ID S2XU58_9STAP Unreviewed; 701 AA.
AC S2XU58;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=HMPREF1208_00234 {ECO:0000313|EMBL:EPD53500.1};
OS Staphylococcus sp. HGB0015.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1078083 {ECO:0000313|EMBL:EPD53500.1, ECO:0000313|Proteomes:UP000014407};
RN [1] {ECO:0000313|EMBL:EPD53500.1, ECO:0000313|Proteomes:UP000014407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGB0015 {ECO:0000313|EMBL:EPD53500.1,
RC ECO:0000313|Proteomes:UP000014407};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Staphylococcus sp. HGB0015.";
RL Submitted (APR-2013) 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:EPD53500.1}.
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DR EMBL; AGEO01000002; EPD53500.1; -; Genomic_DNA.
DR RefSeq; WP_016424500.1; NZ_KE150417.1.
DR AlphaFoldDB; S2XU58; -.
DR GeneID; 72415118; -.
DR PATRIC; fig|1078083.3.peg.232; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_4_1_9; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000014407; 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:UP000014407}.
FT DOMAIN 559..581
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 701 AA; 80067 MW; EEB2A54340033321 CRC64;
MKTMEQKQYN HIELNNQVTK RNENGFFQIE KDQEALAVYL EEIKDKTVHF DSELERLHFL
VDNNFYYNVF NEYSEAQLAE VIAFASSIPF AFASYMSASK FFKDYALKTN DKSKYLEDYH
QHVVIVSLYL AKGNVALAKQ FIQAMIDQRY QPATPTFLNA GRARRGELVS CFLLEVDDSL
NSINYIDSTA KQLSKIGGGV AINLSKLRAR GEAIKGIKGV AKGVLPVAKA LEGGFSYADQ
LGQRPGAGAV YLNIFHYDVE EFLDTKKVNA DEDLRLSTIS TGLIVPSKFF ELAKEGKDFF
MFAPHTVEKE YGVTLDDINI DEYYDQLVEN PNIMKKSKDA REMLNMIAQT QLQSGYPYLM
FKDNANRVHA NSNIGQIKMS NLCTEIFQLQ ETSVINDYGI EDEIKRDISC NLGSLNIVNV
MESDKFRDSV HTGMDALTVV SDEANIQNAP GVRKANSELH SVGLGVMNLH GYLAKNKISY
ESEEARDFAN VFFMMMNYYS IERSMEIAKE RGETFVGFEQ TDYANGRYFE RYTSEDFLPQ
YDKVKALFEN HDIPTREDWK ALQAEVEKYG LYHAYRLAIA PTQSISYVQN ATSSVMPIVD
QIERRTYGNS ETFYPMPFLS PQTMWYYKSA FNTDQMKLID LIATIQTHID QGISTILYVN
SEISTRELSR LYVYAHYKGL KSLYYTRNKL LSVEECTSCS I
//
