ID A8E2R0_BPPHE Unreviewed; 327 AA.
AC A8E2R0;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
GN ORFNames=EFP_208 {ECO:0000313|EMBL:BAF81476.1};
OS Enterococcus phage phiEF24C (Enterococcus bacteriophage phi-EF24C).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Herelleviridae; Brockvirinae; Kochikohdavirus; Kochikohdavirus EF24C.
OX NCBI_TaxID=442493 {ECO:0000313|EMBL:BAF81476.1, ECO:0000313|Proteomes:UP000001151};
OH NCBI_TaxID=1351; Enterococcus faecalis (Streptococcus faecalis).
RN [1] {ECO:0000313|EMBL:BAF81476.1, ECO:0000313|Proteomes:UP000001151}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PhiEF24C {ECO:0000313|EMBL:BAF81476.1};
RX PubMed=18456848; DOI=10.1128/AEM.02371-07;
RA Uchiyama J., Rashel M., Takemura I., Wakiguchi H., Matsuzaki S.;
RT "In silico and in vivo evaluation of bacteriophage phiEF24C, a candidate
RT for treatment of Enterococcus faecalis infections.";
RL Appl. Environ. Microbiol. 74:4149-4163(2008).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|PIRSR:PIRSR000355-2};
CC Note=Binds 2 iron ions per subunit. {ECO:0000256|PIRSR:PIRSR000355-2};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|ARBA:ARBA00011209}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000256|ARBA:ARBA00009303}.
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DR EMBL; AP009390; BAF81476.1; -; Genomic_DNA.
DR RefSeq; YP_001504317.1; NC_009904.1.
DR GeneID; 5666512; -.
DR KEGG; vg:5666512; -.
DR OrthoDB; 4477at10239; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000001151; Genome.
DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:InterPro.
DR CDD; cd01049; RNRR2; 1.
DR Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR026494; RNR_NrdF-like.
DR InterPro; IPR033909; RNR_small.
DR InterPro; IPR000358; RNR_small_fam.
DR NCBIfam; TIGR04171; RNR_1b_NrdF; 1.
DR PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1.
DR PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR PIRSF; PIRSF000355; NrdB; 1.
DR SUPFAM; SSF47240; Ferritin-like; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000355-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000355-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001151}.
FT ACT_SITE 106
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-1"
FT BINDING 68
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 99
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 99
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 102
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 193
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 196
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
SQ SEQUENCE 327 AA; 37340 MW; 6E96788A2C2D709D CRC64;
MNLQEKYEGI NWNKIDDVID QATWKKLTEQ FWLDTRVPVG NDVNDWAKLS DMEQDLINKV
FGGLTLLDTV QSESGVHSLL DDVRTQHEEA VLNNIAFMEA VHAKSYSTIF STFNTPTEID
NIFEWVATNK RLQYKANIIN DIYRNGTPLQ KKSASVLLES FLFYSGFYTP LRYLGEAKMV
NTAEIIKLII RDESVHGTYI GYKYQLGFNQ LPETEQKEME QWVIDLAFKL WENETQYTAE
LYSEIGWTKD VNTFLEYNLN KALANLGMNP LFPTTSADVN PIVMNGISTT TSNHDFFSQV
GNGYLLGKVE PVTDADYNAL DKLASLV
//
