ID Q73QV2_TREDE Unreviewed; 845 AA.
AC Q73QV2;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 114.
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 Name=nrdA {ECO:0000313|EMBL:AAS10836.1};
GN OrderedLocusNames=TDE_0341 {ECO:0000313|EMBL:AAS10836.1};
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=243275 {ECO:0000313|EMBL:AAS10836.1, ECO:0000313|Proteomes:UP000008212};
RN [1] {ECO:0000313|EMBL:AAS10836.1, ECO:0000313|Proteomes:UP000008212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104
RC {ECO:0000313|Proteomes:UP000008212};
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G., Malek J.,
RA Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K., Pal S.,
RA Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E., Baca E.,
RA Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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; AE017226; AAS10836.1; -; Genomic_DNA.
DR RefSeq; NP_970955.1; NC_002967.9.
DR RefSeq; WP_002681315.1; NC_002967.9.
DR AlphaFoldDB; Q73QV2; -.
DR STRING; 243275.TDE_0341; -.
DR PaxDb; 243275-TDE_0341; -.
DR GeneID; 2739340; -.
DR KEGG; tde:TDE_0341; -.
DR PATRIC; fig|243275.7.peg.330; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_12; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000008212; 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; 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; 1.
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:UP000008212}.
FT DOMAIN 1..98
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 845 AA; 96586 MW; 0DF70D06C09405C8 CRC64;
MQIIKRNGET KNYEPEKIEG AIRSAFKSVE NSPHTDLDTI IPPLVKEIEE DILELTKNGS
LVQVETIQDL VEKTLIEHNY YAEVKNFILY RVGRTKRRDS RQMISRFFDT IEIQSVLTEI
QNDFTSDEYS LNLLAHKFLS FRKENMSETE SLAMLIKASV ELTAQDAPDW EFIAARLLML
QFKLKLKTEL EKRQIHSFYE KIKYLENEGL YGTYICEAYS RDELEEAASF INEERNKLFT
YSALDLLLRR YVIHTHSNIV LESPQEMFLG IALHLAMKEK LKRLEWVRRF YDMTSTLKVT
MATPTLSNAR KPYHQLSSCF IDTVPDSLDG IYRSIDNFAK VSKFGGGMGL YFGKVRAVGS
PIRGFMGAAG GIIRWIKLAN DTAVAVDQLG VRQGSVAVYL DVWHKDIPEF LQLRTNNGDD
RMKAHDVFPA VCYPDLFWKT VRDDINSSWH LMCPHEILKT KGYALEDFYG EEWEKRYKDC
VADSRINKRE IPIKELVRLI LKSAVETGTP FAFNRDHANK TNTNPHKGMI YCSNLCTEIS
QNMSGIKHKN IEIKTEDGDT VVATTTIPGD FVVCNLASLV LGNIDVNDEQ EIDTIVSSAV
RALDNVIDLN FYPIPYAQIT NSRYRSIGLG ASGYHHALAK NGIAWESEEH LNFADKVFER
INYAAIKASS QIAKEKGSYS YFEGSDWQTG EYFKKRNYVD ENWKALTEEV KSNGMRNAYL
LAVAPTSSTS IIAGTTAGVD PIMNKYFLEE KKGSLMPRVA PSLSPETYWL YKNAHHIEQG
WSIRAAGLRQ RHIDQAQSVN LYITNEFTFS KVLSLYVKAW EEGLKSIYYV RSRSLEVEEC
ESCSS
//
