ID A0A323V0Y9_9RHOO Unreviewed; 950 AA.
AC A0A323V0Y9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=DNK49_02370 {ECO:0000313|EMBL:PZA18394.1};
OS Parazoarcus communis SWub3 = DSM 12120.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Parazoarcus.
OX NCBI_TaxID=1121029 {ECO:0000313|EMBL:PZA18394.1, ECO:0000313|Proteomes:UP000248259};
RN [1] {ECO:0000313|EMBL:PZA18394.1, ECO:0000313|Proteomes:UP000248259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWub3 {ECO:0000313|EMBL:PZA18394.1,
RC ECO:0000313|Proteomes:UP000248259};
RA Zorraquino Salvo V., Toubiana D., Blumwald E.;
RT "Azoarcus communis strain SWub3 genome.";
RL Submitted (JUN-2018) 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:PZA18394.1}.
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DR EMBL; QKOE01000001; PZA18394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A323V0Y9; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000248259; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 3.20.70.20; -; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF03477; ATP-cone; 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.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR PROSITE; PS51161; ATP_CONE; 2.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000248259}.
FT DOMAIN 13..113
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 130..218
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 950 AA; 105636 MW; 00474114F801773D CRC64;
MDRFPIDPTL AAFQVIRRNG AVVSFDPSKI GVAMTKAFLA VEGRQGAASA RIRDIVGKLT
DTVVQALTRR LPDGGMVHIE DIQDQVELAL MRSGEHDVAR AYVLYRERRS AERAAERAAH
TGDPTVTTVL HVIDGDHRRP LDVAGLQAMC REACAGLDDV SADTVLEHAM HNLYDGVPID
AVRQSLVLAA RTLIEREPNY GFVAARLLLA AIRVEVLGRE TSQTEMADPE RGYAGYFPQA
IDRGIQAGLL DPRLAEYDIA RLAAALDAQR DHQFEYLGLQ TLYDRYFLHV DETRIELPQT
FFMRVAMGLA LNEIDREARA IEFYMLLSSF DFMSSTPTLF NSGTRHSQLS SCYLTTVADD
LEGIYQSIKE NALLQKFAGG LGNDWTPVRA LGSLIRGTNG KSQGVIPFLK VVNDTAVAVN
QGGKRKGAVC AYLETWHLDI EEFLELRKNT GDERRRTHDM NTANWIPDLF MKRVMENAEW
TLFSPVDTPD LHERYGQDFE TAYRSYEDKA ARGEIKLVKR VPAVQLWRKM LTMLFETGHP
WITFKDACNL RSPQQHMGVV HSSNLCTEIT LNTSDTETAV CNLGSVNLPA HLVRDTDSNG
NDSWRLDTDK LRRTVRTAMR MLDNVIDINY YATPKARAAN VRHRPVGLGI MGFSDALHVM
GLAYASDAAV EFADRSMEAV CYHAYWASSE LAEERGRYSS FRGSLWDQSI LPLDSLKLLA
EGRGRLSEGG GALVEVDRSA TLDWDALRAR IAQHGMRNSN CVAIAPTATI SNIVGVSASI
EPDYQNLYVK SNLSGEFTVV NAHLVRDLKA LGLWDEVMVG DLKYFDGSLA PIDRIPADIK
ARYATAFEID PAWLVEAASR RQKWIDQAQS LNLYVAAPSG KKLDELYRLA WLRGLKTTYY
LRTLGATTME KTSAGSPHDQ AQPDQRTDAA SVSIAPRACS ILDPDCEACQ
//
