ID A0A0P8B959_9RHOB Unreviewed; 754 AA.
AC A0A0P8B959;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-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 Name=nrdJ2 {ECO:0000313|EMBL:KPQ04964.1};
GN ORFNames=HLUCCA12_16060 {ECO:0000313|EMBL:KPQ04964.1};
OS Rhodobacteraceae bacterium HLUCCA12.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666916 {ECO:0000313|EMBL:KPQ04964.1, ECO:0000313|Proteomes:UP000050476};
RN [1] {ECO:0000313|EMBL:KPQ04964.1, ECO:0000313|Proteomes:UP000050476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCA12 {ECO:0000313|EMBL:KPQ04964.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
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}.
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:KPQ04964.1}.
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DR EMBL; LJSV01000024; KPQ04964.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P8B959; -.
DR STRING; 1666916.HLUCCA12_16060; -.
DR PATRIC; fig|1666916.3.peg.1579; -.
DR Proteomes; UP000050476; 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}.
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 754 AA; 82557 MW; 0D3C58533BB6F6ED CRC64;
MNRFAAPIAE QIWDMKYRLK DAAGKPVDAT LEDSWRRIAR ALAAVEDDPA HWEDRFYTAL
EDFKFLPAGR IVAGAGTGRS VTLFNCFVMG TIPDSMAGIF DMLKEAALTM QQGGGIGYDF
STIRPRGAPV AGVAADASGP LSFMDVWDAM CRTIMSAGSR RGAMMATMRC DHPDIEDFIT
AKQDSARLRM FNLSVLVTDP FMDAVRADKP WDLTFGGKVF RTVPARDLWN RIMRATYDYA
EPGVIFIDRI NAANNLHYCE TISATNPCGE QPLPPYGACL LGSINLARLV TDPFGRNPQL
DEAVLDDLVR TAVRMMDNVV DASRFPLPQQ AQEAQAKRRI GLGVTGLADA LLMMGLRYGS
DAAVAQTEAW MKAIARAAYL ASTDLAREKG AFPLFDADKF LASGTMQVMD DDVRAAVRAH
GIRNALLTSI APTGTISLFA GNVSSGIEPV FAYSYRRKVL QPDGSRTEEE VEDYAVQMWR
EKNGDAPLPE HFVNAQMLTP LDHVRMQAAA QKWVDSSISK TINCPEDIPF EEFKDVYLAA
WDMGCKGCTT YRPNDVTGSV LSLSEVSESE PQADTGAEVI YLSEPLDRPE ALEGQTYKLK
WPVSEHAIYI TINDVIVGGH RRPFEVFINS KNMEHFAWTV ALTRMISAVF RRGGDVSFVV
EELKAVFDPR GGAWMQGRYV PSILAAIGGV IEEHLVRIGF IEGAGLGLKS DPKARAAIMG
QGARGKACPA CGAYDMVMIE GCMTCRACGH SKCG
//
