ID A0A074JRE2_9RHOB Unreviewed; 754 AA.
AC A0A074JRE2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=DT23_15675 {ECO:0000313|EMBL:KEO59034.1};
OS Thioclava indica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1353528 {ECO:0000313|EMBL:KEO59034.1, ECO:0000313|Proteomes:UP000027471};
RN [1] {ECO:0000313|EMBL:KEO59034.1, ECO:0000313|Proteomes:UP000027471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DT23-4 {ECO:0000313|EMBL:KEO59034.1,
RC ECO:0000313|Proteomes:UP000027471};
RX PubMed=25361528; DOI=10.1007/s10482-014-0320-3;
RA Liu Y., Lai Q., Du J., Xu H., Jiang L., Shao Z.;
RT "Thioclava indica sp. nov., isolated from surface seawater of the Indian
RT Ocean.";
RL Antonie Van Leeuwenhoek 107:297-304(2015).
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|ARBA:ARBA00001922,
CC ECO:0000256|RuleBase:RU364064};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC family. {ECO:0000256|ARBA:ARBA00007405, ECO:0000256|RuleBase:RU364064}.
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:KEO59034.1}.
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DR EMBL; AUNB01000030; KEO59034.1; -; Genomic_DNA.
DR RefSeq; WP_038131165.1; NZ_AUNB01000030.1.
DR AlphaFoldDB; A0A074JRE2; -.
DR STRING; 1353528.DT23_15675; -.
DR eggNOG; COG0209; Bacteria.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000027471; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; cd20336; Rcat_RBR; 1.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR NCBIfam; TIGR02504; NrdJ_Z; 1.
DR PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 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.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|RuleBase:RU364064};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, 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,
KW ECO:0000256|RuleBase:RU364064};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064};
KW Reference proteome {ECO:0000313|Proteomes:UP000027471}.
FT DOMAIN 7..79
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 85..551
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 754 AA; 82927 MW; 2243BFA610DC9487 CRC64;
MTRFAAPIAR QIWDMKYRLK EQDGTPIDGT VEDSWRRIAR ALAVVEKDPA EWEEKFYNAL
EDFKYLPAGR ITAGAGTGRS VTLFNCFVMG TIPDHMGGIF DMLKEAALTM QQGGGIGYDF
STIRPKGAEV KGVAADASGP LSFMDVWDAM CRTIMSAGSR RGAMMATMRC DHPDIEQFIT
AKQDSARLRM FNLSVLVTDA FMEAVKADGP WELTFGDRVY HTLNARDLWN KIMRATYDFA
EPGVIFIDRI NQMNNLNYCE QIAATNPCGE QPLPPYGACL LGSVNLARLV TNPFETQAEL
DPVKLDEIVR LAIRMMDNVV DASRFPLPQQ EEEARNKRRI GLGVTGLADA LLMLGLRYGS
PEAAAQTEAW MKLIARASYL ASVDLAREKG AFPLFDAEKY LASGNMMQMD EDVRAAIAKH
GIRNALLTSI APTGTISLYA GNVSSGIEPV FAYAYTRKVL QPDGSRTEEE VVDYAVQMWR
DLKGDAPLPD HFVNAQTLAP LDHVRMQAAA QKWIDSSISK TINCPEDIAF EDFKSVYMEA
WDSGCKGCTT YRPNDVTGSV LSVSEASEKA PETDQGADVV YLTEPLDRPA ALEGSTYKIK
WPGSEHAIYI TINDIVQGGH RRPFEVFINS KNMEHFAWTV ALTRMISAVF RRGGDVSFVV
EELKAVFDPR GGAWMSGKYV PSILAAIGGV IERHLIATGF IEGEGMGLKT DPEAEKMIVG
EAPRGKACPS CGSYAMRMVE GCMTCADCGH SKCG
//
