ID A0A087MZS5_9BACI Unreviewed; 741 AA.
AC A0A087MZS5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=CH76_12710 {ECO:0000313|EMBL:KFL42378.1};
OS Lysinibacillus sp. BF-4.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1473546 {ECO:0000313|EMBL:KFL42378.1, ECO:0000313|Proteomes:UP000029097};
RN [1] {ECO:0000313|EMBL:KFL42378.1, ECO:0000313|Proteomes:UP000029097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BF-4 {ECO:0000313|EMBL:KFL42378.1,
RC ECO:0000313|Proteomes:UP000029097};
RA Antwerpen M.H., Georgi E., Zimmermann P., Hoermansdorfer S., Meyer H.,
RA Grass G.;
RT "Genome sequence of strain, BF-4, a Lysinibacillus-like bacillus isolated
RT during an anthrax outbreak in Bavaria.";
RL Submitted (MAR-2014) 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:KFL42378.1}.
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DR EMBL; JPUW01000054; KFL42378.1; -; Genomic_DNA.
DR RefSeq; WP_036146899.1; NZ_JPUW01000054.1.
DR AlphaFoldDB; A0A087MZS5; -.
DR eggNOG; COG0209; Bacteria.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000029097; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 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; 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; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000029097}.
FT DOMAIN 599..621
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 741 AA; 83435 MW; F751FF64BDEF1736 CRC64;
MTIKTMTSIS ARVDALTEKY GEEAIEQFLR QSDRFLRKNE AATYGEWADA MVLQTLGFID
EEEPYWTFVA ADIYLHKLYH DAASLRGVAA DNVYESFSVN LAKYVAAGLY SPVLVEKYSP
EELTTLTNTI VPARDTLFTY IGLKTIIDRY VVRDYSKQTV ELPQERFMVI AMILMQDEKD
NRIAKVQEAY WAMSNLYMTM ATPTLANAGK THGQLSSCFI DTVDDSLQGI YDSNTDVATL
SKFGGGIGVY MGKIRSRGSA IRGFKGASSG VLPWIKQLNN TAVSVDQLGQ RQGAIAVYLD
VWHKDVFTFL DLRLNNGDER MRAHDIFTGL CLPDIFMEAV QARSDWHLFD PHEVRNVMGF
SLEDYYDEKR GEGSFRDKYA ACVENPELTR TVVPAIDIMK RIMRSQLETG VPFMFYRDEV
NRKNPNKHEG MIYSSNLCTE IAQNMSPTEF ESVELEDGLI VTKRKAGDFV VCNLSSINLG
RAVPADVLAR VIPIQVRMLD NVIELNTIPV RQAERTNARY RGIGLGTFGW HHLLALKEIA
WESDEAVQFA DELYEQIAYL TIQASSDLAA EKGAYPLFEG SDWQTGAYFT ARGYEGEAWA
DLQEKVATQG MRNGYTMAVA PNSTTAIIAG STASVDPIFQ KSYSEEKKDY KIPVTVPDLN
AKTTWFYKSA YFIDQNWSVK QNAARGRHID QGISFNLYVQ NTVKAKDLLQ LHLNAWDSGV
KTTYYVRSTS VELIDCSSCE S
//
