ID C4L4U2_EXISA Unreviewed; 755 AA.
AC C4L4U2;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=EAT1b_0756 {ECO:0000313|EMBL:ACQ69687.1};
OS Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=360911 {ECO:0000313|EMBL:ACQ69687.1, ECO:0000313|Proteomes:UP000000716};
RN [1] {ECO:0000313|EMBL:ACQ69687.1, ECO:0000313|Proteomes:UP000000716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1283 / AT1b {ECO:0000313|Proteomes:UP000000716};
RX PubMed=21460088; DOI=10.1128/JB.00303-11;
RA Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina Del Rio T.,
RA Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA Hendrix C., Richardson P., Tiedje J.M.;
RT "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT AT1b.";
RL J. Bacteriol. 193:2880-2881(2011).
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; CP001615; ACQ69687.1; -; Genomic_DNA.
DR RefSeq; WP_012726806.1; NC_012673.1.
DR AlphaFoldDB; C4L4U2; -.
DR STRING; 360911.EAT1b_0756; -.
DR KEGG; eat:EAT1b_0756; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_9; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000716; 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; 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}.
FT DOMAIN 613..635
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 755 AA; 85869 MW; 2B009B6D0BD52639 CRC64;
MTSPIHHETM LPAAPTLADV SSLIQSIQTR YPHLSVERYE ERAIRALETK TLTQDVVYDL
LTMHALDMLK AEEPDWTFVA TEMYLNRLYL EAARNRGYEA SMRYGNFYQL VETLTSKRIF
TSALLDTYSK EDMDHLETLI DPSRDRLFTY IGLRTLSDRY LGRDHVKNLY ELPQERFMVI
AMTLMQKEDE TTRLKLVEEA YWALSNLYMT VATPTLSNAG KSYGQLSSCF IDTVDDSLRG
IYDSNTDVAT LSKGGGGIGV YLGKIRSRGS DIKGFKGVSS GALPWMKQLN NTAVSVDQLG
MRQGSIAVYL DIWHKDIFEF LDAKLNNGDE RLRTHDLFTG VCLPDLFMRT VEARGDWHLF
DPHEIRTVMG YSLEDYFDES ENGGSFTEKY MECVNTPELS RVTVPAIDLV KRYMRSQLET
GTPYMFFRDA VNRANPNKHA GMIYSSNLCS EIAQNMSATT IEEEYTQDGK IVITKTPGDF
VVCNLSSIAL ARAVKADVLE RLIPIQMRML DNVIDLNTIE VPQAMITNQK YRAVGLGTFG
WHHLLALEGI RWESVDAVQY AEKLYEKIAY LTIQASMELA KEKGAFGVFE GSEWHTGEYF
KRRNYRSHDD LDWDGLAEAV HQNGVRNAYM MAVAPNSSTA IIAGSTASID PVYKKVYSEE
KKNYKIPVTV PDLTPDTNWF YKSAFEIDQL WSIRQNAARQ RHIDQAISFN LYVKNDVKAT
ELLAMHLEAW SLGMKSIYYT RSTTVEVDEC ESCAS
//
