ID   F8J7G2_HYPSM            Unreviewed;       790 AA.
AC   F8J7G2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE            EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN   OrderedLocusNames=HYPMC_4069 {ECO:0000313|EMBL:CCB67278.1};
OS   Hyphomicrobium sp. (strain MC1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Hyphomicrobium.
OX   NCBI_TaxID=717785 {ECO:0000313|EMBL:CCB67278.1, ECO:0000313|Proteomes:UP000000494};
RN   [1] {ECO:0000313|Proteomes:UP000000494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC1 {ECO:0000313|Proteomes:UP000000494};
RA   Genoscope.;
RT   "The complete genome of Hyphomicrobium sp. MC1.";
RL   Submitted (MAY-2011) 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; FQ859181; CCB67278.1; -; Genomic_DNA.
DR   RefSeq; WP_013949670.1; NC_015717.1.
DR   AlphaFoldDB; F8J7G2; -.
DR   STRING; 717785.HYPMC_4069; -.
DR   KEGG; hmc:HYPMC_4069; -.
DR   eggNOG; COG0209; Bacteria.
DR   HOGENOM; CLU_000404_2_0_5; -.
DR   Proteomes; UP000000494; Chromosome.
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:UP000000494}.
FT   DOMAIN          17..85
FT                   /note="Ribonucleotide reductase large subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00317"
FT   DOMAIN          91..558
FT                   /note="Ribonucleotide reductase large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02867"
SQ   SEQUENCE   790 AA;  85071 MW;  AAE278802F689409 CRC64;
     MSAILSALPA ISDAIWRRKY RFAGSPTAAG DETIEDTFRR VAKAAASAEA DSATQAKWGA
     AFYDAMADFG FQPAGRILAG AGTDRNVTLF NCFVLGAIPD DLSGIFESVK EAALTMQAGG
     GIGHDFSTLR PSGATVKSIG ADASGPVSFM DVWDAMCRTI MSAGQRRGAM MATLRCDHPD
     IEAFVAAKSD PLRLRNFNLS VLVTDAFMEA VKRGSPWELV FEGKVYKTID AKGLWDKIMR
     ATYDYAEPGV IFIDRINAAN NLAYCETISA TNPCGEQPLP PYGACLLGSI NLARFVEKPF
     SPDARVDRQK LEARVATAVR FLDNVIDISR YPLEAQAQEA RAKRRIGLGI TGLADALIFL
     GLSYGSLAAR EKAAEWMAII QNAAYRASAA LAAEKGAFPL YDASAFLARP NVERLGKDVR
     AVIATNGIRN GCLTSIAPTG TISLLAGNVS SGIEPVFDFV YQRRILGDGA TASEETVEDY
     AYRKFRAQFG ENAPLTHAFV TAETLSPAEH VAMQAAMQPY VDSAISKTIN TPEAISFEDF
     RDIYAEAFAL GLKGCTTYRP NAVTGAVLSK AEGANDAKPA PTSSVGASED PAKFGDVVYM
     TKPLERDAAL EGITYKIKWP ASAHALYVTI NDIVRDGRRR PFEIFINTKN LEHYAWTVAL
     TRMVSAVFRR GGDVSFVAEE LKAVFDPEGG RWMGGRYVPS LLAAIGNVIE QHMLHIGFLT
     REDAEGSDAK PMHLPVAAIE RLGGGPQTAA RDGTASQVAV ARICPKCGER ALHHIEGCWT
     CTNCDYSRCG
//