ID A0A0Q9LGH7_9MICO Unreviewed; 800 AA.
AC A0A0Q9LGH7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, 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 ORFNames=ASG70_14440 {ECO:0000313|EMBL:KRE52582.1};
OS Phycicoccus sp. Soil748.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=1736397 {ECO:0000313|EMBL:KRE52582.1, ECO:0000313|Proteomes:UP000051855};
RN [1] {ECO:0000313|Proteomes:UP000051855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil748 {ECO:0000313|Proteomes:UP000051855};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE52582.1, ECO:0000313|Proteomes:UP000051855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil748 {ECO:0000313|EMBL:KRE52582.1,
RC ECO:0000313|Proteomes:UP000051855};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRE52582.1}.
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DR EMBL; LMSC01000012; KRE52582.1; -; Genomic_DNA.
DR RefSeq; WP_056885022.1; NZ_LMSC01000012.1.
DR AlphaFoldDB; A0A0Q9LGH7; -.
DR STRING; 1736397.ASG70_14440; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000051855; 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}.
FT DOMAIN 24..113
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 800 AA; 89031 MW; 9CA7829099F690DC CRC64;
MTQAPVVEDS TTEPTPPTAR RTTMAVRKRN GDSEPVDVMK IVRAVERWCD DLDEVDPTVI
ATRTISGLYD GATTAELDRL SIQTAAEMTA TEPQYSRLAA RLLSNYIDKE VRGQQIASFS
QAVRLGHLEG LIGDDTAAFV EANARKLDHA VDVAHDRRFE YFGLRTVYDR YLLRHPETRS
VIETPQYFLL RVACGLASTP QEAIAFYRLM ASLAYLPSSP TLFNSGTRHT QMSSCYLVDS
PRDQLESIYD RYTQVARLSK FAGGIGISWS RVRSRGALIR GTNGHSNGIV PWLRTLDSSV
SAVNQGGRRK GAACVYLEPW HPDIEEFLEL RDNTGEDARR THNLNIANWV PDEFMRRVEA
DEQWSLVDPD QVPELPDLWG PAFEKAYAAA ERDGRVVRTV SARELYGKMM RTLAQTGNGW
MTFKDASNRT CNQTSDEQGP GAPVVHLSNL CTEIIEVSSD TETAVCNLGS VNLAQHLTAP
RNGVDWERLR ETVRTAVTYL DRVIDINYYP SEESGASNPR WRPVGLGVMG LQDVFFALRL
PFDSDEAREL STRVAEEVYL SALERSAELA SEHGPHPAYE QTRAARGDLQ PDLWSVTPTQ
AERWAALRAA VQDNGLRNSL LVAIAPTATI ASIAGVYECI EPQVSNLFKR ETLSGEFLQV
NTALVRELKA RDLWTPEVRE AIKRSEGSVQ GISAIPADVR HLFRTAWELP QRALIDLAAA
RQPFIDQSQS LNLFLAAPTI GKLSSMYLYA WKAGLKTTYY LRSRPATRIQ QATVSVAVKP
TDQEAVACSL ENPETCEACE
//
