ID A0A0W1AB68_9GAMM Unreviewed; 941 AA.
AC A0A0W1AB68;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:KTD78400.1};
GN ORFNames=Lwal_1835 {ECO:0000313|EMBL:KTD78400.1};
OS Legionella waltersii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=66969 {ECO:0000313|EMBL:KTD78400.1, ECO:0000313|Proteomes:UP000054729};
RN [1] {ECO:0000313|EMBL:KTD78400.1, ECO:0000313|Proteomes:UP000054729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51914 {ECO:0000313|EMBL:KTD78400.1,
RC ECO:0000313|Proteomes:UP000054729};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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:KTD78400.1}.
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DR EMBL; LNZB01000041; KTD78400.1; -; Genomic_DNA.
DR RefSeq; WP_058480491.1; NZ_LT906442.1.
DR AlphaFoldDB; A0A0W1AB68; -.
DR STRING; 66969.Lwal_1835; -.
DR PATRIC; fig|66969.6.peg.1996; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000054729; 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:UP000054729}.
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; 106733 MW; AD27C8D85AB9A4CF CRC64;
MSEILEPVMD IPLASQMELN SNAPGALKTI KRNGKVVVYD DTKIKIAITK AFIADEGGTA
PSSDRIHQQI EELTRQVSQV FKRRLPAGGA IHIEDIQDQV ELALMRSGHY KVARSYVLYR
EERRQAREKE VKQRPKDSKE LLITMPNGEV EPLDMERVNT IVNESCRNLD NVQAEPVIKD
ALRNLYNQAK FEDVHKALIM SARALVEKEP NYTFVSARLL LDSMRMEALT KLKIKSDATF
DEMATLYPSY FKAYIQKGIA QGMLEPKMAD FDLDKLSKAL LPERDMKFTY LSLQTLYDRY
FIHEHGVRYE LPQAFFMRVA MGLAIREQNK EQKAIEFYQL LSSFDYMSST PTLFNSGTVR
PQLSSCYLTT VPDHLDGIYS AIKDNALLSK YAGGLGNDWT PVRAMGAHIQ GTNGKSQGVV
PFLNVADATA VAVNQGGKRK GAVCAYLECW HRDVEEFLEL RKNTGDDRRR THDMNTALWI
PDLFMKRVRE EGDWTLFSPD EVPDLHDQYG KAFETLYVEC EEKARQGLIR NVKTLSAVKL
WRKMLSMLFE TGHPWMTFKD PCNLRSPQQH VGVVHSSNLC TEITLNTSNE EIAVCNLGSI
NLPAHIKNGK LDKEKLKQTI RTAVRMLDNV IDINYYSVPQ ARHSNLQHRP VGLGIMGFQD
ALYELKMDYA SKEAVEFADT SMELVSYYAI EASCDLAKER GSYSTYEGSL WSKGILPIDS
INLLQQSRNK YLEQDRSQKL DWEPLRVKVR TQGMRNSNVM AIAPTATISN ICGVAQSIEP
TYQNLYVKSN LSGEFTVINP YLVADLKALN LWDEVMVNDL KYFNGSVQPI SRIPAELKNR
YATSFEIDPI WLVEAASRRQ KWIDQAQSLN IYMAQPSGKK LDQLYMHAWT RGLKTTYYLR
SLGASNAEKS TVTDGALNAV KIVDTEPKAC LITDPDCEAC Q
//
