ID A0A060AFS0_9CAUD Unreviewed; 343 AA.
AC A0A060AFS0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
OS Listeria phage List-36.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Herelleviridae; Jasinkavirinae; Pecentumvirus; Pecentumvirus list36.
OX NCBI_TaxID=1486422 {ECO:0000313|EMBL:AIA64219.1, ECO:0000313|Proteomes:UP000026982};
RN [1] {ECO:0000313|EMBL:AIA64219.1, ECO:0000313|Proteomes:UP000026982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=List-36 {ECO:0000313|EMBL:AIA64219.1};
RA Rajanna C., Joelle W., Abuladze T., Li M., Anderson B., Sulakvelidze A.;
RT "Genome sequencing of lytic Listeria phages.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000256|ARBA:ARBA00009303}.
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DR EMBL; KJ535721; AIA64219.1; -; Genomic_DNA.
DR RefSeq; YP_009043426.1; NC_024364.1.
DR GeneID; 19685314; -.
DR KEGG; vg:19685314; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000026982; Genome.
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; IPR033909; RNR_small.
DR InterPro; IPR000358; RNR_small_fam.
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 ECO:0000313|EMBL:AIA64219.1}.
FT ACT_SITE 123
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-1"
FT BINDING 86
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 119
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 183
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 217
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 220
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
SQ SEQUENCE 343 AA; 39531 MW; 272166CA19684A42 CRC64;
MLKKIKILEP LNPNKSTAII NGEASGIVNW NDIRYPSFYR AYKELTTNYW LPDEVDMKSD
AKQYNHLSEE EKYAFDSIIG LLATLDSPQT RFIYNIAEYV SDASVHAITA IIAQQEAIHN
ESYSYVLASI TNLQEQNRVF EEARTHPTII KRNAPIMKSY DDFMNNKTPE NMVKALVQSS
ILEGINFYSG FAYFYNLVRQ NKMTGTGKII SFINRDELAH SKFISELIRA IVGENPELQT
DELNDYVYAS FRHAVELEQA WSSEVLQGIE GIDVEEMLDY VKYRANKMLG MLGLQPMYQG
HTENSMTWIK AYADNFTETK TDFFEMRNSS YKKTNLDNGF DDL
//
