ID A0A2N3PLZ8_9PROT Unreviewed; 1206 AA.
AC A0A2N3PLZ8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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 ORFNames=CWS72_26845 {ECO:0000313|EMBL:PKU21421.1};
OS Telmatospirillum siberiense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Telmatospirillum.
OX NCBI_TaxID=382514 {ECO:0000313|EMBL:PKU21421.1, ECO:0000313|Proteomes:UP000233293};
RN [1] {ECO:0000313|Proteomes:UP000233293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=26-4b1 {ECO:0000313|Proteomes:UP000233293};
RA Hausmann B., Pjevac P., Schreck K., Herbold C.W., Daims H., Wagner M.,
RA Pester M., Loy A.;
RT "Draft genome sequence of Telmatospirillum siberiense 26-4b1T, an
RT acidotolerant peatland alphaproteobacterium potentially involved in sulfur
RT cycling.";
RL Submitted (DEC-2017) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKU21421.1}.
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DR EMBL; PIUM01000061; PKU21421.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3PLZ8; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000233293; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000233293}.
FT DOMAIN 31..140
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 191..744
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 825..907
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1206 AA; 131165 MW; 1B5C8324CE6D7F48 CRC64;
MRIERHFTSP GRDAYDGIGF RTTKSEIRNP DGSVVFSQSD IDVPESWSQV ACDVLAQKYF
RRAGVPVALT PVPEEDVPEW LWRKQPAEAD TKTSGETSAR QVFDRMAGTW TYWGWKGGYF
DGEEDAQTFY DEMRYMLCQQ MGAPNSPQWF NTGLHWAYGI DGPSQGHHYV DYRTGQLTKS
ASAYEHPQPH ACFIQSVSDD LVNEGGIMDL WVREARLFKY GSGTGSNFSA LRGDGERLSG
GGRSSGLMSF LKIGDRAAGA IKSGGTTRRA AKMVVVDVDH PDIESFIGWK VMEEQKVAAL
VAGSKLADQT LSAVMAACRA WDGAADSDDR WNPKVNKQLK KAIIAARKAM IPENYVQRVI
TFARQGYTEV KFPVFNTDWD SEAYLTVSGQ NSNNSVRITN AFLQKVLDDG DWELIRRIDG
KVAKTIKARD LWEQIAEAAW SCADPGLQFD TTINEWHTCP ESGRINASNP CSEYMFLDDT
ACNLASLNLI AFRQADDGFD VEGFQHAVRL WTVVLEISVL MAQFPAEKIA ELSYRFRTLG
LGFANIGGLL MASGLAYDSD AGRAYCAAIT ALMTGASYAT SGEMARELGA FPGFPENAEA
MRRVIRNHRR AAYGLTSEYE ELSIPPVPLD AANCPDESLV IAARAAWDEA LRLGEEFGFR
NAQVSVIAPT GTIGLVMDCD TTGIEPDFAL VKFKKLAGGG YFKIINRMVP QALETLGYGA
KDIEEIIRYA VGHGTLKGAP SINHASLAAK GFDAATLEKV EAAVANAFDI KFAFNKYTLG
ESFCTDVLKI PAARLDDVGF DLLAAIGFPR AEIDAANTFV AGAMTLEGAP FLKALHLPIF
DCASPCGKLG KRFLSVTSHI KMMAAAQPFI SGAISKTINM PNSATVEECK EAYLASWRLG
LKANALYRDG SKLSQPLQAS LLDDDGELAD ELAAQPAAAA RTEIVAERIV ERIIAAARRK
LPDRRKGYTQ KAIVGGHKVY LRTGEYEDGK LGEIFIDMHK EGAAFRAMMN NFAIAISIGL
QYGVPLEEFV EAFTFTRFEP SGMVEGNSVI KMSTSILDYV FRELAISYLS RNDLAHVTPP
DLTPDSLGRG NSEGNLPNAG LGAVVERFTS RGYVRSNLMV LKGGSQSTAA VASAGGGTGA
ASAERAVPVA ISETLVREFD VRSEQIREAR LKGYEGDACG ECGNFTLVRN GTCMKCNTCG
STSGCS
//
