ID A0A369UWN1_9GAMM Unreviewed; 725 AA.
AC A0A369UWN1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=DVJ77_04255 {ECO:0000313|EMBL:RDD82739.1};
OS Dyella tabacisoli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=2282381 {ECO:0000313|EMBL:RDD82739.1, ECO:0000313|Proteomes:UP000253782};
RN [1] {ECO:0000313|EMBL:RDD82739.1, ECO:0000313|Proteomes:UP000253782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L4-6 {ECO:0000313|EMBL:RDD82739.1,
RC ECO:0000313|Proteomes:UP000253782};
RA Zhou X.-K., Li W.-J., Duan Y.-Q.;
RT "Dyella tabacisoli L4-6T, whole genome shotgun sequence.";
RL Submitted (JUL-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:RDD82739.1}.
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DR EMBL; QQAH01000003; RDD82739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369UWN1; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000253782; 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:UP000253782}.
FT DOMAIN 30..101
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 114..660
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 725 AA; 81065 MW; 337E7C5B79427BC5 CRC64;
MSIVRAQAVG SNQMGSDVSR EAAAAIPLQP ASYDIWDKKY RLKAKSGEPV DGSIDETYQR
VARALSEVEA TPELREHWFE RFLWALRRGA IPAGRITSNA GALAHKPATS TINCTVSGTI
RDSMDDILEK VHEAGLTLKA GCGIGYEFST LRPRGAYVSG AGAYTSGPLS FMDIYDKMCF
TVSSAGGRRG AQMGTFDVSH PDVKEFIRAK REDGRLRQFN LSLLITDGFM QAVEHDLDWP
LVFPVHVKEE DEIDLTDASK VVWREWPTHE NYVGRDDGLV ACKIYGHIRA RHLWDMIMVS
TYDYAEPGFI LIDKVNEMNN NWWCEHIRAT NPCGEQPLPP YGSCLLGSIN LTTFVRDPFG
PKARFDWDEY RDVVKIFTRM LDNVVEINGL PLPQQRDEIL SKRRHGMGFL GLGTTLTMLK
HRYGTAESVA FTEDVSREMA VAGWEVALDL AKEKGPAPIL SRDFTVTGEM LRKRPEMVSD
GYSIGDTIPG RVLHAKYSRY MQRIASIAPN LVAQLAETGA RFTHHSSIAP TGTISLSLAN
NASNGIEPSF AHHYSRNVIR EGRKTKEKVE VFSYELLAYR ALINADALPF STDTLTKLPD
YFVAADDISP KEHVDIQAAA QLWVDSSISK TANVPTDYPY EDFKDIYFYA YKQGLKGCTT
FRFNPAAFQG VLVKDSDLES TLYRFELEDG SVIELKGNEE VEYDGETHTA ANLFDALKEG
YYGKF
//
