ID A0A198FHC0_9GAMM Unreviewed; 708 AA.
AC A0A198FHC0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=M983_2549 {ECO:0000313|EMBL:OAT24317.1};
OS Proteus myxofaciens ATCC 19692.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=1354337 {ECO:0000313|EMBL:OAT24317.1, ECO:0000313|Proteomes:UP000094023};
RN [1] {ECO:0000313|EMBL:OAT24317.1, ECO:0000313|Proteomes:UP000094023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19692 {ECO:0000313|EMBL:OAT24317.1,
RC ECO:0000313|Proteomes:UP000094023};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (APR-2016) 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:OAT24317.1}.
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; LXEN01000125; OAT24317.1; -; Genomic_DNA.
DR RefSeq; WP_066751571.1; NZ_LXEN01000125.1.
DR AlphaFoldDB; A0A198FHC0; -.
DR STRING; 1354337.M983_2549; -.
DR PATRIC; fig|1354337.4.peg.2618; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000094023; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000094023}.
FT DOMAIN 560..582
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 708 AA; 80873 MW; 76BC2CD923A5AFF6 CRC64;
MTQPIEQRDY HALNAMLNLY DEQGNIQFDK DKLATHHFFR QHVNQNTVFF HDLKEKLDFL
VEQHYYEAHV LEQYDFTFIK QLFKHAYSKK FRFQSFLGAF KYYTSYTLKT FDGERYLERY
EDRVCMVALT LAQGNTELAT HIVDEVISGR FQPATPTFLN CGKQQRGELV SCFLLRIEDN
MESIGRSVNS ALQLSKRGGG VAFLLTNLRE AGAPIKRIEN QSSGVVPIMK MLEDAFSYAN
QLGARQGAGA VYLHAHHPDI YHFLDTKREN ADEKVRIKTL SLGVVIPDIT FELAKRNEDM
YLFSPYDVER VYGVPMSEIS VSEKYAEMVN NGEIRKKKIK AREFFQTLAE IQFESGYPYI
MFEDAVNRAN PIAGRINMSN LCSEILQVNS ASEYHPDLSY QHIGHDISCN LGSMNIAMAM
DSPDFAHTIN TAIRALSSVA EMTKIESVPS IEKGNQASHA IGLGQMNLHG YLAREGIYYG
SEEALDFTNI YFYTVTYYAL LASNQLAIEK KQTFKGFEHS KYASGEYFDK YVSQEWLPKT
QKVHQLFSQS NVHIPTQEDW EKLKQSIMAN GIYNQNLQAI PPTGSISYIN NSTSSIHPIA
APIEIRKEGK IGRVYYPAPF MTNENRQYYQ DAYEIGAEKI IDTYAQATQH IDQGLSLTLF
FSDEATTRDI NKAQIYAWRK GIKTLYYIRI RQTALAGTEI KGCVSCAL
//
