ID A0A1C4NL96_9ACTN Unreviewed; 966 AA.
AC A0A1C4NL96;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=GA0115240_13456 {ECO:0000313|EMBL:SCD98765.1};
OS Streptomyces sp. DvalAA-14.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1839759 {ECO:0000313|EMBL:SCD98765.1, ECO:0000313|Proteomes:UP000199020};
RN [1] {ECO:0000313|EMBL:SCD98765.1, ECO:0000313|Proteomes:UP000199020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DvalAA-14 {ECO:0000313|EMBL:SCD98765.1,
RC ECO:0000313|Proteomes:UP000199020};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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; FMCH01000318; SCD98765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4NL96; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000199020; 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; -; 1.
DR InterPro; IPR013678; RNR_2_N.
DR InterPro; IPR000788; RNR_lg_C.
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; PF08471; Ribonuc_red_2_N; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 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 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:UP000199020}.
FT DOMAIN 54..137
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 158..697
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 104641 MW; D5C8354BA5C59CEE CRC64;
MTETTSGPAR GSRTKGSKAG KGLRIERIHT TPGVHPYDEV VWEHRDVVMT NWRDGSVNFE
QRGVEFPDFW SVNAVNIVTS KYFRGAVGGP QREKSLKQLI DRVVRTYRAA GEEHGYFSSP
ADAEIFDHEL TYALLHQVFS FNSPVWFNVG TAQPQQVSAC FILSVDDSMD SILDWYKEEG
MIFKGGSGAG LNLSRIRSSK ELLSSGGNAS GPVSFMRGAD ASAGTIKSGG ATRRAAKMVV
LDVDHPDVEA FIETKVKEEE KIRALRDAGF DMDLGGDDIT SVQYQNANNS VRVNDEFMKA
YEAGSPFGLR ARMTGEVIEE VDARGLFRKL AEAAWACADP GIQYDDTINH WHTSPETGRI
TASNPCSEYM HLDNSSCNLA SLNLMKFLRQ DDSGHQTFEA ERFAKVVELV ITAMDISICF
ADFPTEKIGE TTRAFRQLGI GYANLGALLM ATGHAYDSDG GRGLAGAITS LMTGTSYRRS
AELASVVGAY DGYARNADAH KRVMRQHSDA NTAAKRVDDL DTPVWAAATE AWQDVLRLGE
KNGFRNAQAS VLAPTGTIGL MMDCDTTGVE PDLALVKFKK LVGGGSMQIV NNTVPAALKR
LGYQPEQVEA IVAHIAEHGH VIDAPGLKHE HYSVFDCAMG ERAISAMGHV RMMAAAQPFL
SGAISKTVNL PESATVEEVE EVYFEGWKLG LKALAIYRDN CKVGQPLSAK KKGSQQAGTE
AAVQAPAAVP AAVEKVVEYR PVRKRLPKGR PGITTSFTVG GAEGYMTANS YPDDGLGEVF
LKMSKQGSTL AGMMDAFSIA VSVGMQYGVP LETYVSKFTN MRFEPAGLTD DPDVRMAQSI
VDYIFRRLAL DFLPFETRSA LGIHSAPERQ RHLDTGSYEP TDEEMDVEGL AQSAPRESEA
ARPPLSVAKP EAAVPAPKEA HSSTELLEIQ LGLNADAPLC FSCGTKMRRA GSCYVCEGCG
STSGCS
//
