ID A0A0W0GKM5_9CHLR Unreviewed; 587 AA.
AC A0A0W0GKM5;
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=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=DEALK_00160 {ECO:0000313|EMBL:KTB49105.1};
OS Dehalogenimonas alkenigignens.
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalogenimonas.
OX NCBI_TaxID=1217799 {ECO:0000313|EMBL:KTB49105.1, ECO:0000313|Proteomes:UP000053947};
RN [1] {ECO:0000313|EMBL:KTB49105.1, ECO:0000313|Proteomes:UP000053947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP3-3 {ECO:0000313|EMBL:KTB49105.1,
RC ECO:0000313|Proteomes:UP000053947};
RA Key T.A., Richmond D.P., Bowman K.S., Cho Y.-J., Chun J., da Costa M.S.,
RA Rainey F.A., Moe W.M.;
RT "Genome sequence of the organohalide-respiring Dehalogenimonas
RT alkenigignens type strain (IP3-3T).";
RL Submitted (JUN-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|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:KTB49105.1}.
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DR EMBL; LFDV01000001; KTB49105.1; -; Genomic_DNA.
DR RefSeq; WP_058437537.1; NZ_KQ758903.1.
DR AlphaFoldDB; A0A0W0GKM5; -.
DR STRING; 1217799.DEALK_00160; -.
DR PATRIC; fig|1217799.6.peg.16; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000053947; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053947}.
FT DOMAIN 1..81
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 84..554
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 587 AA; 64983 MW; 61F045FD3E2684D8 CRC64;
MELSQNARII LNKRYLKKDE GGNIIETPED MFRRVANVIA SVERRYKTDE TAWADEFYRM
MTGLEFLPNS PTLLNAGRER GLLSSCFVLP VEDSIEGISC ALVKAMTIHK FGGGTGFSFG
HIRPEGDLVS GNLSSAGGPV KLIKVFSEAT NYIRQAGVRC GCNSASLPVN HPDILKFIQA
KRDGSASANF ATNIEITDDF VDRVRHGKYC QLINPRNGVV TGEIPARVIM DSIAEGAWET
GDPGIMFIDR INDSNPTPQL GNFETTDPCG GQLLVPFESA TLGTINLSLM VSEDSEKPSI
DYLRLGDVIP KAVRFLDNVL DVNLYPLGDV EKASRATRKI GLGLMGFAEL LIKLGIRYDS
DQALEIADEL MWFVRTKTYE ASENLARERG TFPAFTGSVF DRQDGHPMRH ASCLTFTNTG
TTSILANTSC GIHPIYAMVM VRNILDGERL LDINQAFEQI AKKFGFFNSK LVEELLSGVS
PVNCQRIPEP FRQLFVTARD IDPEWCIRMQ AVFQRHIDNA ISQTVNFPKS ATVEDIKSMF
LKAYDLGLKG VTAYRDTSRD AQVLCTGPEC VEVAQRYFQS NGMVEAV
//
