERFEDRVVM VSLALARGNQ EHAMAFMREI IAGRFQPATP TFLNAGKKSR GELISCFLLR
LEDNMESIGR GINSALQLSK RGGGVALMLT NIREHGAPIK GIENQSSGVI PVMKLLEDSF
SYANQLGARQ GAGAVYLNAH HPDILRFLDT KRENADEKIR IKTLSLGVVI PDITFELAKK
NEDMYLFSPH DIEKVYGVPF SEISVTEKYD EMVDDKRIRK KKINAREFFQ TLAEIQFESG
YPYIMFEDTV NKANPIDGRI TMSNLCSEIL QVNEASKFND DLSYDHLGTD ISCNLGSLNI
AKTMDSPDFG ATVETAVRAL TAVSEMSAID SVPSIRRGND EAHAIGLGQM NLHGFLARER
VHYGSAEGVD FTSVYFAAIT YHAIRASNQI SIEKGETFVG FDKSTYATGE FFDKYTDRDW
LPETEEIQAL FDRMNVTLPT RDDWAALKKS VMEHGLYNRN LQAVPPTGSI SYINNSTSSI
HPIVSKVEIR KEGKIGRVYY PAAFMSNDNL EYYRDAYEIG PEALIDTYAA ATEHVDQGLS
LTLFFPAEAT TRDINRAQIY AWKKGIKTIY YVRLRQSSLE GTEVQGCVSC TL
//
