ID Q215K3_RHOPB Unreviewed; 1262 AA.
AC Q215K3;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|ARBA:ARBA00014409, ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU364064};
GN OrderedLocusNames=RPC_2380 {ECO:0000313|EMBL:ABD87933.1};
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD87933.1};
RN [1] {ECO:0000313|EMBL:ABD87933.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18 {ECO:0000313|EMBL:ABD87933.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-2006) 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|ARBA:ARBA00025437, 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 ---------------------------------------------------------------------------
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; CP000301; ABD87933.1; -; Genomic_DNA.
DR AlphaFoldDB; Q215K3; -.
DR STRING; 316056.RPC_2380; -.
DR KEGG; rpc:RPC_2380; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_0_1_5; -.
DR OrthoDB; 9762933at2; -.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 3.
DR InterPro; IPR013678; RNR_2_N.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR InterPro; IPR029072; YebC-like.
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; PF08471; Ribonuc_red_2_N; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF75625; YebC-like; 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 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 31..147
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 198..752
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 813..913
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1262 AA; 138799 MW; 865D2368F57F8380 CRC64;
MKIERRYTQD GQSPYAEIAF RLTTSEIRNP DGSVVFRLEN VEVPEFWSQV ASDVLAQKYF
RKAGVAARLK KVEEETVPSW LWRSVPDTEA LALLPENERF VSELSSKQVF DRLAGCWTYW
GWKGDYFSSE DDARAFNDEL RYMLAKQMVA PNSPQWFNTG LHWAYGVDGP GQGHFYVDWK
TGKLTKSKSA YEHPQPHACF IQGIQDDLVN EGGIMDLWVR EARLFKYGSG TGSNFSRLRG
EGEKLSGGGR SSGLMSFLKI GDRAAGAIKS GGTTRRAAKM VVVDADHPDI ETYIDWKVKE
EQKVAALVTG SKLNQKHLKA VLKACVNCEG SGDDCFDPEK NPALRREIKL ARRALVQDAM
IKRVIQYAKQ GYKEIDFPTY DTDWDSEAYL TVSGQNSNNS VSLKDDFLRA VETDGDWNLI
GRTNKKVMKT LKARDLWEKI GYAAWASADP GLHFNTTMND WHTCKASGDI RASNPCSEYM
FLDDTACNLA SANLLTMYDT TTNRFDVDAY EHLCRLWTVV LEVSVMMAQF PSKQIAELSY
EFRTLGLGFA NIGGLLMTMG LSYDSKEGRA LCGALSAIMT GTAYSTSAEM AQKLGPFPGY
KKNAGHMLRV IRNHRRAAHG ESRGYEGLAV NPVPLDHASC PQEDVVTHAK AAWDKALELG
EAHGYRNAQT TVVAPTGTIG LVMDCDTTGI EPDFALVKFK KLAGGGYWKI INRAVPAALR
ILGYPEHQIA EIEAYAVGHG SLSNAPAINV ATLKAKGFTD EALKKVEAAL PTAFDIKFAF
NKWTFGEEFL HDTLKLAPDL IAAPNFDLLA AIGFSKREIE AANIHICGAM TIEGAPHLKA
EHYAVFDCAN PCGKVGKRYL SVESHIRMMA ATQPFISGAI SKTINMPNDA TVDDCKSAYL
LSWKLALKAN ALYRDGSKLS QPLNSQLIAD EDDEDDGIDA FMEKPMAART AALSEKVVER
LVERIVVMRE REKMPDRRKG YTQKAVVGGH KVYLRTGEYD DGRIGEIFID MHKEGAALRS
FINNFAIAVS LGLQYGVPLE EYVDAFTFTR FEPAGPVQGN DSIKYATSIL DYVFRELAVS
YMGRFDLAHV DPRESHFDAL GKGIAEGKSP EPAQANKYLS KGLTRSRTDN LVVMRQAPAA
TPPATGGETA RSTSTAGVHS VTALGGTQAA HGARVADTLE GVTALKAEAD HDLSPTEKLE
ALQWSKANTA REQAKPSKSE RRAEAKAKGY EGEMCGECGH FSLVRNGTCM KCDTCGATTG
CS
//
