ID A0A1B1PUB9_9RHOB Unreviewed; 762 AA.
AC A0A1B1PUB9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=AYJ57_17340 {ECO:0000313|EMBL:ANT62191.1};
OS Salipiger sp. CCB-MM3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1792508 {ECO:0000313|EMBL:ANT62191.1, ECO:0000313|Proteomes:UP000092483};
RN [1] {ECO:0000313|EMBL:ANT62191.1, ECO:0000313|Proteomes:UP000092483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCB-MM3 {ECO:0000313|EMBL:ANT62191.1,
RC ECO:0000313|Proteomes:UP000092483};
RA Lau N.-S., Sam K.K., Abdullah A.A.-A., Chong A.S.-C.;
RT "Genome feautures of moderately halophilic polyhydroxyalkanoate-producing
RT Yangia sp. CCB-MM3.";
RL Submitted (FEB-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; CP014596; ANT62191.1; -; Genomic_DNA.
DR RefSeq; WP_066108880.1; NZ_CP014596.1.
DR AlphaFoldDB; A0A1B1PUB9; -.
DR STRING; 1792508.AYJ57_17340; -.
DR KEGG; yan:AYJ57_17340; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000092483; Chromosome 2.
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:UP000092483}.
FT DOMAIN 8..79
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 85..551
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 762 AA; 83311 MW; FCFC3F060B53A93F CRC64;
MTRFAAPIAE QIWDMKYRFK EADGTPIDQS VEDSWRRIAR ALASVETDAD AWEAKFYGAL
EDFQYLPAGR ITAGAGTARS VTLFNCFVMG TIPDSMSGIF DMLKEAALTM QQGGGIGYDF
STIRPKGAHV AGVAADASGP LSFMDVWDAM CRTIMSAGSR RGAMMATMRC DHPDVEQFIS
AKADSARLRM FNLSVLVTDP FMEAVKADGS WDLQFDGKVY HTVKARDLWN KIMKATYDYA
EPGVIFIDRI NKANNLSYIE QIAATNPCGE QPLPPYGACL LGSINLARLV DTPFETGAEI
PEAKLDELVA LAVRMMDNVV DASNFPLPQQ AEEAQNKRRI GLGVTGLADA LLMMGLRYGS
EEAAAQTESW LKRIARASYL ASVELAKEKG AFPLFDAEKF LASGNMEQMD DDVREAIRTH
GIRNALLTSI APTGTISLYA GNVSSGIEPV FAYAYTRKVL QKDGTRTEEE VVDYAVQMWR
DKFGDAELPD YFVNAQTLAP LEHVRMQAAA QKWIDSSISK TINCPEDISF EGFKDVYMEA
YETGCKGCTT YRPNDVTGSV LSVSESADKT PAESPSVATE TDEAGAEVVY MSEPLDRPQS
LEGHTYKLKW PDSEHAIYLT INDIIVGGHR RPFEVFINSK NMEHYAWTVA LTRMISAVFR
RGGDVSFVVE ELKAVFDPRG GAWVQGKYIP SILAAIGGVI EKHLIATGFL EGEGKGLKAD
PTAKVVGLDA PRGKACPSCG QFSMMMVEGC MTCSSCGHSK CG
//
