ID G2MX24_9THEO Unreviewed; 770 AA.
AC G2MX24;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=Thewi_2302 {ECO:0000313|EMBL:AEM79650.1};
OS Thermoanaerobacter wiegelii Rt8.B1.
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=697303 {ECO:0000313|EMBL:AEM79650.1, ECO:0000313|Proteomes:UP000008276};
RN [1] {ECO:0000313|EMBL:AEM79650.1, ECO:0000313|Proteomes:UP000008276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rt8.B1 {ECO:0000313|EMBL:AEM79650.1,
RC ECO:0000313|Proteomes:UP000008276};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Zeytun A., Daligault H., Detter J.C., Han C.,
RA Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Hemme C.,
RA Woyke T.;
RT "Complete sequence of Thermoanaerobacter wiegelii Rt8.B1.";
RL Submitted (AUG-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; CP002991; AEM79650.1; -; Genomic_DNA.
DR RefSeq; WP_014063507.1; NC_015958.1.
DR AlphaFoldDB; G2MX24; -.
DR STRING; 697303.Thewi_2302; -.
DR KEGG; twi:Thewi_2302; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_2_0_9; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000008276; 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; cd20336; Rcat_RBR; 1.
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 InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR024434; TSCPD_dom.
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; 2.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR Pfam; PF12637; TSCPD; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 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}.
FT DOMAIN 2..83
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 86..405
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 409..555
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 612..695
FT /note="TSCPD"
FT /evidence="ECO:0000259|Pfam:PF12637"
FT REGION 577..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 770 AA; 85962 MW; 5C46E4C3C0B8675E CRC64;
MKITENARKV LERRYLAKDE NGKPIETVEE MFERVAKTIA EVDLIYDKNA DVEAVKKRFY
DMMVALDFLP NSPTLMNAGR PLGQLSACFV LPVGDSMEEI FDAVKYAAII HKSGGGTGFS
FSRLRPKGAT VRSTGGVASG PVSFMKVFNA ATEAVKQGGT RRGANMGILR VDHPDILEFI
QCKKDNNEIT NFNISVAITE EFMKAVEEDR EYDLIDPHTG KVVNRLRARE VFDLIVEMAW
RNGEPGIVFL DRINEKNPTP EVGEIESTNP CGEQPLLPYE SCNLGSINLE NMLKKVEGRY
AIDYDKLRET VYDAVHFLDN VIDANKYPLP QIEEMTKGTR KIGLGVMGFA NMLLRLGIPY
DSEEAVELGE ELMEFIDETS KEASIKLAEQ RGTFGFYDKS IYKKMGIKIR NATTTTIAPT
GTISIIAGTS SGIEPVFAIA MTRNVMDNTE LVEVNPVFKE VAIERGFYSE ELMREIARRG
SLKDIKGIPE DVKRVFVIAH DIDPEWHVKM QAAFQKHVDN AVSKTVNFRN EATVEDVRRT
YLLAYELGCK GVTIYRDGSR ESQVLNLGIK EKKVETKPIE EQTKNEPLRP RPRPPVTRGI
TEKVRIGCGN LYITVNYDDQ GICEVFTNLG RAGGCPSQSE ATSRLISIAL RSGIDAKTIV
EQLKGIRCHS TLRQMATNKE IKVLSCPDAI GKVIEKVMKI RVEEEQQFAP IDVPIYENNH
NGDEDDPKEE VALSEADLLD EEKFCPECGS PIEHEGGCVV CKNCGYSKCG
//
