ID D1NXW2_9GAMM Unreviewed; 710 AA.
AC D1NXW2;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=PROVRUST_04751 {ECO:0000313|EMBL:EFB74251.1};
OS Providencia rustigianii DSM 4541.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=500637 {ECO:0000313|EMBL:EFB74251.1, ECO:0000313|Proteomes:UP000005512};
RN [1] {ECO:0000313|EMBL:EFB74251.1, ECO:0000313|Proteomes:UP000005512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4541 {ECO:0000313|EMBL:EFB74251.1,
RC ECO:0000313|Proteomes:UP000005512};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2009) 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:EFB74251.1}.
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DR EMBL; ABXV02000002; EFB74251.1; -; Genomic_DNA.
DR AlphaFoldDB; D1NXW2; -.
DR STRING; 500637.PROVRUST_04751; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_4_1_6; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000005512; 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; 1.10.1650.20; -; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR026459; RNR_1b_NrdE.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013554; RNR_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR NCBIfam; TIGR04170; RNR_1b_NrdE; 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 Pfam; PF08343; RNR_N; 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}.
FT DOMAIN 562..584
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 710 AA; 80972 MW; 6600A68E12668579 CRC64;
MDKMQDIHNV DYHSLNAMLN LYDSEGRLQL DKDKQAAHAY FRQHVNQNTV FFHDLKEKLD
FLVNENYYES EVLEQYEFQF IKQLFKQAYA HKFRFKTFLG AFKYYTSYTL KTFDGQRYLE
RYEDRVCMVA LTLAQGSKSL ASLLVDEIIS GRFQPATPTF LNCGKKQRGE LISCFLLRIE
DNMESIGRSV NSALQLSKRG GGVAFLMTNL REQGAPIKHI ENQSSGVVPV MKMLEDAFSY
ANQLGARQGA GAVYLHAHHP DILRFLDTKR ENADEKIRIK TLSLGVVIPD ITFQLAKNNE
DMYLFSPYDV QREYGVAMSE ISVSEKYHEM VNNKAIKKFK INAREFFQTI AEIQFESGYP
YILFEDTANR ENPIAGRINM SNLCSEILQV NQPSTYEDDL NYKTVGKDIS CNLGSMNIAS
TMDSPDFALS IETAVRALTA VSDMSYINSV PSIAQGNQQS HAIGLGQMNL HGYLAREHIY
YGSEQGLDFT NIYFYTVAYY ALKTSNQLAI ERQQTFDGFS ASKYASGEYF DKYINKIWSP
KTQTVQELFR RSGIKIPTQA DWLALKQSVM TYGIYNQNLQ AIPPTGSISY INNSTSSIHP
VVAPIEIRKE GKIGRVYYPA PFMTNENLKF YQDAYQIGPE KIIDTYAEAT QHVDQGLSLT
LFFDGDATTR DINRAQIYAW RKGIKTLYYI RLRQTALEGT EVEGCVSCSL
//
