ID D3ILH8_9BACT Unreviewed; 854 AA.
AC D3ILH8;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=HMPREF0670_02297 {ECO:0000313|EMBL:EFC67651.1};
OS Prevotella sp. oral taxon 317 str. F0108.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=575615 {ECO:0000313|EMBL:EFC67651.1, ECO:0000313|Proteomes:UP000003829};
RN [1] {ECO:0000313|EMBL:EFC67651.1, ECO:0000313|Proteomes:UP000003829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0108 {ECO:0000313|EMBL:EFC67651.1,
RC ECO:0000313|Proteomes:UP000003829};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella sp. Oral Taxon 317 strain F0108.";
RL Submitted (NOV-2009) 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; GG740075; EFC67651.1; -; Genomic_DNA.
DR RefSeq; WP_009231391.1; NZ_GG740075.1.
DR AlphaFoldDB; D3ILH8; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_2_2_10; -.
DR Proteomes; UP000003829; 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 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:UP000003829}.
FT DOMAIN 23..87
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 105..637
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 854 AA; 96343 MW; 668BEF4F6D0B51D5 CRC64;
MENNKTYSYE EAFAAALDYF AGDELAARVW VNKYAMKDSF GNIYEKSPED MHWRIANEIA
RIEGKYPNPL SAQEVYELLD HFRYIVPAGS PMTGIGNGYQ VASLSNCFVV GLEGDADSYG
AILRIDEEQV QLMKRRGGVG HDLSHIRPKG SPVNNSALTS TGLVPFMERY SNSTREVAQD
GRRGALMLSV SIKHPDSEAF IDAKMTEGKV TGANVSVKID DSFMQAAVDD KPYVQQFPIE
GDNPEVKKEI SAKTLWEKIV HNAWQSAEPG VLFWDTILRE SIPDCYADLG FRTVSTNPCG
EIPLCPYDSC RLLCVNLFSY VVNPFTKEAY FDFDKFAKHV AVAQRIMDDI VDLELEKIDL
IMEKIKDDPQ NDEVKGAEYH LWEKIKRKSS MGRRTGVGIT AEGDMIAALG LRYGTQEATD
VSVSVHKRLA LAAYRSSVVM AKERGAFEIF DAKREAANPF ILRLKEADQS LYDDMVAYGR
RNIACLTIAP TGTTSLMTQT TSGIEPVFMP VYKRRRKVNP NDTDVHVDFV DEVGDSFEEY
IVYHKKFMDW MKANGFDTDK RYTQEEIDAI VEQSPYYKAT ANDVDWLMKV RMQGEIQKWV
DHSISVTVNL PNDVDEALVN RLYVEAWRSG CKGCTIYRDG SRSGVMISVS KKDKKKEDKQ
EEQPIVPCKQ PEVTEVRPKE LACDVVRFQN NKEKWVAFVG LLNGYPYEIF TGLQDDDEGI
ALPKSVTKGK IIKNIGPDGR SRYDFQFENK RGYKTTVEGL SEKFNPEYWN YAKLISGVLR
YRMPIDHVIK LVGSLQLKSE SINTWKIGVE RALKKYITDG TEATGMKCPS CGQESLVYQE
GCLICKNCGA SRCG
//
