ID A0A2M9CLT3_9MICO Unreviewed; 826 AA.
AC A0A2M9CLT3;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=CLV46_2430 {ECO:0000313|EMBL:PJJ72853.1};
OS Diaminobutyricimonas aerilata.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Diaminobutyricimonas.
OX NCBI_TaxID=1162967 {ECO:0000313|EMBL:PJJ72853.1, ECO:0000313|Proteomes:UP000228758};
RN [1] {ECO:0000313|EMBL:PJJ72853.1, ECO:0000313|Proteomes:UP000228758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27393 {ECO:0000313|EMBL:PJJ72853.1,
RC ECO:0000313|Proteomes:UP000228758};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) 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:PJJ72853.1}.
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DR EMBL; PGFF01000001; PJJ72853.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9CLT3; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000228758; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR005144; ATP-cone_dom.
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; PF03477; ATP-cone; 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; PS51161; ATP_CONE; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000228758}.
FT DOMAIN 3..94
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 779..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 826 AA; 92319 MW; E4C148A9E1E24F37 CRC64;
MAITVVKRNG EREPYDANKI NLAIEHASAG LDDNITWVTQ IASELELTLF DGITTQQLDE
AVIQVALQNV KDDPAFDTVA ARLLLKTIYK RVLGDYETAD ELKSLHEQHF EKNVRRGVEE
GLLDPRLTQM FDFDRLAAAL EPAHDELLKY IGVVTLNNRY GIKGRNGDAL EVPQYFWMRI
AMGLSLNEAD PTSHAIAFYE KMSKLEYLAA GSTLVNAGTI YPQLANCFVM EMQDDMEHIA
KTTRDVMWLT KGTGGIGLSV TKLRAQGSPI RSNNTTSTGP IPFMHTIDSI LRAVSRGGKK
FGALCFYMEN WHLDFGEFLD LRQNSGDPYR RTRTANTAVW ISDEFMKRVQ NDDDWYLFDP
LEVADLNELY GKAFSKRYAE YVEKAERGEL RMFKKIRARE QFKAILISLQ STSHPWLTWK
DTINNRALNN NTGTIHLSNL CTEITLPQDI DNVSVCNLAS INLSRHLANG RLDFAKIEES
ARLAVRQLDN LIDITRSSVK EADYSNQQNR AVGLGVMGFT DVVEKLGLSY ESEEAYDLID
EIMEHVSYAA IDESANLAQE RGAYPNFQGS RWSQGMVPLD SIDLTEADRG VEVKVNRTSR
LDWDALRAKV KGGMRNATLM AIAPTASIGL VAGTTPGLDP QFSQIFSRAT SNGKFLEVNR
NLVTDLQRLG LWDSVREAIL RSQGDIQNIA AIPDHIKAVY KTSFQLSPYA FLEVAARAQK
WIDQAISRNM YLETRDIDDM MDIYTSAWER GVKTTYYLHM KPRHTAEQST VRVNKSEQIG
EGTKRGFGAA TPGTPAPVSA EPAAEPAVAA PARKGFGFGG LTAKDN
//
