ID A0A0G1REQ0_9BACT Unreviewed; 811 AA.
AC A0A0G1REQ0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=UX29_C0004G0007 {ECO:0000313|EMBL:KKU19405.1};
OS Parcubacteria group bacterium GW2011_GWA2_46_10.
OC Bacteria.
OX NCBI_TaxID=1618835 {ECO:0000313|EMBL:KKU19405.1, ECO:0000313|Proteomes:UP000033973};
RN [1] {ECO:0000313|EMBL:KKU19405.1, ECO:0000313|Proteomes:UP000033973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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:KKU19405.1}.
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DR EMBL; LCLQ01000004; KKU19405.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1REQ0; -.
DR STRING; 1618835.UX29_C0004G0007; -.
DR PATRIC; fig|1618835.3.peg.182; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000033973; 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; 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 InterPro; IPR008926; RNR_R1-su_N.
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.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 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}.
FT DOMAIN 12..90
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 96..583
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 811 AA; 90403 MW; 16AA71DA9850930B CRC64;
MNKQLKDKIN KSYSENALKM MNKRYLWEDA KGKKETPADM LDRVSRDLAA VETKYGKKVN
EVKKIEKDFL EVMMNKEFTP AGRTITNSGA GTKVVANCIV LPIPDSMEGI FQTLKDAALS
QQAGSGLGFA LDELRPTFSP TKTSRGFSSG SVSFLKVYDA AFGTIKQQGR HGANMAMISV
EHPDFHDFLI SKAREGDIRN FNISVKLTDR FMKQVLEHPD KQWYCVWKGK KVRPHKVLRN
PNGSVSGVEP MDITVGQIFD EIAHYAWNNG EPGVVFIDEV NRKNPLPDLG PIYTSNPCGE
QFLHAYDNCN LGSINLAVLV ENGKLDEKRL REVTRVAVRM LDNVIDKFDF PVAKVSEMAI
KNRRVGLGIM GFADLLYQLG IKYNSKEGYA MAERAMGIIQ EEAHKASRDL VREKGEFPNW
KKSVFAKGKK KVKMRNAALT TVAPTGSIAM MFDCSSGLEP NFALAFIKQD KDGEFYQYLN
RHFETELNRR GFSKEEKEAI KEEVVAKGTI QHLVELPQDL RDAFVVAMDI SGPEHIAMQS
VFQKHVDNSI SKTINLPNHA TVEDVKQTYI DAWKMKCKSC TVYRDGSRAI QILNVGKNEG
DIVKTTEDPN NLKSQVVERG EVVLEVTRSA DTTLQERERP EVLNGKTYRV RTGYGKLFIT
INSDEKGRPF EVFATLGKSG GYFQEQTEAI CRLISLALRS NINARYIVDH LKGIRGPMVT
MTAKGTILSL PDAIAKILEE HINGGEGVDF DGEVVMATVE DEAQMLSQGG TNAARSVADY
GYMPECPECG GQIVMSEGCI ECKSCGFSRC G
//
