ID A0A0W0V8M6_9GAMM Unreviewed; 939 AA.
AC A0A0W0V8M6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN Name=rir1 {ECO:0000313|EMBL:KTD16487.1};
GN ORFNames=Ljor_0793 {ECO:0000313|EMBL:KTD16487.1};
OS Legionella jordanis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=456 {ECO:0000313|EMBL:KTD16487.1, ECO:0000313|Proteomes:UP000055035};
RN [1] {ECO:0000313|EMBL:KTD16487.1, ECO:0000313|Proteomes:UP000055035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL-540 {ECO:0000313|EMBL:KTD16487.1,
RC ECO:0000313|Proteomes:UP000055035};
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: Catalyzes the reduction of ribonucleotides to
CC deoxyribonucleotides. May function to provide a pool of
CC deoxyribonucleotide precursors for DNA repair during oxygen limitation
CC and/or for immediate growth after restoration of oxygen.
CC {ECO:0000256|RuleBase:RU364064}.
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:RU364064};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|RuleBase:RU364064};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC family. {ECO:0000256|RuleBase:RU364064}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406}.
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:KTD16487.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNYJ01000011; KTD16487.1; -; Genomic_DNA.
DR RefSeq; WP_058470339.1; NZ_RDQQ01000001.1.
DR AlphaFoldDB; A0A0W0V8M6; -.
DR STRING; 456.Ljor_0793; -.
DR PATRIC; fig|456.5.peg.844; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000055035; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
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:0071897; P:DNA 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; IPR013344; RNR_NrdJ/NrdZ.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR NCBIfam; TIGR02504; NrdJ_Z; 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}; Cobalamin {ECO:0000256|RuleBase:RU364064};
KW Cobalt {ECO:0000256|RuleBase:RU364064};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634,
KW ECO:0000256|RuleBase:RU364064};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064};
KW Reference proteome {ECO:0000313|Proteomes:UP000055035}.
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 939 AA; 106268 MW; 300B2626894B52B4 CRC64;
MSEILEPVKD VPQTGQLELA ANVPGVLKTI KRNGKVVQYD DNKIKVAITK AFIAIEGSNA
AASNRIHEQV NQLTQQITQA FKRRLPSGGA IHIEDIQDQV ELALMRSSHY EVARAYVLYR
EEHRKVRENA LKQQARDAKV PLITMPDGEI KPLDMERVKT IVNEACRDLD NVSAEPVIKD
ALRNLYNQAK LEDVHKALIM AARTLVEKEP NYTYVSARLL LDSLRSEALN KLQMQTEATF
DEMAELYPAY FKAYLAQGIN QGLLDHKLAE FDLDKLGKAL LPQRDMQFTY LSLQTLYDRY
FIHENGERYE LPQAFFMRVA MGLAIREPEK NERAIEFYLL LSSFDYMSST PTLFNSGTVR
PQLSSCYLTT VPDDLDGIYS AIKDNALLSK FAGGLGNDWT PVRAMGSYIK GTNGKSQGVV
PFLNVADATA VAVNQGGKRK GAVCAYLECW HRDVEEFLEL RKNTGDDRRR THDMNTALWV
PDLFMKRVHE DGEWTLFSPD EVPELHEEYG KAFEAFYTKC EEKARRGEIK NAKTLSAVKL
WRKMLSMLFE TGHPWLTFKD PCNLRSPQQH AGVIHSSNLC TEITLNTSQD EIAVCNLGSI
NLPAHIRNGQ LDNEKLKQTI TTAVRMLDNV IDINYYSVPQ ARNSNLQHRP VGLGLMGFQD
ALYELKINYA SQEAVEFADV SMELISYYAI EASCELAKER GNYSSYEGSL WSKGILPIDS
INLLQQARNK YLEQDRSQRL DWESLRVKVR TQGMRNSNVM AIAPTATISN ICGVSQSIEP
TYQNLYVKSN LSGEFTVINP YLVADLKALN LWDEVMVNDL KYFNGSVQPI SRIPNELKAR
YATAFEIDPI WLVEAASRRQ KWIDQAQSLN IYMAKPSGKK LDQLYKYAWI KGLKTTYYLR
SMGATNAEKS TIADGALNAV KIEEPKVCSI LDPDCEACQ
//
