ID A0A0H3FIX7_KLEAK Unreviewed; 714 AA.
AC A0A0H3FIX7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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 OrderedLocusNames=EAE_01425 {ECO:0000313|EMBL:AEG95221.1};
OS Klebsiella aerogenes (strain ATCC 13048 / DSM 30053 / CCUG 1429 / JCM 1235
OS / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006 / CDC 819-56)
OS (Enterobacter aerogenes).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1028307 {ECO:0000313|EMBL:AEG95221.1, ECO:0000313|Proteomes:UP000008881};
RN [1] {ECO:0000313|Proteomes:UP000008881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 /
RC NCIMB 10102 / NCTC 10006 {ECO:0000313|Proteomes:UP000008881};
RA Shin S.H., Kim S., Kim J.Y., Yang K.-S., Seo J.-S.;
RT "Complete sequence of Enterobacter aerogenes KCTC 2190.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEG95221.1, ECO:0000313|Proteomes:UP000008881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 /
RC NCIMB 10102 / NCTC 10006 {ECO:0000313|Proteomes:UP000008881};
RX PubMed=22493190; DOI=10.1128/JB.00028-12;
RA Shin S.H., Kim S., Kim J.Y., Lee S., Um Y., Oh M.K., Kim Y.R., Lee J.,
RA Yang K.S.;
RT "Complete genome sequence of Enterobacter aerogenes KCTC 2190.";
RL J. Bacteriol. 194:2373-2374(2012).
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}.
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DR EMBL; CP002824; AEG95221.1; -; Genomic_DNA.
DR RefSeq; WP_015703234.1; NC_015663.1.
DR RefSeq; YP_004590500.1; NC_015663.1.
DR AlphaFoldDB; A0A0H3FIX7; -.
DR KEGG; eae:EAE_01425; -.
DR PATRIC; fig|1028307.3.peg.276; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_4_1_6; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000008881; Chromosome.
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 566..588
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 714 AA; 80129 MW; 10809FD37640DEE9 CRC64;
MATTTAERVT AGASDFHALN AMLNLYDSNG RIPLEKDQQA VEAFIHNHVR PNSVPFAGLE
EKLQWLSDEG YYDPAVLARY ERRFVLALFA HAHQHGFRFR TFLGAWKFYT SYALRTFDGK
RYLEHFADRA CMVALTLAQG DETLARQLAD EILAGRFQPA TPTFLNAGKQ QRGELVSCFL
LRIEDNMESI GRAVNSALQL SKRGGGVAFL LSNLREAGAP IKRIENQSSG VVPVMKMLED
AFSYANQLGA RQGAGAVYLH AHHPDILRFL DTKRENADEK IRIKTLSLGV VIPDITFQLA
KEDAQMALFS PYDVERLYGK AFGDIAVSEM YAQLVADDRV RKRWIRARDL FQRLAEIQFE
SGYPYIMFED TVNRANPIAG RINMSNLCSE ILQVNSASTF DENLDYATVG EDISCNLGSL
NIAHAMDSPD FARTVEVAVR GLTAVSDMSD IRSVPSVAAG NAASHAIGLG QMNLHGYLAR
EGIAYGSPEG LDFTNLYFYT VTWHALRTSM AMARERGVRF AGFEQSRYAS GDYFQQYLQG
DWQPKTTTVR ELFARAGITL PDREMWRQLR DDVMRYGIYN RNLQAIPPTG SISYINHATS
SIHPIVAKIE IRKEGKTGRV YYPAPFMTND NLALYQDAWE IGPQKIIDTY AEATRHVDQG
LSLTLFFPDT ATTRDINKAQ IYAWKKGIKT LYYIRLRQLA LEGTEIEGCV SCAL
//
