ID A0A371JN88_9FLAO Unreviewed; 848 AA.
AC A0A371JN88;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=DX873_13595 {ECO:0000313|EMBL:RDY58709.1};
OS Allomuricauda nanhaiensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=2292706 {ECO:0000313|EMBL:RDY58709.1, ECO:0000313|Proteomes:UP000261828};
RN [1] {ECO:0000313|EMBL:RDY58709.1, ECO:0000313|Proteomes:UP000261828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM1704 {ECO:0000313|EMBL:RDY58709.1,
RC ECO:0000313|Proteomes:UP000261828};
RA Dang Y.;
RT "Muricauda nanhaiensis sp. nov., isolated from seawater of the South China
RT Sea.";
RL Submitted (AUG-2018) 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:RDY58709.1}.
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; QTJX01000003; RDY58709.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371JN88; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000261828; 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:UP000261828}.
FT DOMAIN 29..94
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 111..643
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 848 AA; 95807 MW; 29CEE724DD6BB86F CRC64;
MQNTKVRSHK KTYSQDEAFK ASLDYFNGDD LAAMVWVNKY ALKDSEGNIY EKTPDDMHNR
IAEEISRIEK KYPNPLTKKE VFDLIKNFRY IVPQGSPMAG IGNPFQIASL SNCFVIGTEG
KSDSYGAIMK IDQEQVQLMK RRGGVGHDLS HIRPKGSPVK NSALTSTGLV PFMERYSNST
REVAQDGRRG ALMLSASINH PDAEDFIDAK TEQGKVTGAN ISVRIDDGFM QAVESEGAYV
QKFPVFSEKP KVSKSIEAKP LWDKIVNNAW QSAEPGILFW DTISRESIPD CYADFGYRTV
STNPCGEIPL CPYDSCRLLA INLFSYVEQP FTKEATFNFE LFKKHVAFAQ RIMDDIIDLE
LEKIDAILDK INSDPELEET KAVELSLWNK IRHKAHEGRR TGIGITAEGD MLAALGLRYG
SEIANEFSVE VHKTIALEAY RASVETAKER GAFGIYDAEL EKDNPFIQRL RKADEKLYYE
MLEHGRRNIA LLTIAPTGTT SLMTQTTSGI EPVFLPVYKR RRKVNPNDRA AKVDFVDEVG
DSWEEYIVFH HRFKQWMEVQ GIATDKDYSQ EELDDLIKKS PYYRATSNDV DWLSKVHLQG
AVQKWVDHSI SVTINLPNDA SKELVGKLYL EAWKSGCKGV TVYRDGSRSG VLISADDKKE
EGKLNPFPTK RPQVLQADVV RFQNNKEKWI AFIGLIDDKP YEIFTGLADD EDGILLPRWV
TEGMIIKNRD EEGVSRYDFQ FKNKRGYKTT IEGLSHKFDP EYWNYAKLIS GTLRHGMPIE
NVVDVINSLQ LDSESINTWK NGVARALKRY VADGTLAKGQ KCDNCSSGNL IYQEGCLTCK
DCGSSKCG
//
