ID A0A0A0DMJ2_9BURK Unreviewed; 967 AA.
AC A0A0A0DMJ2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=JY96_03795 {ECO:0000313|EMBL:KGM39439.1};
OS Aquabacterium sp. NJ1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Aquabacterium.
OX NCBI_TaxID=1538295 {ECO:0000313|EMBL:KGM39439.1, ECO:0000313|Proteomes:UP000029993};
RN [1] {ECO:0000313|EMBL:KGM39439.1, ECO:0000313|Proteomes:UP000029993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJ1 {ECO:0000313|EMBL:KGM39439.1,
RC ECO:0000313|Proteomes:UP000029993};
RA Masuda H.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGM39439.1, ECO:0000313|Proteomes:UP000029993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJ1 {ECO:0000313|EMBL:KGM39439.1,
RC ECO:0000313|Proteomes:UP000029993};
RA Shiwa Y., Yoshikawa H., Zylstra G.J.;
RT "The draft genome sequence of a soil bacterium, Aquabacterium sp. strain
RT NJ1, capable of utilizing both liquid and solid n-alkanes.";
RL Submitted (OCT-2014) 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:KGM39439.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JRKM01000001; KGM39439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0DMJ2; -.
DR STRING; 1538295.JY96_03795; -.
DR eggNOG; COG0209; Bacteria.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000029993; 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:UP000029993}.
FT DOMAIN 34..134
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 149..238
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 967 AA; 107659 MW; F9AF5432748A554B CRC64;
MQTSTPSTMP TPASVMPGAA AVAVEPRQSA YSAYQIIRRN GAVVSFEPSK IAVALMKAFL
AVHGTQGAAS ASVRETVDGL TEMVVRGLLR SRPSGGTFHI EDIQDQVELS LMRGGHHEIA
RAYVLYRERR AQERAKQADA QQAAALPTLT VIDRGQRVPL DLARLQALIV EACSGLGDDV
KAAPILAETQ RNLYDGVSID EVYKAAILAA RTRIEHDPAY TRATARLLQH TIRREILGEE
VTHAEMATRY ADYFPTFIKK GVEAELLDER MQQFDLARLG AALKYERDLN FDYLGLQTLY
DRYFLHHNGQ RIEMPQAFFM RVAMGLALNE IDREARAIEF YELLSSFDFM SSTPTLFNSG
TRRSQLSSCY LTTVPDDLDG IYEAIKENAL LSKFAGGLGN DWTPVRALGS HIKGTNGKSQ
GVVPFLKVVN DTAVAVNQGG KRKGAVCAYL ESWHLDVEEF LELRKNTGDD RRRTHDMNTA
NWIPDLFMRR VMEGGDWTLF SPATCPDLHD KFGKAFEEAY TAYEAKADRG EIKLFKRVKA
TDMWRRMLSM LFETGHPWIT FKDACNVRSP QQHVGVVHSS NLCTEITLNT NGGEIAVCNL
GSVNLAQHIK DGAIDQEKVK KTVKTAMRML DNVIDINYYA VKKARDSNLR HRPVGLGIMG
FQDALYQLRT PYASQEAIEF ADRSMEAVCY YAYWASTELA EERGRYSSYR GSLWDRGILP
IDSLKLLAEQ RGGYVEVDTS TSMDWDALRA RIAMFGMRNS NCVAIAPTAT ISNIIGVDAS
IEPCFGNLSV KSNLSGEFTV VNEYLVRDLK KLGLWDDVMV MDLKHFDGSL RRIDRVPEDL
KNLYATAFEV EPVWLVEAAS RRQKWIDQAQ SLNIYMAGAS GKKLDETYKL AWLRGLKTTY
YLRTVGATHA EKSTVSRGQL NAVSNMVGGS MNAAPQQAAA PVEAAPAEPA TDIKFCSIDN
PDCEACQ
//
