ID B1XZE5_LEPCP Unreviewed; 1007 AA.
AC B1XZE5;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN OrderedLocusNames=Lcho_4257 {ECO:0000313|EMBL:ACB36508.1};
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB36508.1, ECO:0000313|Proteomes:UP000001693};
RN [1] {ECO:0000313|EMBL:ACB36508.1, ECO:0000313|Proteomes:UP000001693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC {ECO:0000313|Proteomes:UP000001693};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) 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 ---------------------------------------------------------------------------
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; CP001013; ACB36508.1; -; Genomic_DNA.
DR AlphaFoldDB; B1XZE5; -.
DR STRING; 395495.Lcho_4257; -.
DR KEGG; lch:Lcho_4257; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_2_0_4; -.
DR OMA; SYMRVFD; -.
DR Proteomes; UP000001693; Chromosome.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
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; -; 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:UP000001693}.
FT DOMAIN 35..102
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 108..600
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1007 AA; 108179 MW; 2A39109FEE4B9EB6 CRC64;
MNDLQRQDMS LFSDLAEARV NGASRGAARA LPEQPISAEV LIEKYAKGDE SSIEQVRRRV
AAALASVEAP EARELWTERF LAAQERGFVP AGRIASAAGT TLSATLINCF VQPVGDSIAE
PEEGFPGIYT ALTEAAETMR RGGGVGYDFS RIRPYGAWVG STQSHASGPV SYMRVFDRSC
ETVESAGSRR GAQMGVLRCD HPDVEAFIHA KDKGDLKNFN ISVGVTDVFM KAVEADTDVD
LVHKAEPGEK QKAAGARQRA DGLWVYRSVR ARDLWDQIMR STYDHAEPGV LFLDRINQDN
NLSYCETIAA TNPCAEQPLP PYGCCCLGSV DLTHFVQRPF ESDASFDDAA FAEVCATATR
MLDNVLDATV WPLPAQQQEA ANKRRVGLGF TGLGDALIML GLRYDTPAAR AMATHISEVM
RDAAYIASSD LAQERGAFPL FNADLYLSGN SFASRLPAAV KEHIRVNGLR NSHLLSIAPT
GTISLAFADN ASNGIEPPFS WTYTRKKREA DGTFKEFAVE DHAWRLYRHL KGADAPLTDA
FVTALEMSAE AHESMVAAVA PCIDTSISKT VNVPADYPYE DFQGLYMAAW KSGLKGLATY
RPNSVLGSVL SVTPTVPVVA ETAATPQPLT VPVSLGTPLD AGSANQRLRV DRLPQPVLAS
LRWPSRPDLS NGNPAWSYMI QHPHGDFALF VGELPAEAGP DAGLFDKTLP FEVWVNGAEQ
PRGLGALAKT LSMDMRANDP SWLKLKLDAL ATVAEERAFD MPFPPTGEKR LFPGVVAATA
AVIRWRCEQL GALQEGGPTP VLDAMFSRDE PRTGTDGTLA WAVDIHNPAT GEEFTLTLKE
VTLPTPEGGH VTRPCAIGFA GNYPRALDGL ARLLSLDMRV IDPAWIGMKL RKLLNVGEPL
GHFMAPIPGQ KRQQIWPSTV AYVARLVIHR YAMLGVLTEE GEPVSAMGVL AAPQRAVAAG
ASSGAAVSGA ASAPMAGSPC PECGNATMIH KDGCDFCTSC GFVGACG
//