ID A0A225MH49_9BURK Unreviewed; 972 AA.
AC A0A225MH49;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=CEY11_14745 {ECO:0000313|EMBL:OWT58249.1};
OS Candidimonas nitroreducens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Candidimonas.
OX NCBI_TaxID=683354 {ECO:0000313|EMBL:OWT58249.1, ECO:0000313|Proteomes:UP000214603};
RN [1] {ECO:0000313|Proteomes:UP000214603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-089 {ECO:0000313|Proteomes:UP000214603};
RA Fan M., Lin Y.;
RT "Herbaspirillum phytohormonus sp. nov., isolated from the root nodule of
RT Robinia pseudoacacia in lead-zinc mine.";
RL Submitted (JUN-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}.
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:OWT58249.1}.
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DR EMBL; NJIH01000008; OWT58249.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A225MH49; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000214603; 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:UP000214603}.
FT DOMAIN 35..135
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..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 108346 MW; 4137CBB26AE5B20A CRC64;
MQTTQIAESR PEAAPSPVPA PADQGTANVG QWHNFHIIRR NGAVVGFEPG KIAIAMTKAF
LAVNGGQGAA SARVRELVEK LTAQAVGALV RNRPSGGTFH IEEIQDQVEL ALMRSGEHDV
ARAYVLYREK RSQERARSGQ AQAPAQQSTL NVTDNGTTRP LDLAHLRNII DEAGSNLSHL
VDTDAILKET VKNLYDGIPV DEVFKSAILS ARALVEKEPA YSQVTAGLLL HTIRKEVLGE
EVSQSDMATR YAEYFPRFIK IGIENELLDP KLRQYDLPRL SQALKAERDH QFNYLGLQTL
YDRYFLHVHG RRIELPQVFF MRVAMGLALN EIDREARAIE FYEILSSFDF MSSTPTLFNS
GTVHSQLSSC YLTTVSDDLE GIYDAIKENA LLAKYAGGLG NDWTPVRALR SHIKGTNGES
QGVVPFLKVV NDTAVAVNQG GKRKGAVCAY LETWHLDIEE FLELRKNTGD ERRRTHDMNT
ANWIPDLFMK RVMENGEWTL LSPSDAPDLH DKYGRAFEQA YLGYEDKIAR GELKLYKKVP
AVSLWRKMLS MLFETGHPWL TFKDPCNIRS PQQHVGVVHG SNLCTEITLN TSDTEIAVCN
LGSVNLTAHL RQNDAGGYEL DHDKLQRTID IAMRMLDNVI DINYYAVPKA RNSNARHRPV
GLGIMGFQDC LHKMRVPFAS DAAVEFSDRS SEAVCYYAYW ASSKLAAERG SYSSFKGSLW
DRGILPQDTL ALLREERGGH VEIDDSSTLD WDSLRSHIHQ HGMRNSNCIA IAPTATIANI
IGVSPCIEPN YRNLYVKSNL SGEFTVVNDY LVRDLKERNL WDEVMVADLK YFDGSLARID
RVPDDLRELY ATAFEIHPRW VIECGARRQK WIDQSQSLNI FMTGVSGKKL DETYKLAWVR
GLKTTYYLRS NSATNAEKST GRGGELNAVS SGSGQSAAAA AQAAALPEAE IVGTVCTLRP
GDEGFEECEA CQ
//
