ID A0A1I2G1N3_9BURK Unreviewed; 978 AA.
AC A0A1I2G1N3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN04489711_11329 {ECO:0000313|EMBL:SFF11575.1};
OS Paracidovorax wautersii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Paracidovorax.
OX NCBI_TaxID=1177982 {ECO:0000313|EMBL:SFF11575.1, ECO:0000313|Proteomes:UP000199119};
RN [1] {ECO:0000313|EMBL:SFF11575.1, ECO:0000313|Proteomes:UP000199119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27981 {ECO:0000313|EMBL:SFF11575.1,
RC ECO:0000313|Proteomes:UP000199119};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FONX01000013; SFF11575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2G1N3; -.
DR STRING; 1177982.SAMN04489711_11329; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000199119; 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}.
FT DOMAIN 36..136
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 150..239
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 978 AA; 108523 MW; EE5BC6A368A19D5E CRC64;
MQAALNTPSL DVNRTQAPSE ADASSGMPSL NTLSHYQTIR RNGAVVPFEP QKIAVALMKA
FLAVHGTQGA ASASVRETVD ALTQAVVRGL IRSRPQGGTF HIEDVQDQVE LGLMRGGHHE
VARAYVLYRE RRAQERVHQQ EKLAPAMPAL RVIDNGQRVD LDILRLHQLI ESACSGLGAD
IHAAPIVSET MRNLYDGVPM DEVYKASILA ARTLIEKDPD YTYATARLLL HTIVREVLGR
DVVPAEMSAA YASYFPEFIQ KGVDNELLDP RLLEFDLDRL GKALNAQRDQ QFDYLGLQTL
YDRYFLHVRK TRIELPQAFF MRVAMGLSLN EADREARAIE FYEVLSSFDF MSSTPTLFNS
GTLRSQLSSC YLTTVPDDLD GIYESIKENA LLSKFAGGLG NDWTRVRALG SHIKGTNGES
QGVVPFLKVV NDTAVAVNQG GKRKGAVCTY LETWHLDIEE FLELRKNTGD DRRRTHDMNT
ANWIPDLFMR RVMEKGTWTL FSPSSVPDLH DLFGSAFEKA YVAYEEKAAR GEIKPSRTIQ
ATDLWRKILT MLFETGHPWI TFKDACNVRS PQQHAGVVHS SNLCTEITLN TSDTETAVCN
LGSVNLMRHL KDGANGKELD HAKLRKTIST AMRMLDNVID INYYAVEKAR TSNMRHRPVG
LGLMAFQDSL YELRVPYASE AAVEFADRSM EAICYYAYWA STELAKERGR YESYTGSLWD
RGILPIDSLN LLEEARGGYV EVDRSSTLDW DALRKKIAQD GMRNSNCVAI APTATISNIV
GVDASIEPSF GNLSVKSNLS GEFTVINGYL VRDLKRLGLW DDVMVMDLKH FKGSLHSIDR
VPQEVKALYS TAFEVAPTWL VEAASRRQKW IDQAQSLNIY MAGASGKKLD ETYKLAWVRG
LKTTYYLRTQ SATHVEMSTV NTRQLNSVAS GSEGSAPAAA APSALEAAAA AAQAQAAALP
ATDVKFCAID DPTCEACQ
//
