ID   A0A1H1HR94_9BURK        Unreviewed;       868 AA.
AC   A0A1H1HR94;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE            EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN   ORFNames=SAMN05443245_4205 {ECO:0000313|EMBL:SDR27980.1};
OS   Paraburkholderia fungorum.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=134537 {ECO:0000313|EMBL:SDR27980.1, ECO:0000313|Proteomes:UP000183487};
RN   [1] {ECO:0000313|Proteomes:UP000183487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAS106B {ECO:0000313|Proteomes:UP000183487};
RA   Varghese N.;
RL   Submitted (OCT-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|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; FNKP01000002; SDR27980.1; -; Genomic_DNA.
DR   RefSeq; WP_074768228.1; NZ_FNKP01000002.1.
DR   AlphaFoldDB; A0A1H1HR94; -.
DR   OrthoDB; 9762933at2; -.
DR   Proteomes; UP000183487; Unassembled WGS sequence.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
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; 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; 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}.
FT   DOMAIN          109..608
FT                   /note="Ribonucleotide reductase large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02867"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   868 AA;  95146 MW;  74B29F0461BDE713 CRC64;
     MAEDTPSTRA ATPAVAAPSA QSAPITPPAP LVAPQQFSVD VLLEKYAKGD EQSADDVFQR
     VARGVAQAEP AALRESVEAL FADNLRHGAL GAGRIMSAAG TGIAATLINC FVQPVGDAIQ
     GVDEQGLPGI YVALLQAAET MRRGGGVGYN FSAIRPKGAR VRTTSSSASG PCSYMDVFDA
     SCRTVESAGS RRGAQMAVLD CNHPDLLEFI EAKHSKGRWN NFNVSVGVTD EFMRAVEEDQ
     PWQLVHRAEP SPAMRSADDV RQREDGLWVY GERPAREIWD RIMRSTYDVA EPGIVFISRM
     NEDNNLRAVE TIRATNPCGE QPLPAYGCCN LGPLNLTRFV IDPFAQMQGR QASFDWDGLA
     KRTRTQVRFL DNVLDVTLWP LQQQHDESRA KRRIGVGFTG LGDTLVMLGL RYNSQEGRDF
     AVRIAKLMRD EAYRASVELA KERGAFALFD AERYLEAGTF ASRLPEDIKQ AIRRDGIRNS
     HLLSIAPTGT VSLAFADNAS NGIEPAFSWT YTRMKVMADG GRESFDVEDY AYRLYRELGG
     NVDKLPDYFV SALQMSARDH LEMMAAVQPY VDTSISKTVN VPADYPFHAF ESLYFDAWKS
     GLKGLATYRP NETLGAVLSV SPPQQTSDDT LADTDLDPLR IAIDHRPKGE LPAIIEKVEY
     LTQAGKKSLY VAVSFIEVTG RLGGEDVTIE RPIEFFIPTG QRDESQQWIT ATMRSLSLAA
     RGGFVGRNLQ DMRKVSWDRG QVRLGEVQRL DGHRTPRWHD SEVAALAFAI QQILHRRGFL
     DAEGNQLPSR VLARLPRGQM KAESALPADF GIRPFPSEAD ARAVTQSEGA SGMHVMLGRK
     CGSCGANAVI RKDGCDFCTA CGEVGACG
//