ID M7NFZ4_9BACL Unreviewed; 733 AA.
AC M7NFZ4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
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:EMR06111.1};
GN ORFNames=C772_01756 {ECO:0000313|EMBL:EMR06111.1};
OS Bhargavaea cecembensis DSE10.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Bhargavaea.
OX NCBI_TaxID=1235279 {ECO:0000313|EMBL:EMR06111.1, ECO:0000313|Proteomes:UP000011919};
RN [1] {ECO:0000313|EMBL:EMR06111.1, ECO:0000313|Proteomes:UP000011919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE10 {ECO:0000313|EMBL:EMR06111.1,
RC ECO:0000313|Proteomes:UP000011919};
RX PubMed=23766406;
RA Shivaji S., Ara S., Begum Z., Ruth M., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Bhargavaea cecembensis Strain DSE10T, Isolated
RT from a Deep-Sea Sediment Sample Collected at a Depth of 5,904 m from the
RT Chagos-Laccadive Ridge System in the Indian Ocean.";
RL Genome Announc. 1:e00346-13(2013).
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 -!- PATHWAY: Genetic information processing; DNA replication.
CC {ECO:0000256|ARBA:ARBA00005160, 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:EMR06111.1}.
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DR EMBL; AOFT01000008; EMR06111.1; -; Genomic_DNA.
DR RefSeq; WP_008299182.1; NZ_AOFT01000008.1.
DR AlphaFoldDB; M7NFZ4; -.
DR STRING; 1235279.C772_01756; -.
DR PATRIC; fig|1235279.3.peg.1753; -.
DR eggNOG; COG0209; Bacteria.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000011919; 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:UniProtKB-UniPathway.
DR CDD; cd01679; RNR_I; 1.
DR Gene3D; 3.20.70.20; -; 1.
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; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011919}.
FT DOMAIN 590..612
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 733 AA; 82993 MW; F4C95ADA76371D33 CRC64;
MVTTKPTDQL DILSALEQEF TSEKIAPLRR AAEGYSGPSL SQHLIREALG RVDESETYWT
DVAARILLAQ LYRDQQERRE TEDAYGDFAR HVRTQAEAGL YTLALTEHYS ERELQEIGTF
LDPSRDRLFT YTGLKTLTDR YVATDFNKKQ VELPQERWLV IAMTLMRNET EDRLGKIKEA
YWALSNLYMT VATPTLANAG KPHGQLSSCF IDTVDDSLQG IYDSNTDIAN LSKYGGGIGV
YMGKVRSRGA AIRGFKGASS GVLPWIKQLN NTAVSVDQLG QRQGAVAVYL DVWHKDILTF
LDLKLNNGDE RLRAHDIFTG VCLPDLFMEQ VEARGDWHLF DPHEVRTVMG WSLEDFYDES
FGAGSFRERY ADCVAHPDIH SEKVPAIDIM KRIMRSQLET GVPFMFYRDE VNRMNPNKHE
GIIYSSNLCS EIAQNMSATS ASQEVLEDGV IVSRRTPGDF VVCNLSSINL GKAVPAGVLG
RLIDIQVRML DNVIDLNQIP VLQAQVTNRR YRGIGLGTFG WHHLLALNSI QWESEEAVEF
ADKLYEDIAY HTIRASAKLA GEKGAYPLFF GSDWQTGTYF GRRGYKGERW DALRVEVEKS
GVRNGYMMAV APNSSTSVIA GSTASIDPVF RPFYHEEKKD YKLPVVAPDL DHRTYDVYRR
SAYIVDQRWS VRQNAARQRH IDQSISFNLY VPNTIRASVL LDLHLQAWKS GLKTTYYTRS
TASDVEECEW CQS
//