ID A0A2V3WG72_9BACI Unreviewed; 900 AA.
AC A0A2V3WG72;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=DES38_10215 {ECO:0000313|EMBL:PXW92437.1};
OS Streptohalobacillus salinus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Streptohalobacillus.
OX NCBI_TaxID=621096 {ECO:0000313|EMBL:PXW92437.1, ECO:0000313|Proteomes:UP000247922};
RN [1] {ECO:0000313|EMBL:PXW92437.1, ECO:0000313|Proteomes:UP000247922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22440 {ECO:0000313|EMBL:PXW92437.1,
RC ECO:0000313|Proteomes:UP000247922};
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 (MAY-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:PXW92437.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QJJR01000002; PXW92437.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3WG72; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000247922; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
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 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 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:UP000247922}.
FT DOMAIN 160..690
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 900 AA; 100809 MW; 2B00593320A1B067 CRC64;
MSELIKEIYG ELEKTPFQVL LQLDRYTVKE MDISTLNVGD VVVAVYDETI PESPQKDFGK
VTAFDGKIVT FEGEITQKTH QVSTRHVSIP LDYKWEDSVD RYVLGAMSIE ETYKHKDLDQ
FKPRIHNSLY QEKIVPGGRV QASMGIFEKY GKQYDLTAYN CYVLPNPKDS RKGIINGSLS
EMTEIMSRGG GVGIALSTLR PRNARVYGVN GISSGSVSWG GLLSYATGLI EQGGSRKGAL
MLQLHISHPD IYDFITIKRE SGKVTNANLS VQLTKEFMEA VEADADWHLI FPDTKHEAYD
QNWAGQYQDI HDWLEAGLPV EIYETVKARE LYDLIIESAH ASAEPGVMVY DHMNDGYMTS
TQQLIKTADG KQYVLDSESL KRKQEATPWN NTFYYQKNVS SNPCGEQPLC GNGICNLIHI
NLAEFYDEET EDVNWEDLNQ AVADAIRYAD DVIDYTVYFR EENERIQKEQ RRIGMGTLGL
HDLLIDLKLR YGSETSIVFI DKLYSFIKNS AYRASAELAK VRGKFPKFDE KILQARVPKS
LDEDVIKLIK KYGLRNSHLL TQAPTGTTGT KTGSQGYSRS TGVEPFFSIK WERESRLGKT
IDYLGKAKDY LEKTGEKRLP DYFVSAMCEE KDGSPKITPK NHVDVQAAIQ KHNDSAISKT
CNVPNHFTIE QTKELYSYGI EQGVVGLTIY RDGSRDTQVL TNIKDEADTE ATPVNEAIQA
FEDEDREITS KQFYKRPQRL IGETIKSATP FGKMYVTVNR HPQNQVIEEV FLNLGKTGAD
ISAIADGLAI ALTGLLSPRI ANLTQEEKLN WIIKKFNGIK GQSSIGFGKN QIESLPDALA
KVLMQLGQDE ESEVTPAVAE QKLNLGSVDI CPSCGQSTFV KQDGCTTCLI DLGGCGFSKC
//
