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Database: UniProt
Entry: B1XZE5_LEPCP
LinkDB: B1XZE5_LEPCP
Original site: B1XZE5_LEPCP 
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}.
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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
//
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