ID C5T381_ACIDE Unreviewed; 975 AA.
AC C5T381;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=AcdelDRAFT_1361 {ECO:0000313|EMBL:EER61045.1};
OS Acidovorax delafieldii 2AN.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=573060 {ECO:0000313|EMBL:EER61045.1, ECO:0000313|Proteomes:UP000003856};
RN [1] {ECO:0000313|EMBL:EER61045.1, ECO:0000313|Proteomes:UP000003856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2AN {ECO:0000313|EMBL:EER61045.1,
RC ECO:0000313|Proteomes:UP000003856};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Shelobolina E.S.,
RA Picardal F., Roden E., Emerson D.;
RT "The draft genome of Acidovorax delafieldii 2AN.";
RL Submitted (MAY-2009) 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:EER61045.1}.
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DR EMBL; ACQT01000028; EER61045.1; -; Genomic_DNA.
DR RefSeq; WP_005794793.1; NZ_ACQT01000028.1.
DR AlphaFoldDB; C5T381; -.
DR PATRIC; fig|573060.9.peg.3787; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000003856; 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:UP000003856}.
FT DOMAIN 32..132
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 146..235
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 919..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 975 AA; 108697 MW; B0FB81B9C7CDF86C CRC64;
MQAALNTPPS HTAASQALAP NAPEASHVLN HYQIIRRNGA VVPFEPQKIA VAMMKAFLAV
HGTQGAASAS VREVVDTLTH NVTRALMRSR PGGGTFHIED VQDQVELGLM RSGHHEIARA
YVLYRERRTQ ERTRHNEEQL PQAPQLHVLD GGERVVLDQG RLQSLIESAC TGLGADVSAQ
PIVAETMRNL YDGVPMEEVY KASILAARTL IEKDPDYTYA TARLLLHTIV REVLGREVAP
ADMAQSYVDY FPQFIKKGVE NDLLDERLLQ YDLQRLGAAL KAERDLQFDY LGLQTLYDRY
FLHVKKNRIE LPQAFFMRVA MGLSLNEIDR EARAIEFYEI LSSFDFMSST PTLFNSGTLR
SQLSSCYLTT VPDDLDGIYE SIKENALLSK FAGGLGNDWT RVRALGSHIK GTNGESQGVV
PFLKVVNDTA VAVNQGGKRK GAVCTYLETW HLDIEEFLEL RKNTGDDRRR THDMNTANWI
PDLFMRRVME KGTWTLFSPS NVPDLHDLFG TDFEKAYVAY EEKAARGEIK PARTVQATDL
WRKILTMLFE TGHPWITFKD ACNVRSPQQH AGVVHSSNLC TEITLNTSDT ETAVCNLGSV
NLLQHLKNGQ IDHDKLKKTI TVAMRMLDNV IDINYYAVKK ARDSNLRHRP VGLGVMAFQD
SLYELRIPYA SQEAVEFADQ SMEAICYYAY WASTELARER GRYSSYKGSL WDRGILPLDT
LDMLAQARGG YVEVDRSATL DWDALRKKIA QDGMRNSNCV AIAPTATISN IIGVDASIEP
SFGNLSVKSN LSGEFTVING GLVRDLKRLG LWDDVMIMDL KHFKGSLHPI DRVPQDIKAL
YSTAFEVEPR WLVEAASRRQ KWIDQAQSLN IYMAGASGKK LDDTYKLAWV RGLKTTYYLR
TQSATHVEMS TVNTRQLNAV SSGHDNGGSH ASAAQSAPPS TMEAAIAAAA LQAAELPATD
IKFCAIDDPT CEACQ
//
