ID A0A0B2BT82_9ACTN Unreviewed; 988 AA.
AC A0A0B2BT82;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|ARBA:ARBA00014409, ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU364064};
GN ORFNames=CLV56_3270 {ECO:0000313|EMBL:PJJ53775.1};
OS Mumia flava.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Mumia.
OX NCBI_TaxID=1348852 {ECO:0000313|EMBL:PJJ53775.1, ECO:0000313|Proteomes:UP000230842};
RN [1] {ECO:0000313|EMBL:PJJ53775.1, ECO:0000313|Proteomes:UP000230842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27763 {ECO:0000313|EMBL:PJJ53775.1,
RC ECO:0000313|Proteomes:UP000230842};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) 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|ARBA:ARBA00025437, 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:PJJ53775.1}.
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DR EMBL; PGEZ01000002; PJJ53775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2BT82; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000230842; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR013678; RNR_2_N.
DR InterPro; IPR000788; RNR_lg_C.
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; PF08471; Ribonuc_red_2_N; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 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 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:UP000230842}.
FT DOMAIN 54..137
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 158..694
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 988 AA; 107440 MW; 211E7B92D8F4A627 CRC64;
MTETVSGPTG RKGGRARGRS KGLTIDRVYT TEGVHPYDDV TWERRDVVQQ NWKTGETVFE
QRGVEFPDFW SANASTIVTT KYFRGAVGSE DREQSLKQLL DRVVLTYVKA GKDHGYFATE
SDAEVFEHEL TYMLLHQVFS FNSPVWFNVG TSSPQQVSAC FILAVDDSMD SILNWYKEEG
LIFKGGSGAG LNLSRIRSSK ELLRSSGGTA SGPVSFMRGA DASAGTIKSG GATRRAAKMV
VLDVDHPDVE EFVQTKAREE DKIRVLRDAG FDMDLGGDDI TSVQYQNANN SVRVTDEFMR
AVEDGTDFGL RARTTGEVID TVDAKKLFAD IAQAAWECAD PGLQYDTTIN DWHTTPETGR
ITASNPCSEY MHLDNSSCNL ASLNLLKFLQ DDGSFDSATF VKAVELIITA MDISICFADF
PTEAIGETTR KFRQLGIGYA NLGALLMASG LAYDSDGGRA LAASITSLMT GTSYRRSAEL
AGVVGPYDGF KQNAEPHARV MRKHQAANDA VRTMHAMDIA VHREATKQWA KGIEIGTKNG
WRNAQASVLA PTGTIGFMMD CDTTGIEPDF SLVKFKKLVG GGSMQIVNQT VPAALKKLGY
TTETIEAIVE YIAEHGHVID APGLKPEHYE VFDCAMGERA IKPMGHVRMM AATQPFLSGA
ISKTVNMPET ATVEEIQDIY FQGWKLGLKA LAVYRDNCKV GQPLSVEKKK SADADGRGAS
EASDRDPAEP EVKTVVIEKP TRKRLPKKRP SITQSFTVGG AEGYMTSGSY PDDGLGEVFL
KLGKQGSTLA GVMDAFSIAV SIGLQYGVPL ETYVQKFTNL KFEPAGLTDD PDVRMSQSIM
DYIFRRLALD YLPFDVRSQI GIYSAEERQR QLDTGSYLPA EDEEIPESES LKSSPAPDTD
RRGASEASDR DASVAELERE AQIDADDAEI MAESAKPAPR SAHTSAELLQ VISGTEVDAP
LCFTCGTKMR PAGSCHVCEG CGATSGCS
//
