ID I3QGN3_9FLAO Unreviewed; 570 AA.
AC I3QGN3;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN Name=nrdA {ECO:0000313|EMBL:AFJ90768.1};
GN ORFNames=BGIGA_323 {ECO:0000313|EMBL:AFJ90768.1};
OS Blattabacterium sp. (Blaberus giganteus).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Blattabacteriaceae; Blattabacterium.
OX NCBI_TaxID=1186051 {ECO:0000313|EMBL:AFJ90768.1, ECO:0000313|Proteomes:UP000006466};
RN [1] {ECO:0000313|EMBL:AFJ90768.1, ECO:0000313|Proteomes:UP000006466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGIGA {ECO:0000313|EMBL:AFJ90768.1,
RC ECO:0000313|Proteomes:UP000006466};
RX PubMed=22843586; DOI=10.1128/JB.00789-12;
RA Huang C.Y., Sabree Z.L., Moran N.A.;
RT "Genome Sequence of Blattabacterium sp. Strain BGIGA, Endosymbiont of the
RT Blaberus giganteus Cockroach.";
RL J. Bacteriol. 194:4450-4451(2012).
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|RuleBase:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
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DR EMBL; CP003535; AFJ90768.1; -; Genomic_DNA.
DR RefSeq; WP_014726639.1; NC_017924.1.
DR AlphaFoldDB; I3QGN3; -.
DR STRING; 1186051.BGIGA_323; -.
DR KEGG; bbg:BGIGA_323; -.
DR PATRIC; fig|1186051.3.peg.318; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_7_0_10; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000006466; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:InterPro.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR039718; Rrm1.
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; 3.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003410}.
FT DOMAIN 26..90
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 94..221
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 224..394
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 400..549
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 570 AA; 65072 MW; 3D6AD5FFBE05EA60 CRC64;
METHPIAEKE GWKVGKDFPV WANNELYLTT IKGGYLLDGE TPFEAYNRLA KNAAKILKKP
KIEGEFFNIF WRGWLIPSTP VMVNLGTEKG LPISCFSGRI GDSMYEIYRK NLEMAILSKH
GGGTSYDFSL VRPVGSSIKN GTLGNSDGII PFIKSYDSAI VASKQGRTRR GAVAIYLNIE
HKEYPEFLKI REPKGDINRQ CHNVHQGVII SNSFMEKVLQ KNGKERSLWI DTLKERVQTG
EPYLFFKENA NKNLPENWKK HGLKIHHSNL CSEIMLPTDE SHTLVCCLSS LNLYKYIEWK
NTNTVFYSIL FLDAVMQEFI DKGKHIRGIE DSVRFAEKSR ALGLGTLGWH SYLQSNMIPF
ISIKSEMLTH NIFRNIQLES QKATKYLAKE YGESEWNIGT GRRNLTLMAM APNRSSAKLA
GGLSQGVEPL AANIYVDDDS KGMHIRKNPY LENILIKNGY NIPEVWEQIA NEKGSCLGLT
ALNEEQKNVF RCFKEINQLE LIKQASIRQK YIDQGQSINL SFHQNAPAKY INKVHIEAWK
IGLKSLYYYR SESILRADTR NRDLYSESLL
//
