(data stored in ACNUC7421 zone)

SWISSPROT: A0LEV8_SYNFM

ID   A0LEV8_SYNFM            Unreviewed;       728 AA.
AC   A0LEV8;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 78.
DE   RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE            EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN   OrderedLocusNames=Sfum_0259 {ECO:0000313|EMBL:ABK15960.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK15960.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK15960.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
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., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-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
CC       limitation and/or for immediate growth after restoration of
CC       oxygen. {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,
CC         Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:57930, ChEBI:CHEBI:73316;
CC         EC=1.17.4.1; Evidence={ECO:0000256|RuleBase:RU364064};
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000256|RuleBase:RU364064};
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase
CC       class-2 family. {ECO:0000256|RuleBase:RU364064}.
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DR   EMBL; CP000478; ABK15960.1; -; Genomic_DNA.
DR   RefSeq; WP_011697133.1; NC_008554.1.
DR   STRING; 335543.Sfum_0259; -.
DR   EnsemblBacteria; ABK15960; ABK15960; Sfum_0259.
DR   KEGG; sfu:Sfum_0259; -.
DR   eggNOG; ENOG4105BZH; Bacteria.
DR   eggNOG; COG0209; LUCA.
DR   HOGENOM; HOG000229277; -.
DR   KO; K00525; -.
DR   OMA; LEIWHID; -.
DR   OrthoDB; 357568at2; -.
DR   BioCyc; SFUM335543:G1G7I-262-MONOMER; -.
DR   Proteomes; UP000001784; Chromosome.
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: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   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013509; RNR_lsu_N.
DR   InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR   InterPro; IPR008926; RNR_R1-su_N.
DR   InterPro; IPR024434; TSCPD_dom.
DR   Pfam; PF02867; Ribonuc_red_lgC; 1.
DR   Pfam; PF00317; Ribonuc_red_lgN; 1.
DR   Pfam; PF12637; TSCPD; 1.
DR   PRINTS; PR01183; RIBORDTASEM1.
DR   SUPFAM; SSF48168; SSF48168; 1.
DR   TIGRFAMs; TIGR02504; NrdJ_Z; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0LEV8.
DR   SWISS-2DPAGE; A0LEV8.
KW   Cobalamin {ECO:0000256|RuleBase:RU364064};
KW   Cobalt {ECO:0000256|RuleBase:RU364064};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   DNA synthesis {ECO:0000256|RuleBase:RU364064};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364064};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364064};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784}.
FT   DOMAIN       12     92       Ribonuc_red_lgN. {ECO:0000259|Pfam:
FT                                PF00317}.
FT   DOMAIN       95    561       RIBORED_LARGE. {ECO:0000259|Pfam:
FT                                PF02867}.
FT   DOMAIN      599    686       TSCPD. {ECO:0000259|Pfam:PF12637}.
SQ   SEQUENCE   728 AA;  80323 MW;  71D5B6A0BC2CAA94 CRC64;
     MTLVKKEHPL RMTPNALVVL RKRYLEKDDE GKPIETPEEL FWRVARTIAQ ADVAFQGPEK
     AEETADRFYA LMTSLDFIPN SPTLMNAGRP LGQLSACFVL PVEDSIDSIF EAIKHAAMIH
     KSGGGTGFSF SRIRPENDKV LSTQGVASGP VSFMSVFDTA TETIKQGGTR RGANMGILRV
     DHPDIEKFIT CKTDNDRMTN FNISIAVTDS FMKAVEEDAE YELISPRTRE RVQSLSARKV
     FDEITQSAWR NGEPGIIFLD VMNRHNPTPH VGEIESTNPC GEQPLLPYES CNLGSINLAS
     MHRDGNIDYE HLKEVVWDAV HFLDNVIEVN NYPLQIIEDM TRGNRKIGLG VMGFSDLLIS
     LGVPYNSEAA VETAEKVMSF IQQESKAASA HYGKERGNFV NYAGSIYERP ETPHMRNATT
     TTIAPTGTIS IIAGCSSGIE PLFAISFVRK VLDGQELVEV HPLFQKVARE RGFYSDDLMK
     KIAEKGSIKN FLEIPADVRN VFVTSHDVTP DWHIRIQAAF QKHTDNAVSK TINFPFSATP
     EDVSSAYLQA YKLGCKGLTI YRDGSRDVQV LNIQRKPQYP QVEPRPRPDR TTGITERVNT
     GCGKLYVTIN SDEYGFCEVF AQMGKAGGCA YSQIEATSRL ISLALRSGVK VEAVIRQLVG
     IRCPSPTWGN GEQVVSCSDA IAKVLNRHAH ANVTSVGDEM GACPDCGAAV EHEGGCIVCR
     SCGFSRCS
//

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