ID I4VN57_9GAMM Unreviewed; 1077 AA.
AC I4VN57;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN ORFNames=UU9_11893 {ECO:0000313|EMBL:EIL88648.1};
OS Rhodanobacter fulvus Jip2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1163408 {ECO:0000313|EMBL:EIL88648.1, ECO:0000313|Proteomes:UP000004210};
RN [1] {ECO:0000313|EMBL:EIL88648.1, ECO:0000313|Proteomes:UP000004210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jip2T {ECO:0000313|Proteomes:UP000004210};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
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|RuleBase:RU003410};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|RuleBase:RU003410}.
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:EIL88648.1}.
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DR EMBL; AJXU01000048; EIL88648.1; -; Genomic_DNA.
DR AlphaFoldDB; I4VN57; -.
DR STRING; 1163408.UU9_11893; -.
DR PATRIC; fig|1163408.3.peg.2430; -.
DR eggNOG; COG0209; Bacteria.
DR eggNOG; COG1372; Bacteria.
DR Proteomes; UP000004210; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:InterPro.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR CDD; cd00081; Hint; 1.
DR Gene3D; 3.20.70.20; -; 2.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
DR Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR NCBIfam; TIGR01445; intein_Nterm; 1.
DR PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR SUPFAM; SSF55608; Homing endonucleases; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW Reference proteome {ECO:0000313|Proteomes:UP000004210}.
FT DOMAIN 426..576
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
SQ SEQUENCE 1077 AA; 120377 MW; D981CD400E5890A7 CRC64;
MEIPLQPASQ DIWDKKYRLK NKSGEPVDAD VDGTWQRVAR ALSDVETTPE LREHWYERFL
WALRRGAIPA GRITSNAGAL AHKPATSTIN CTVSGTIRDS MDDILEKVHQ AGLTLKAGCG
IGYEFSTLRP RGAYVSGAGA YTSGPLSFMD IYDKMCFTVS SAGGRRGAQM GTFDISHPDA
KEFIRAKRED GRLRQFNLSL LITDGFMQAV EHDQDWPLVF PVHVKEKDEI DLADPTKVVW
REWPIHENYV DREDGLVACK IYGTIRARHL WDMIMVSTYD YAEPGFILID KVNEMNNNWW
CEHIRATNPC VTADTRLATQ HGMVPIGELY ANGAPLNVSV DRRSLELEGR GVETRPAKPA
FMTAPRAPVF KVTTEDGYEI KATEWHDFYV ERGKIKLRDL KVGDRMLVQS GKGQFGQQGS
EDLGLLLGMI TGDGHFTNRG KDQQAAIVSL WGEERALADR VATYINTLIA HTATGDLRQY
KVSPVAVPER NHVFIRSVLL ARLLEHYGFS AATKLRVPAV VWRGSEACVK SYLRALFQCD
GTVNVSGRSQ SCSVRLASSQ PDLLRDVQML LANFGVFCRI KQRRVAGTRK LPDGHGGSRA
YACSADHELI IDGESRERFM DEIGFLLPIK TQRYLDWREG KALRKTQRFA SKISSIEYVG
EEAVFDTTQP DHNAVIFNGL VTGQCGEQPL PPYGSCLLGS INLTTFVRDP FGPKARFDWD
EYRDVVKVFT RMLDNVVEIN GLPLEQQRNE IMGKRRHGMG FLGLGSTLTM LKHRYGTADA
VAFTEEVSRE LAVAGWEVAL ELAKEKGPAP VLAQEFTVTG DMLRKRPEMV ADGYKVGDAI
PGRVLHAKYS RYMQRIATVA PELVNALAET GARFTHHSSI APTGTISLSL ANNASNGIEP
SFAHSYSRNV IREGKKSKER VEVLSYELLA YRALINADAK PFAEEAENKL PAYFVAADDI
SPKEHVDIQA ASQKWIDSSI SKTANVPTDY PYEDFKDIYF YAYKQGLKGC TTFRFNPAAF
QGVLVKESDL ENTLYRFELE DGSVMELKGN EQVEYDGEMH SAANLFDALK EGYYGKF
//
