ID A0A0P7ZL30_9EURY Unreviewed; 683 AA.
AC A0A0P7ZL30;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN Name=nrd {ECO:0000313|EMBL:KPQ44788.1};
GN ORFNames=MPEBLZ_00610 {ECO:0000313|EMBL:KPQ44788.1};
OS Candidatus Methanoperedens sp. BLZ1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Candidatus Methanoperedenaceae; Methanoperedens.
OX NCBI_TaxID=1719120 {ECO:0000313|EMBL:KPQ44788.1, ECO:0000313|Proteomes:UP000050360};
RN [1] {ECO:0000313|EMBL:KPQ44788.1, ECO:0000313|Proteomes:UP000050360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Arshad A., Speth D.R., De Graaf R.M., Op Den Camp H.J., Jetten M.S.,
RA Welte C.U.;
RT "A metagenomics-based metabolic model of nitrate-dependent anaerobic
RT oxidation of methane by Methanoperedens-like archaea.";
RL Submitted (SEP-2015) 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}.
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:KPQ44788.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LKCM01000055; KPQ44788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7ZL30; -.
DR PATRIC; fig|1719120.3.peg.669; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000050360; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR005144; ATP-cone_dom.
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 NCBIfam; TIGR02504; NrdJ_Z; 1.
DR PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR Pfam; PF03477; ATP-cone; 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.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
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|RuleBase:RU364064};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064}.
FT DOMAIN 6..97
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 683 AA; 76041 MW; EDD786015CD5FF03 CRC64;
MIFLPQKIRK RDGRIVDFDR AKIAKAIFKA FIATKSQDGE RTEDLAGQVV ELLDKRITGI
PGVEDVQDAV EEVLIKNGYT GIAKAYILYR EKRAQIRKAK EFFGVRDELK MSVNAVHVLE
RRYLLKDDKG EVLETPLQLF ERIAKAVALD PESEEEFLNI LVNLEFLPNT PTLMNAGTDI
GQLSACFVIP VEDSLTSIFD AVKSMALIQQ SGGGTGFSFS RIRPKGDIVK STQGVASGPV
SFMRVFDTTT DIIKQGGKRR GANMGILRAD HPDIIEFITA KTKEGFLTNF NISVAVDDKF
MNAVREDSDY ELINPRNRKV VKKVKAREIW NLIITMAWRT GDPGIIFIDE INRHNPTPHI
GEIESTNPCG ELPLLPYESC NLGSINLAKI VKNGSIDWEK LEKTVNIGVR FLDNIIDINK
YPLPQIEEIT KANRKIGLGV MGFADMLVQL GISYDSEEAL KTAEEVMGFI QEKSHISSER
LAQVRGAFPN FPGSIYKKPI RNSTVTTVAP TGTISIIGGC SSGIEPLFAV SFVRNVLEGT
KLIEVNPYFE SVAKERGFYS EELMMKIAKT GTLAGIKEIP DDVKRVFVTA FDIAPRWHVK
MQAAFQKYSD NAVSKTINFP NDVDIKEVET AFMLAYELKC KGITVYRYGS KSRQVLYLGD
SMDKYVSVDS EYSGGCAAQV CPV
//
