ID A0A3M7TUR0_9BACI Unreviewed; 731 AA.
AC A0A3M7TUR0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=EBO34_00305 {ECO:0000313|EMBL:RNA68454.1};
OS Alteribacter keqinensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacter.
OX NCBI_TaxID=2483800 {ECO:0000313|EMBL:RNA68454.1, ECO:0000313|Proteomes:UP000278746};
RN [1] {ECO:0000313|EMBL:RNA68454.1, ECO:0000313|Proteomes:UP000278746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KQ-3 {ECO:0000313|EMBL:RNA68454.1,
RC ECO:0000313|Proteomes:UP000278746};
RA Wang H.;
RT "Bacillus Keqinensis sp. nov., a moderately halophilic bacterium isolated
RT from a saline-alkaline lake.";
RL Submitted (OCT-2018) 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:RNA68454.1}.
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DR EMBL; RHIB01000001; RNA68454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M7TUR0; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000278746; 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.
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:UP000278746}.
FT DOMAIN 127..204
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 207..716
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 731 AA; 83302 MW; 33C8D44D58F7B283 CRC64;
MTKTITYHSE LTEQLIAEFP NLTWTNWPQE TGNTTVTLKD MQQQALDRMH TEEPDWTYVA
ARYRLKELYE TIAAERFCEV REAYERFPET LRYLTNENIY SHELEAGYSE EEQRELAKTL
DPDLDKQFTF LGLHTFIDRY LAKSQDNKTV ELPQERFMII AMVLMQHEPK NVRLTLVKEA
YWAMANLYMT VATPTLANAG KTHGQLSSCF IDTMGDSLRG IFDSTTDAAT LSKNGGGIGI
YLGKVRSKGS SIKGFKGNSS GVLPWMKQLN NTAVSVDQLG QRQGAIAVYL DVWHKDIFSF
LDAKLNNGDE RKRTHDLFTG VSLPDLFMEK VEAREAWCLF DPHEVRQTMG FSLEDCYDEE
KGAGSFREKY EVCVNNPKLS REEVPAIDIM KRIMISQLET GTPYMFYRDE ANRMNPNSHR
GMIYGSNLCT EIMQNMSETT VTEEKTKDGT ILITKTAGDY VVCNLSSINL AKAIPDDVLK
RLIPIQVRML DNVIDVNRLE VPQAKLTNEK YRGIGLGTYG WHHLLALTGI RWESEEAVAF
ADELYETIAR LTIQASANLA KEKGSYPAYK GSDWEKGLYF TKRGLDLHWE STINMVKQSG
LRNGYLMAVA PNSSTAILAG TTASIDPIYR KEYAEEKKNY RIPVTAPDLS SETTWFYKAA
HEIDQHWSIR QNAARQRYID QGISFNLYVK NTIKAKDLLA LHLHAWKEGL KTTYYVRSTS
SEIEECDSCA S
//
