ID A0A1X7LIL0_9BACL Unreviewed; 863 AA.
AC A0A1X7LIL0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=SAMN06295960_3443 {ECO:0000313|EMBL:SMG53102.1};
OS Paenibacillus aquistagni.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1852522 {ECO:0000313|EMBL:SMG53102.1, ECO:0000313|Proteomes:UP000193834};
RN [1] {ECO:0000313|EMBL:SMG53102.1, ECO:0000313|Proteomes:UP000193834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11 {ECO:0000313|EMBL:SMG53102.1,
RC ECO:0000313|Proteomes:UP000193834};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-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|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; FXAZ01000005; SMG53102.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7LIL0; -.
DR STRING; 1852522.SAMN06295960_3443; -.
DR Proteomes; UP000193834; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
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; 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; 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:UP000193834}.
FT DOMAIN 144..628
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 643..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 863 AA; 94813 MW; 8A30F006CDD2C389 CRC64;
MLNTGKQRLE GLSEKIFLDR YARKNADTSQ TKVGDIVLVL TKDDPKFPAK EVGEVIERRG
NTVSVKVRSG DIVESSVEKL TLTIEKTPEE MWDRLAQAMA SVEVPEKQAE WTDKFRYILD
DWKLVPGGRI AAGAGASDEL TLFNCYVIPS PKDSRGGIME TLSEMTEIMA RGGGVGINLS
SLRPRRAIVR GVNGTSSGSV SWGGLFSYTT GLIEQGGSRR GALMLMINDW HPDLEDFITV
KQTAGQVTNA NLSVCVSNGF MKAVKEDLDW ELVFPDTTDP EYDELWDGDL DKWKSLGKAV
IPYRTVRARD VWHTIIESAW KSAEPGVVFM EYYNQMSNSW YFNPIICTNP CGEQGLPAWG
VCNLSAINLS KFYDEDKHDV AWDELGKVTR YSVRFLDNVI DKTPYHFEKN KENQQTERRV
GLGSMGLAEL MIKLGIRYGS PESLEFLDKL YGFIARESYL ASSEIAGEKG SFKAFDAEKY
LMSGFMKNMV DRYPEVGESI REHGMRNVTV ITQAPTGSTG TMVGTSTGIE PYFAFKYFRQ
SRLGFDEQFV PIAQEWLDAH PGESLPDYYI TAMDLNAEDH IRVQAAIQRW VDSSISKTAN
APNDFTVEDT KSLYELAFDL GCKGVTIYRD GSRDTQVLTT EKKDAEKQEA AQPEPNAEPA
SEPASIAAAS EPAPAVVDLS ASSSGNAYLR RPQVLRGATY KINTPFGMAY ITINDYDHTP
AEIFLNVGKA GSDVFAMAEA LGRVCSLFLR YGDHGNKVEL LIKHLKGIGG SGAIGFGANR
VESIADAVAK ALETHIHETG SQPNGIDPAP IAATMEQVEP KAVTIGAKGS ADSRDLCPSC
GTASLLNVEG CKTCANCGYS RCN
//
