ID M8DIW7_9BACL Unreviewed; 749 AA.
AC M8DIW7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN ORFNames=I532_05880 {ECO:0000313|EMBL:EMT53518.1};
OS Brevibacillus borstelensis AK1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1300222 {ECO:0000313|EMBL:EMT53518.1, ECO:0000313|Proteomes:UP000012081};
RN [1] {ECO:0000313|EMBL:EMT53518.1, ECO:0000313|Proteomes:UP000012081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK1 {ECO:0000313|EMBL:EMT53518.1,
RC ECO:0000313|Proteomes:UP000012081};
RA Rajan I., PoliReddy D., Sugumar T., Rathinam K., Alqarawi S., Khalil A.B.,
RA Sivakumar N.;
RT "Assembly of a new bacterial strain Brevibacillus borstelensis AK1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
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:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
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:EMT53518.1}.
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DR EMBL; APBN01000002; EMT53518.1; -; Genomic_DNA.
DR AlphaFoldDB; M8DIW7; -.
DR STRING; 1300222.I532_05880; -.
DR PATRIC; fig|1300222.3.peg.1206; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000012081; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd01679; RNR_I; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF03477; ATP-cone; 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.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000012081}.
FT DOMAIN 7..97
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 749 AA; 85369 MW; A95A2F7879D22E70 CRC64;
MNAVTTIQIV KRNGEQEDLR IDKLKKVIGY ACKDYPACDP LELEMDACIQ FRDGMTTKEI
QRIVMQTAVE KTSVETPEWQ FVAARLLAYD LYKDAAINRG YRGHFGYGDF TELVHTLTEK
GLYGSYLLET YSDEEIQELQ AYLKPERDEL FNYAGLRLLA DRYLIKDYDK GVMELPQERF
MIIAMHLAMK EQDKLKHAKD FYDILSKLEI TVATPTLANA GTPHHQLSSC FIDTVDDSLS
GIMNTAGATS MVSKFGGGVG IYLGKVRSRG SSIRGHKGAS GGIVPWTRLY NQIAISVDQL
GTRAGAFAIY LDVWHADILD FLLLKTNNGD DRMKAHDIFP GVCIPDLFME RVKERGMWYL
FDPHEVREVM GFSLEDSYGE EFARRYELCV QEEKLTIKTE IPAIEIMKRI MASAFETGTP
FIFFRDTVNR ANPNKHAGMV YSSNLCTEIM QNMSPTVFVS EELEDGEVVY RYRPGDFVVC
NLSSLNLGRL QSTEDIARIV PIQMRMLDNV IDLNYYPVKQ AEATNQKYRA VGLGTSGYHQ
YLAQNGIKWE SEEHIEAADK LYEEIAYQAI KTSMELAREK GTYRVFEGSE WQTGEYFERR
GYTDERWTSL KEDVARYGMR NAWTFAVAPT GTTSLIAGST ASTDPVYAKF FVEEKRSGNI
PQTAPNLNEN TFFYYKEAHR IDQQWSIRAA GARQVHIDQA QSFNLYITPQ ITAPEFLDLY
IQAWENGLKT IYYVRNQSVE VEDCVSCSA
//
