ID D8JTR4_HYPDA Unreviewed; 956 AA.
AC D8JTR4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 OrderedLocusNames=Hden_0809 {ECO:0000313|EMBL:ADJ22626.1};
OS Hyphomicrobium denitrificans (strain ATCC 51888 / DSM 1869 / NCIMB 11706 /
OS TK 0415).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=582899 {ECO:0000313|EMBL:ADJ22626.1, ECO:0000313|Proteomes:UP000002033};
RN [1] {ECO:0000313|Proteomes:UP000002033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51888 / DSM 1869 / NCIB 11706 / TK 0415
RC {ECO:0000313|Proteomes:UP000002033};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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; CP002083; ADJ22626.1; -; Genomic_DNA.
DR RefSeq; WP_013214841.1; NC_014313.1.
DR AlphaFoldDB; D8JTR4; -.
DR STRING; 582899.Hden_0809; -.
DR KEGG; hdn:Hden_0809; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_5; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000002033; Chromosome.
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; 2.
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:UP000002033}.
FT DOMAIN 29..129
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 143..232
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 956 AA; 106673 MW; 8DC8C1C8A1B7A769 CRC64;
MSITLEARPS QHYESSSTGI PKATVDPVFQ VIRRNGSVTP FDASKISVAL TKAFLAVEGG
RAAASRRVHE TVDGLTSQIV VALTRRGVQE RTFHIEEIQD QVELALMRGE HHKVARAYVL
YREERKRERA AETAAPIPTM PSISVKSKDG SLAPLDAARL RKLIEESCAG LADVSAEAIL
SETQRNLYDG ITRDELADAP VLAARTLIET EPNYTFVTAR LLMDKLRREA LSFVAGRTDE
ARQSEMGERY PEYFRAFIAK GIVADLLDPE LARFDLDRLG GALKPERDGI FQYLGLQTLY
DRYFLQTHGI RFELPQAFFM RVAMGLALRE IDREAKAIEF YDLISTFDFM CSTPTLFNAG
TPRPQLSSCF LTTVPDDLDG IFKSIKDNAL LAKYSGGLGN DWTRVRGLGA HIKGTNGESQ
GVVPFLKVAN DTAIAVNQGG KRKGAVCAYL ETWHIDIEEF LDLRKNAGDD RRRTHDMNTA
HWIPDLFMQR VAEDGQWTLF SPDETPDLHD LYGTAFAERY EAYEEKAERM EMKVARRVRA
VDLWRRMLTM LFETGHPWIT FKDPCNLRSP QQHCGIVHSS NLCAEITLNT SNDEVAVCNL
GSINLVAHVT NDGVDFDKLE RTVKTAMRML DNVIDINFYT IPEARRSNLR HRPVGMGLMG
FQDALQALRI NYGSEEAVAF ADTSMEAISF HAISASVDLA AERGRYPSFD GSLWSQGILP
IDSIELLKSA RGTDLRLDTS STLDWDGLRD RVRTTGMRNS NTMAIAPTAT ISNICGVAQS
IEPAFRNLYV KSNMSGDFTV VNPFLVRDLK ARGLWDEVMI SDLKYFDGSL GAIDRIPEDL
KALYATAFEI DAHWLVDAAA RRQKWIDQGQ SLNLYIAAPN GRKLDALYRL AWERGLKTTY
YLRSQSATHV EKSTLKGTDG KLNAVSSSVH HSAPENIEAM AGKACLIDDP TCEACQ
//
