ID A0A1F1K991_9MICO Unreviewed; 851 AA.
AC A0A1F1K991;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=HMPREF3099_06110 {ECO:0000313|EMBL:OFS13374.1};
OS Kytococcus sp. HMSC28H12.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Kytococcaceae;
OC Kytococcus.
OX NCBI_TaxID=1581067 {ECO:0000313|EMBL:OFS13374.1, ECO:0000313|Proteomes:UP000176675};
RN [1] {ECO:0000313|EMBL:OFS13374.1, ECO:0000313|Proteomes:UP000176675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC28H12 {ECO:0000313|EMBL:OFS13374.1,
RC ECO:0000313|Proteomes:UP000176675};
RA Ploux O.;
RL Submitted (MAR-2016) 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:OFS13374.1}.
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DR EMBL; LWPN01000207; OFS13374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F1K991; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000176675; 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:UP000176675}.
FT DOMAIN 12..101
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 851 AA; 93133 MW; 9D0A5315785226CF CRC64;
MDGTPTTSRH PMRVVKRSGE HEEVDLAKIV TAIERCTDGL PEVDPMRVAT RTIAGLYDGA
TTAELDKLAI ATAAEMTATE PQYSRLAGRL LAGTIDKEVR GQGIATFSQA VRTGHEQGLI
GDVTAAFVAE HASLLDDAVH RAQAAHADWR FDYFGLRTVY DRYLLRHPLT RAVIESPQYW
LMRVAAGLSR TAPEAVEFYE LLSSLAYLPS SPTLFNSGPR HTQMSSCYLI DSPRDDLDSI
YERYHQVAKL SKFAGGIGLA FSRIRSRGAL IRGTNGHSNG IVPWLRTLDS SVAAVNQGGR
RKGAACIYLE PWHPDVEEFL ELRDNTGEDA RRTHNLNLAH WIPDEFMRRV EADGEWSLID
PDAVPELPDL WGPAFDAAYR AAEERGDVVR TVSARYLYGR MMRTLAQTGQ GWMTFKDASN
RACNQTSDDQ TPRVAADGTV QPAPVVHLSN LCTEIIEVTS NDETAVCNLG SVNLAQHLRW
SDGTTGARPQ DAAARAVGVD EEKLRATVRL AVTYLDRVID INYYPSEQAA ASNPRWRPIG
LGSMGLQDVF FALRMPFDSP EARELSTRIA EEIQLSALER SAELAEQLGA HPSFDETRAA
KGQLQHDLYG VTPTQTERWA AVRARIAEHG LRNSLMIAIA PTATIASIAG CYECIEPQVS
NLFKRETLSG EFMQVNTALV DELKSLGLWT DTVREKLKAD NGSVAGIADL PEEARRLFRT
AWELPQKALI EMAAARQAYV DQSQSLNLFM ESPHIGKLSS MYLYAWKAGL KTTYYLRSRP
ATRIQQATVS GVRAGASWGA ATGAPGASQP TAPGAPGVVG GLTASEPVRT FTDAEALACS
LENPEACEAC E
//
