ID D3HSB8_LEGLN Unreviewed; 941 AA.
AC D3HSB8;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=rir1 {ECO:0000313|EMBL:CBJ11806.1};
GN OrderedLocusNames=LLO_1440 {ECO:0000313|EMBL:CBJ11806.1};
OS Legionella longbeachae serogroup 1 (strain NSW150).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=661367 {ECO:0000313|EMBL:CBJ11806.1, ECO:0000313|Proteomes:UP000001060};
RN [1] {ECO:0000313|EMBL:CBJ11806.1, ECO:0000313|Proteomes:UP000001060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSW150 {ECO:0000313|EMBL:CBJ11806.1,
RC ECO:0000313|Proteomes:UP000001060};
RX PubMed=20174605; DOI=10.1371/journal.pgen.1000851;
RA Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D.,
RA Newton H., Sansom F., Jarraud S., Zidane N., Ma L., Bouchier C.,
RA Etienne J., Hartland E., Buchrieser C.;
RT "Analysis of the Legionella longbeachae genome and transcriptome uncovers
RT unique strategies to cause Legionnaires' disease.";
RL PLoS Genet. 6:E1000851-E1000851(2010).
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; FN650140; CBJ11806.1; -; Genomic_DNA.
DR RefSeq; WP_003631798.1; NC_013861.1.
DR AlphaFoldDB; D3HSB8; -.
DR STRING; 661367.LLO_1440; -.
DR KEGG; llo:LLO_1440; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_6; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000001060; 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; 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:UP000001060}.
FT DOMAIN 27..127
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 141..230
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 941 AA; 106587 MW; A1438BB962A0117F CRC64;
MSATLDPVND VPQISQLELT ANAPGLLKTI KRNGKVVNYD DTKIKIAITK AFIADEGGTA
STSDRIHQQI EELTRQITQV FKRRLPSGGA VHIEDIQDQV ELALMRSGHY KVARAYVLYR
EEHRKARENE LKKQASDQKL LLITMPDGEL KPLDTERMDT IVHEACRNLE HVDAEPVIKD
ALRNLYNEAK FADVHKALIM AARTLVEKEP NYTYVSARLL LDCLRIEALH KLGIEADATF
DEMSQLYPAY FKIYVAHGIK QGMLDEKMAD FDLEKLGKAL LPERDMKFTY LSLQTLYDRY
FIHDQGIRYE LPQAFFMRVA MGLAIREKDK NEKAIEFYQL LSSFDYMSST PTLFNSGTIR
PQLSSCYLTT VPDHLDGIYS AIKDNALLSK YAGGLGNDWT PVRAMGSHIK GTNGKSQGVV
PFLNVADATA VAVNQGGKRK GAVCAYLECW HKDVEEFLEL RKNTGDDRRR THDMNTALWI
PDLFMMRVRE DADWTLFSPD EVPELHDQFG KAFEALYNKY EEKAHQGLMK NVKTVSAVKL
WRKMLSMLFE TGHPWMTFKD PCNLRSPQQH CGVVHSSNLC TEITLNTSEE EIAVCNLGSI
NLPAHIKNGK LDIEKLKQTI KTAVRMLDNV IDINYYSVPQ ARNSNLKHRP VGLGLMGFQD
ALYELKIDYA SEEAVEFADS SMELISYYAI EASCDLAKER GSYSSYEGSL WSKGILPIDS
INLLQQARNK YLEQDRSQRL DWESLRIKVR TQGMRNSNVM AIAPTATISN ICGVAQSIEP
TYQNLYVKSN LSGEFTVINP YLVADLKALE LWDEVMVNDL KYFNGSVQPI SRIPADLKKR
YATSFEIDPI WLVDAASRRQ KWIDQAQSLN IYMAEPSGKK LDQLYMHAWI RGLKTTYYLR
SMGASNAEKS TVTDSALNAV KIMTEAPKAC SILDPDCEAC Q
//
