ID Q07NP5_RHOP5 Unreviewed; 1255 AA.
AC Q07NP5;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
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=RPE_2501 {ECO:0000313|EMBL:ABJ06439.1};
OS Rhodopseudomonas palustris (strain BisA53).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316055 {ECO:0000313|EMBL:ABJ06439.1};
RN [1] {ECO:0000313|EMBL:ABJ06439.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisA53 {ECO:0000313|EMBL:ABJ06439.1};
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., Kim E., Harwood C.S., Oda Y.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL Submitted (SEP-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}.
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DR EMBL; CP000463; ABJ06439.1; -; Genomic_DNA.
DR AlphaFoldDB; Q07NP5; -.
DR STRING; 316055.RPE_2501; -.
DR KEGG; rpe:RPE_2501; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_0_1_5; -.
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 35..151
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 202..757
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 816..917
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1255 AA; 138299 MW; FCB2EC5D06F748C9 CRC64;
MGTTMQIERR YTTDGQSPYA EIEFRLTTSE IRNPDGSVVF RLENVEVPDT WSQVASDVLA
QKYFRKAGVA ARLKKVEEET VPSWLWRSVP DTEALAELPE NERFVSEHSS KQVFDRLAGC
WTYWAWKGSY FTDEASARAF HDELRFMLAK QMVAPNSPQW FNTGLHWAYG VDGPGQGHYY
VDWKTGKLTK SKSAYEHPQP HACFIQGIQD DLVNEGGIMD LWVREARLFK YGSGTGSNFS
RLRGEGERLS GGGRSSGLMS FLKIGDRAAG AIKSGGTTRR AAKMVVVDVD HPDIEAYIDW
KVKEEQKVAA LVTGSKINQK HLKAVLKACV NCEGSGDDCF DPEKNPALRR EIKLARRALV
TDNMIKRVIQ YAKQGYKEID FPIYDTDWDS EAYLTVSGQN SNNSVSLKDD FLRAVETDGD
WNLTARTSKK VMKTIKARDL WEKIGTAAWA SADPGLHFNT TMNDWHTCKA SGDIRASNPC
SEYMFLDDTA CNLASANLLT FYDIEAKRFD VDAYEHLCRL WTVVLEVSVM MAQFPSKQIA
ELSYEFRTLG LGFANIGGLL MTMGLSYDSK EGRALCGGLT AIMTGVSYAT SAEMAQKLGP
FPGYKKNASH MLRVIRNHRR AAHGESRGYE ALAVAPVPLD HASCPQPEII THAKAAWDRA
LELGELHGYR NAQTTVVAPT GTIGLVMDCD TTGIEPDFAL VKFKKLAGGG YWKIINRAVP
AALRVMGYPE SQIAEIEAYA VGHGSLSNAP AINHSTLKAK GFTDEALKKV EAALPTAFDI
KFAFNKWTFG EEFLHDALKL EPEAIAAPNF DLLAAIGFSK REIEAANIHI CGAMTVEGAP
HLKAEHYAVF DCANPCGKIG KRYLSVESHI RMMAAAQPFI SGAISKTINM PNDATVEDCK
SAYLLSWKLA LKANALYRDG SKLSQPLNSQ LISDDDEDDD AIESFLEKPM AARTAALSEK
VVERLVERIV VMREREKMPD RRKGYTQKAV VGGHKVYLRT GEYDDGRIGE IFIDMHKEGA
ALRSFINNFA IAVSLGLQYG VPLEEYVDAF TFTRFEPAGP VQGNDSIKYA TSILDYVFRE
LAVSYMGRFD LAHVDPRESG FDALGKGVDE GRSPEQPAQA NKYLSKGLTR SRTDNLVVMR
TPAGPDGAPR AISTANVTAL GGAHTSRVAD QIEGVTALKQ EADHDLSPTE KLEALQWSKA
ATAREQAAPS KAERRAEAKA KGYEGEMCGE CGNFTLVRNG TCMKCDTCGS TTGCS
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