ID A0A370G7W2_9COXI Unreviewed; 600 AA.
AC A0A370G7W2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=C8D86_1271 {ECO:0000313|EMBL:RDI39196.1};
OS Aquicella lusitana.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Aquicella.
OX NCBI_TaxID=254246 {ECO:0000313|EMBL:RDI39196.1, ECO:0000313|Proteomes:UP000254720};
RN [1] {ECO:0000313|EMBL:RDI39196.1, ECO:0000313|Proteomes:UP000254720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16500 {ECO:0000313|EMBL:RDI39196.1,
RC ECO:0000313|Proteomes:UP000254720};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-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:RDI39196.1}.
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DR EMBL; QQAX01000027; RDI39196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370G7W2; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000254720; 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:UP000254720}.
FT DOMAIN 13..81
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 87..574
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 600 AA; 67498 MW; 9C3D1FE1DAF85AF7 CRC64;
MNTFKEPISN NVWDLKYRYR FQGHIIDQTI EDTWRRVAVA VAGAEKTQDE QAYWQKAFYR
LLEDFQFLPG GRILAGAGTE HAVTLFNCFV MDIAEDSLKG IFDALREGAL TLQQGGGVGY
DFSVLRPKGA LVKKTGTTSS GPVSFMRIWD TTCKILLATG ARRGAMMAVL RCDHPDIEEF
ISAKEDPLEL RHFNVSVMVT DAFMEAVRDD ADWPLVFPTK ESSKNPQDIV YRQWGSAFKP
VPCRIYRHVK ARELWHKIIR SAYQYAEPGV LFGDTINRMN TLWYRERINA TNPCGEIPLP
PYGACNLGSI NLTQFVEAPF SPSAKLNWIA IEETIRVATR FQDNVIDISH YPLPVQREQA
TGTRRIGIGV TGLADAFVML GVRYGSPASI ELAAKIMKKV AEATWQASIE LASEKGTFPF
FQEDYLRGNF VLGLDEQIRR SLAQHGIRNS HHNTIAPTGT ISLLANNVSN GIEPVFKADY
DRHVRVQDEK TIVFHVKDYA FQLWQQKNKN GLPPEWVDTD SLTPEAHLQI QGAMQPFIDN
AISKTINIPR DFPFEKMVDV YSKAYALGLK GCTVFRPNPV TGSVLEASKS DSVDHCCPFE
//
