ID A0A0F0LB48_9MICO Unreviewed; 723 AA.
AC A0A0F0LB48;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 Name=nrdE2 {ECO:0000313|EMBL:KJL28776.1};
GN ORFNames=RS83_02257 {ECO:0000313|EMBL:KJL28776.1};
OS Microbacterium oxydans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=82380 {ECO:0000313|EMBL:KJL28776.1, ECO:0000313|Proteomes:UP000033640};
RN [1] {ECO:0000313|EMBL:KJL28776.1, ECO:0000313|Proteomes:UP000033640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BEL4b {ECO:0000313|EMBL:KJL28776.1,
RC ECO:0000313|Proteomes:UP000033640};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) 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:KJL28776.1}.
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DR EMBL; JYIW01000025; KJL28776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0LB48; -.
DR PATRIC; fig|82380.11.peg.2292; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000033640; 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}.
FT DOMAIN 575..597
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 723 AA; 81652 MW; D21EE74456A98E25 CRC64;
MGSAVEEQAV TEQVAFKINP GYEGLDYHAL NAMLNLYDAN GKIQFDADKR AAREYFLQHV
NQNTVFFHSL KERLDYLVEK EYYEGAVIEK YSMEFIQKLN DLAYGKKFRF ETFLGAFKYY
TSYTLKTFDG KRYLERFEDR VVMTALGLAD GDEKLAVALV EEIISGRFQP ATPTFLNAGK
AQRGELVSCF LLRIEDNMES IARGINSALQ LSKRGGGVAL LLSNIRESGA PIKQIENQSS
GIIPVMKLLE DSFSYANQLG ARQGAGAVYL NAHHPDIMRF LDTKRENADE KIRIKTLSLG
VVVPDITFEL AKNDEDMYLF SPYDVEKVYG VPFGDISVTE KYREMVDNPR IKKTKINARE
FFQTVAEIQF ESGYPYVMFE DTVNKANPIK GRINMSNLCS EILQVNTPTT YNDDLSYDNI
GKDISCNLGS MNIALSMDAD DLGQTVETAI RALTAVSDQS HIGSVRSIED GNDRSHAIGL
GQMNLHGYLA REHVYYGSEE GIDFTNIYFY TVLFHALRAS NNLAIERGTT FDGFEDSTYA
SGAFFDKYIE RAWVPETEKV KELFAGKHIP TQDDWAELKA SIQKHGIYNQ NLQAVPPTGS
ISYINNSTSS IHPIASKIEI RKEGKLGRVY YPAAFMTNDN LEYYQDAYEI GYEKVIDTYA
AATQHVDQGL SLTLFFKDTA TTRDINKAQI YAWRKGIKTI YYIRLRQMAL EGTDMAECVS
CML
//
