ID A0A0S8II74_9BACT Unreviewed; 767 AA.
AC A0A0S8II74;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=AMJ95_11475 {ECO:0000313|EMBL:KPK97007.1};
OS Omnitrophica WOR_2 bacterium SM23_72.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1703777 {ECO:0000313|EMBL:KPK97007.1, ECO:0000313|Proteomes:UP000051899};
RN [1] {ECO:0000313|EMBL:KPK97007.1, ECO:0000313|Proteomes:UP000051899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_72 {ECO:0000313|EMBL:KPK97007.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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}.
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:KPK97007.1}.
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DR EMBL; LJUU01000064; KPK97007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8II74; -.
DR PATRIC; fig|1703777.3.peg.74; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000051899; 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 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; 1.
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 4..86
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 89..562
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 619..700
FT /note="TSCPD"
FT /evidence="ECO:0000259|Pfam:PF12637"
SQ SEQUENCE 767 AA; 84874 MW; 526325B7A774F4D3 CRC64;
MELKLSENAL KVLERRYLKK DESGKPIETP KQMFQRVALA IASAEKKYGK SDREMENLAE
DFYKMMASLE FMPNSPTLMN AGKELGQLSA CFTLPIDDSM ESIFETLKVT SLIHKSGGGT
GFSFSRLRPK NAVVRTTGGI ASGPVSFMKV YDAATEAVKQ GGSRRGANMG ILRVDHPDIL
EFITCKEDNK RITNFNISVA ITDDFMEKLE KGEDYDLIDP RTHKAVARLS SRKVFDLVVK
QAHKNGEPGI VFIDRINQFN PTPKLGNIES TNPCGEQPIL PYESCDLGSI NLALMVKKVG
SRYEIDWGRL KEVTHLGVHF LDNLIDVNKF PMPQIEKATK LTRKIGLGIM GWASLLIKLN
IPYNSDEAVA LAEKTMAFIL QEATRQSLEL GETKGVFPAF KGSIYDKKKE GGMRMRNATL
TTIAPTGTIS IIAGPTSSGI EPLFAISYYR NVMDNDKLVE VEPLFEEVAK CRGFYSRELM
EKIAEKSSIQ EIEEIPDDVK RVFVTSHDIS PEWHVRMQAA FQKHVHNATS KTINFPYEAT
VEDVRKAYLL AYELGCKGIT IYRDRSREEQ VLNVGNPIQN PGKTEQISVA LKKEIAPRPR
PEVIIGTTTK VSTGCGNLYV TINVDEEGTP FELFTQMGKA GGCAASQLEA IGRLVSLGFR
SGLEVKSIIE QLRNIRCPSP SWEKGQRIFS CADAIARVVE KRLVSKQVVK AALETTPIPM
KHSHDDEGAS SGLGGHADIV GVCPDCGGAL RHEEGCQRCH ACGYSKC
//
