ID A0A316GNH8_9RHOB Unreviewed; 1224 AA.
AC A0A316GNH8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=C7455_101740 {ECO:0000313|EMBL:PWK62710.1};
OS Roseicyclus mahoneyensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseicyclus.
OX NCBI_TaxID=164332 {ECO:0000313|EMBL:PWK62710.1, ECO:0000313|Proteomes:UP000245708};
RN [1] {ECO:0000313|EMBL:PWK62710.1, ECO:0000313|Proteomes:UP000245708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16097 {ECO:0000313|EMBL:PWK62710.1,
RC ECO:0000313|Proteomes:UP000245708};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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:PWK62710.1}.
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DR EMBL; QGGW01000001; PWK62710.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316GNH8; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000245708; 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; -; 3.
DR InterPro; IPR013678; RNR_2_N.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR InterPro; IPR029072; YebC-like.
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; 2.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF75625; YebC-like; 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:UP000245708}.
FT DOMAIN 31..147
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 198..747
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 800..911
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1224 AA; 133505 MW; 83ADD08DE00CEF0F CRC64;
MKIERRFTRA GADVYADLDF TTTTSEIRNP DGTVVFKLEN VEVPLGWSQV ASDVIAQKYF
RKAGVPARLK PVREKGVPEF LWRQVADEQA LEALPQDARY VGEISAKQVF RRLAGAWAYW
GWKGGYFTSE SDAEAYFAEM QLMLARQMAA PNSPQWFNTG LHWAYGIDGP AQGHFYVDYK
TGKLTRSTSS YEHPQPHACF IQSVADDLVN DGGIMDLWVR EARLFKYGSG TGTNFSHLRG
EGEKLSGGGK SSGLMGFLKI GDRAAGAIKS GGTTRRAAKM VIVDADHPDI EAFIDWKVIE
EQKVASLVAG SKSHEKMLNG IFTAIREWDG SREAAVDPAQ NEALKKAIRA AKSASIPETY
VKRVLDYAKQ GYTSIEFPTY DTDWDSEAYS SVSGQNSNNS IRVTDNFLKA VERDEDWQLL
NRVGGKVAKT IKARELWDKV GHAAWACADP GIQFHDTVNA WHTCPEDGAI RGSNPCSEYM
FLDDTACNLA SMNLLTFHSG GKFDAESYIH ACRLWTLTLE ISVMMAQFPS KEIAQRSYDF
RTLGLGYANI GGLLMNMGLG YDSPEGRAMC GALTAIMTGV SYATSAEIAS ELGAFAGFAK
NREHMLRVIR NHRAAAYGKT DGYEGVNVNP VALDHANCPD QRLVALARQA WDEALALGEQ
HGYRNAQATV IAPTGTIGLV MDCDTTGIEP DFALVKFKKL AGGGYFKIIN QSVPGALETL
GYSSSQIEEI IAYAVGHGTL GQAPGINHTA LIGHGFGRTE IEKIEAALPS AFDIRFVFNQ
WTLGAEFCTK TLGIPADKLN DPTFEMLRHL GFTKPEIDAA NDHVCGTMTL EGAPFLKTDH
YHVFDCANPC GKKGKRYLGV DAHIYMMAAA QSFISGAISK TINMANHATI EDCQKAYELS
WSLGVKANAL YRDGSKLSQP LASALVEDDE DAQEVMESGT TMQKAQVIAE KIVEKIVIKE
VIKAHREKLP SRRKGYTQKA IVGGHKVYLR TGEYEDGNLG EIFIDMHKEG AGFRAMMNNF
AIAVSVGLQY GVPLEEFVDA FTFTKFEPSG MVQGNEAIKN ATSILDYIFR ELAVSYLDRT
DLAHVQPQGT SFDDVGRGAE EGVSNIREVP ESRASTPIEV LKQVASTGYL RKRAPQELMV
FQGGMDPVVT LETLIPEVRG GGTTIAAVAS TTAVTTGTVS MDAATRAKMQ GYEGEACGEC
GNYTLVRNGT CMKCNTCGGT SGCS
//
