ID A0A159YZH1_9RHOB Unreviewed; 755 AA.
AC A0A159YZH1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=AKL17_0651 {ECO:0000313|EMBL:AMY67911.1};
OS Frigidibacter mobilis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Frigidibacter.
OX NCBI_TaxID=1335048 {ECO:0000313|EMBL:AMY67911.1, ECO:0000313|Proteomes:UP000076128};
RN [1] {ECO:0000313|EMBL:AMY67911.1, ECO:0000313|Proteomes:UP000076128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cai42 {ECO:0000313|Proteomes:UP000076128};
RA Geng S., Pan X., Wu X.;
RT "Complete genome sequence of Defluviimonas alba cai42t isolated from an
RT oilfield in Xinjiang.";
RL Submitted (SEP-2015) 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; CP012661; AMY67911.1; -; Genomic_DNA.
DR RefSeq; WP_066809683.1; NZ_CP012661.1.
DR AlphaFoldDB; A0A159YZH1; -.
DR STRING; 1335048.AKL17_0651; -.
DR KEGG; daa:AKL17_0651; -.
DR PATRIC; fig|1335048.3.peg.676; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000076128; Chromosome.
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}.
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 755 AA; 83084 MW; E25B338BA6BDAE30 CRC64;
MTRFAAPIAE QIWDMKYRLK EADGTPVDQS VDDTWRRIAR SLAAVEAEPE LWEGRFYSAL
EDFKYLPAGR IIAGAGTARS VTLFNCFVMG TIPDSMGGIF DMLKEAALTM QQGGGIGYDF
STIRPRGAEV HGVAADASGP LSFMDVWDAM CRTIMSAGSR RGAMMATMRC DHPDVEQFIE
AKQDAARLRM FNLSVLITDP FMEAVKADGS WDLQFKGRIY RTVQARDLWN KIMQATYDFA
EPGVIFIDRI NRMNNLGYAE TIAATNPCGE QPLPPYGACL LGSINMARLV RNPFEAGADL
DPEALDDLVR LSIRMMDNVV DASRFPLPQQ AEEARAKRRI GLGVTGLADA LLMTGLRYGS
EEAAAQTEAW MKRIARAAYL ASVDLAREKG AFPLFDAEKY LASGNMMQMD EDVREAVRTH
GIRNALLTSI APTGTISLYA GNVSSGIEPV FAYAYKRKVL QKDGSRTEEE VVDYAVKLWR
DKFGDAPLPD YFVNAQTLPP LDHVRMQAAA QKWIDSSISK TINCPEDIDV EAFKDVYMAA
WDQGCKGCTT YRPNAVTGSV LSVSESTESA PEVDQGAEVV YLTEPLDRPQ SLEGATYKLK
WPDSEHAIYI TINDIVQGTR RRPFEVFINS KNMEHFAWTV ALTRMISAVF RRGGDVSFVV
EELKAVFDPR GGAWMQGRYV PSILAAIGGV IERHMIATGF LAGEGMGLKS DPQAERMVAG
GEAPRGKACP SCGSYALRMV EGCMTCADCG FSKCS
//
