ID A0A1U7NPB4_9FIRM Unreviewed; 837 AA.
AC A0A1U7NPB4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=BO225_03060 {ECO:0000313|EMBL:OLU47398.1};
OS Dubosiella newyorkensis.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Dubosiella.
OX NCBI_TaxID=1862672 {ECO:0000313|EMBL:OLU47398.1, ECO:0000313|Proteomes:UP000186705};
RN [1] {ECO:0000313|EMBL:OLU47398.1, ECO:0000313|Proteomes:UP000186705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NYU-BL-A4 {ECO:0000313|EMBL:OLU47398.1,
RC ECO:0000313|Proteomes:UP000186705};
RA Cox L.M., Sohn J., Tyrrell K.L., Citron D.M., Lawson P.A., Patel N.B.,
RA Iizumi T., Perez-Perez G.I., Goldstein E.J., Blaser M.J.;
RT "Description of two novel members of the family Erysipelotrichaceae:
RT Ileibacterium lipovorans gen. nov., sp. nov. and Dubosiella newyorkensis,
RT gen. nov., sp. nov.";
RL Submitted (NOV-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:OLU47398.1}.
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DR EMBL; MPKA01000050; OLU47398.1; -; Genomic_DNA.
DR RefSeq; WP_076340830.1; NZ_MPKA01000050.1.
DR AlphaFoldDB; A0A1U7NPB4; -.
DR STRING; 1862672.BO225_03060; -.
DR GeneID; 78274928; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000186705; 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:UP000186705}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 837 AA; 96654 MW; BE2D1C3825FD75E9 CRC64;
MQIEKRDHQL QTFDGHKIKN AILKAFQSVG STISQTHLDQ IVETIETEIK NAPTICTVEQ
IQDLVEEELM RFHYFKEAKS YILYRDKRSQ KRAILEKFKE RIDDPEIVAL IKRTQNEFEN
ASFLDLFHKF QTYDHPNLTS MEALDILMRC CVELISIESP DWEMIAARFL MCKLHRLTHH
YWSQKNARTF YEKIKIMEQE GYYGSYILEA YTQEEIDELE RALKPDHDLL FTYSGLDLLA
KRYLLTSHDH QLMELPQEMF MGIAMHLAIP EGERKVEWAK KIYTVLSTLK ATMATPTMAN
ARKPFHQMSS CFIDTVSDSL DGIYKSLDNF AKVSKFGGGM GMYFGKVRAS GSTIRGFEGA
AGGVIRWIKL VNDTAIAVDQ LGVRSGAVAV YLDAWHKDLP EFLALRTNNG DDRQKAHDVF
PGICYPNLFW KMAEESLDQM WYLMDPHEIH EVKGYHLEDC FGPLWEERYW DCVADPKIDK
RPILLKDLVR LIIKSAVETG TPFTFNRDIV NEANPNSHKG MIYCSNLCTE IAQNMSPLYH
IEQEIKDEQG QSIVVDTYLP GDFVVCNLAS LSLGHIDVND DQELEDVIST IIRALDNVIE
LNYAPIPFAK ITNANYRSIG LGTSGYHHML VNNKIRFESQ EHLDFVDKLY EKINYYTIKA
SHQLAKEKGA YPNFHGSEWE SGAYFRKRHY EGEAWEKLQE EVQREGLRNA YLLAIAPTSS
TSILAGTTAA IDPIMNKFFL EEKKGSMIAR IAPNLNPETF WFYKQAHHID QSWLIRAAGV
RQRHIDQSQS VNLYITNEYT LRQVLNLFIE AYRENVKTLY YVRSKSLEVE ECESCSA
//
