ID A0A428JEL8_9RHOB Unreviewed; 765 AA.
AC A0A428JEL8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=EJA01_17905 {ECO:0000313|EMBL:RSK30641.1};
OS Rhodovulum robiginosum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=68292 {ECO:0000313|EMBL:RSK30641.1, ECO:0000313|Proteomes:UP000275159};
RN [1] {ECO:0000313|EMBL:RSK30641.1, ECO:0000313|Proteomes:UP000275159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12329 {ECO:0000313|EMBL:RSK30641.1,
RC ECO:0000313|Proteomes:UP000275159};
RA Gupta D., Guzman M.S., Bose A.;
RT "Draft genome sequence of a marine photoferrotrophic bacterium, Rhodovulum
RT robiginosum.";
RL Submitted (DEC-2018) 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:RSK30641.1}.
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DR EMBL; RWGU01000051; RSK30641.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428JEL8; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000275159; 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:UP000275159}.
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 765 AA; 84034 MW; 60FA97BDEA7146BC CRC64;
MTRFAAPIAE QIWDMKYRLK AADGTPRDLT VEDSWRRIAR ALAVVEDDPA QWEERFYDAL
VDFRFLPAGR ITAGAGTGRS VTLFNCFVMG TIPDSMAGIF DMLKEAALTM QQGGGIGYDF
STIRPKGADV HGVAADASGP LSFMDVWDAM CRTIMSAGSR RGAMMATMRC DHPDIEDFIT
AKQDAARLRM FNLSVLVTDA FMEAVKNDGS WELIFGGKVY HTVQARDLWN KIMRATYDYA
EPGVIFIDRI NAMNNLSYCE TIAATNPCGE QPLPPYGACL LGSINLARLV RDPFEDAAAL
DEAELDELVT TAVRMMDNVV DVSRFALPQQ ADEAKAKRRI GLGVTGLADA LLMVGLRYGS
DEAARQTERW LHRIARAAYL GSVQLAKEKG AFPLFEAEKY LASGSLTHMD EDVRAAIAEH
GIRNALLTSI APTGTISLYA GNVSSGIEPV FAYSYTRKVL QRDGSRSEEE VVDYAVQMWR
EKFGEAELPD HFVNAQTLSP SEHVKMQAAA QKWVDSSISK TINCPEDIDF DAFQNVYLQA
YETGCKGCTT YRPNDVTGSV LSVSEQKPEA ASAEHIVVTD GQHAVPPGDV VYISEPLDRP
QALEGNTYKL KWPDSEHAIY ITINDVVVGG RRRPFEVFIN SKNMEHFAWT VALTRMISAV
FRRGGDVSFV VEELKAVFDP RGGAWMQGKY IPSILAAIGG VIEHHLISIG FIDGEGMGLK
ADPQIEAMAV GETRRGPACP SCGSYEMRMV EGCMTCMSCG HSKCS
//
