ID A0A1H4P8V6_9RHOB Unreviewed; 781 AA.
AC A0A1H4P8V6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=SAMN05519105_1822 {ECO:0000313|EMBL:SEC03866.1};
OS Rhodobacter sp. 24-YEA-8.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1884310 {ECO:0000313|EMBL:SEC03866.1, ECO:0000313|Proteomes:UP000199640};
RN [1] {ECO:0000313|EMBL:SEC03866.1, ECO:0000313|Proteomes:UP000199640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=24-YEA-8 {ECO:0000313|EMBL:SEC03866.1,
RC ECO:0000313|Proteomes:UP000199640};
RA de Groot N.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; FNSK01000001; SEC03866.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4P8V6; -.
DR STRING; 1884310.SAMN05519105_1822; -.
DR Proteomes; UP000199640; 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:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
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 Pfam; PF00317; Ribonuc_red_lgN; 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 Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116};
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:UP000199640}.
FT DOMAIN 31..104
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 110..576
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 729..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 83593 MW; 18326E7FEF906CD9 CRC64;
MPDTEPDAAA ADRLTGPAAQ AGSVAQGGFA TPIAARIWDM KYRLKNADGM PIDLTVADSW
RRVARALAVD EPDPAGAEAR FMSALESFRF LPAGRILAGA GTDRAVTLFN CFVMGAIPDS
MEGIFQALKE AALTLQQGGG IGYDFSTIRP KGALVASVAA DASGPLSFMD VWDAMCRTIM
SAGARRGAMM AVLRCDHPDI LDFITAKQDP ARLRMFNLSV LVTDAFMAAV NADQSWELVF
GGTVYHSLPA RALWDRIMRA TYDYAEPGVI FIDRINRMNN LHYAEVISAT NPCGEQPLPP
YGACLLGSVN LAALVRDPFT EAARIAGDEL ADLVATAVRM LDNVIGQSRF PLPEQEAEAR
AKRRIGLGVT GLADALLMCG LRYGSDEAVV QTDAWLKALS RAAYLASVDL AKERGPFPLF
EADAFLAGGT MAAMDRDIRD AIRSHGIRNA LVTSIAPTGT ISLYAGNVSS GIEPVFAWST
RRRVLQKDGS AREEEVGDYA LMRWRALQGE APLPAHFVTA QELAPMDHLR MQAAAQRHID
SSISKTINCP ADIPFEAFRD VYLAAWDMGC KGCTTYRPNA VTGSVLSVAP APGDSETPRD
APLPRPATLS GETYKIRWPG SEHALYITVN DIVSGGRRRP FEVFINSKNM EHFAWTVALT
RMISAVFRRG GDVSFVVGEL KAVFDPRGGA WIDGRYIPSI LAAIGGVIER HLIATGFIAG
EGMGLNSDPG ALSPGEAPGS GMGTRAGEPG PQAICPSCGS FDLRREEGCL ICASCGFSQC
S
//
