ID   A0A0B7IWP0_9PROT        Unreviewed;       732 AA.
AC   A0A0B7IWP0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE            EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN   ORFNames=BN1209_1671 {ECO:0000313|EMBL:CEN56707.1};
OS   Candidatus Methylopumilus turicensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylopumilus.
OX   NCBI_TaxID=1581680 {ECO:0000313|EMBL:CEN56707.1, ECO:0000313|Proteomes:UP000056322};
RN   [1] {ECO:0000313|Proteomes:UP000056322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMS-10A-171 {ECO:0000313|Proteomes:UP000056322};
RA   Salcher M.M.;
RL   Submitted (DEC-2014) 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}.
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DR   EMBL; LN794158; CEN56707.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B7IWP0; -.
DR   STRING; 1581680.BN1209_1671; -.
DR   KEGG; mbac:BN1209_1671; -.
DR   HOGENOM; CLU_000404_2_0_4; -.
DR   Proteomes; UP000056322; Chromosome 1.
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   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:UP000056322}.
FT   DOMAIN          40..108
FT                   /note="Ribonucleotide reductase large subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00317"
FT   DOMAIN          121..667
FT                   /note="Ribonucleotide reductase large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02867"
SQ   SEQUENCE   732 AA;  82168 MW;  A310CB63B75BEAB5 CRC64;
     MLNKLQNKTG IPPMLQAVKT PEEAAMSENN QKEVPMQSVS LDIWDKKYRL KTKQGDHVDQ
     NMDDSYSRVA RALADVEEES KRAEWHEKFL WALRHGAIPA GRITSNAGAL EHKPATSTIN
     CTVSGIVEDS MDGILNKVHE AGLTLKAGCG IGYEFSTLRP KGAFVAGAGA YTSGPLSFMD
     IFDKMCFTVS SAGGRRGAQM ATFDISHPDV TDFIKAKREA GRLRQFNLSC LITKEFMEAV
     KADADWKLAF PVTSKEATVD ALDTKDEAQV VWREWPIKDK YLTRESDGKT ACRVYKTIRA
     RRLWDVIMSS TYDFAEPGFI LIDRVNEMNN NWFCENIRAT NPCGEQPLPP YGACLLGSVN
     LTKFVRNPFT DQATFDWDEY RQVVSIFTRM LDNVVEINGL PLEQQRAEIA RKRRHGMGYL
     GLGSTLTMLK MKYGEEASVA FTEEVTKVMA ETGWTVGIDL AKEKGAAPIM DEEFVVTGDM
     LSKRPEMVKD GFKLGDKVKG KVLMGMYSRY MQQFPEALRK QIAKTGVRFS HHSSIAPTGT
     ISLSLANNAS NGIEPSFAHH YARNVIREGK KSKEKVDVFS YELLAYRELI NSKAMPFSDA
     EDEKLPDYFL DSSTIQAKAH VDIQAAAQKW IDSSISKTIN VPTDYDFEDF KNIYLYAYDK
     GLKGCTTFRF NPEAFQGVLV TEKDLENTTY KFTLEDGTVV EVKGNEEIEY DGEMHSAANL
     YDALKEGYYG KF
//