ID A0A0X3TKB1_9RHOB Unreviewed; 761 AA.
AC A0A0X3TKB1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=AVO45_12980 {ECO:0000313|EMBL:KUJ76222.1};
OS Ruegeria marisrubri.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1685379 {ECO:0000313|EMBL:KUJ76222.1, ECO:0000313|Proteomes:UP000053791};
RN [1] {ECO:0000313|EMBL:KUJ76222.1, ECO:0000313|Proteomes:UP000053791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZGT118 {ECO:0000313|EMBL:KUJ76222.1,
RC ECO:0000313|Proteomes:UP000053791};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUJ76222.1}.
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DR EMBL; LQBQ01000036; KUJ76222.1; -; Genomic_DNA.
DR RefSeq; WP_068349029.1; NZ_LQBQ01000036.1.
DR AlphaFoldDB; A0A0X3TKB1; -.
DR STRING; 1685379.AVO45_12980; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000053791; 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:UP000053791}.
FT DOMAIN 8..80
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 761 AA; 84079 MW; 7B8018795C844FCC CRC64;
MSRFAAPIAE QIWDMKYRFK KADGSPIDLT VEDTWRRIAR DLARIEQDPD HWEEKFYEAL
EDFKFLPAGR ITAGAGTARQ VTLFNCFVMG TIPDSMGGIF DMLKEAALTM QQGGGIGYDF
STIRPRGADV HGVAADASGP LSFMDVWDAM CRTIMSAGSR RGAMMATMRC DHPDIEQFIT
AKSDPARLRM FNMSVLVTDA FMDAVKADGP WELVFDGKVY HTVQARDLWN KIMQATYDYA
EPGVIFIDRI NQANNLSYCE TIAATNPCGE QPLPPYGACL LGSINLTRLV ADPFEKGARL
DLDALKELVA TAVRMMDNVV DVSKFPLPEQ KNEAQNKRRI GLGVTGLADA LLMLGLRYGS
DEAARQTEEW LHQIARAAYL ASVDLAREKG AFPLLDTEKY LASGTMQQMD EDVRAAIREH
GIRNALLTSI APTGTISLYA GNVSSGIEPV FAYTYTRKVL QKDGSRTEEE VVDYAVQMWR
DKFGDKALPD YFVNAQTLTP AEHVKMQAAA QKWVDSSISK TINCPEDISF EEFKDVYMQA
WDQGCKGCTT YRPNDVTGSV LSVSESADKA PGESADAPHE LDGGDVIYMS EPLDRPQSLE
GSTYKLKWPD SEHAIYLTIN DIIIGGRRRP FEVFINSKNM EHYAWTLALT RMISAVFRRG
GDVSFVVEEL KAVFDPRGGA WVKGKYIPSI LAAIGGVIEQ HLIAIGFLEG EGMGLKSDPQ
AQQVVNADLP RGKACPSCGQ YEMRMVEGCM TCASCGHSKC G
//
