ID A0A0E3Y6P4_9ENTR Unreviewed; 762 AA.
AC A0A0E3Y6P4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=nrdA {ECO:0000313|EMBL:AKC60040.1};
GN ORFNames=BTURN675_472 {ECO:0000313|EMBL:AKC60040.1};
OS Blochmannia endosymbiont of Polyrhachis (Hedomyrma) turneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX NCBI_TaxID=1505596 {ECO:0000313|EMBL:AKC60040.1, ECO:0000313|Proteomes:UP000033094};
RN [1] {ECO:0000313|EMBL:AKC60040.1, ECO:0000313|Proteomes:UP000033094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=675 {ECO:0000313|EMBL:AKC60040.1,
RC ECO:0000313|Proteomes:UP000033094};
RX PubMed=25861561;
RA Williams L.E., Wernegreen J.J.;
RT "Genome evolution in an ancient bacteria-ant symbiosis: parallel gene loss
RT among Blochmannia spanning the origin of the ant tribe Camponotini.";
RL PeerJ 3:E881-E881(2015).
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}.
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DR EMBL; CP010048; AKC60040.1; -; Genomic_DNA.
DR RefSeq; WP_046288937.1; NZ_CP010048.1.
DR AlphaFoldDB; A0A0E3Y6P4; -.
DR STRING; 1505596.BTURN675_472; -.
DR KEGG; bed:BTURN675_472; -.
DR PATRIC; fig|1505596.4.peg.483; -.
DR HOGENOM; CLU_000404_3_0_6; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000033094; Chromosome.
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 Gene3D; 1.10.1650.20; -; 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:UP000033094}.
FT DOMAIN 5..95
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 762 AA; 87181 MW; FF3740563B7337B9 CRC64;
MNHNLVVTKR NGSQELINLD KIHKVINWAA KNLKNVSVSQ VELRAHIQFY NGIKTSDIQE
TIIKSAADLI SQKTPDYQYL AARLSIFHLR KKAYGKFEPP KLYQHVLRLV EIGKYDKHLL
QNYSPEDFEK MNNFIDHHRD MNFSYAAVKQ LEGKYLIQNR VSGEIYESPQ FMYILISACL
FSKYSDTHRM YYIKEFYNAV STFKISLATP IMAGVRTPTR QFSSCVLIEC ADNLDSINAT
SSAIVKYVSQ RAGIGINAGR IRAIGSPIRN GEAFHTGCIP FYKHFQTAVK SCSQGGVRGG
AATLFYPIWH LEIENLLVLK NNRGIDSNRI RHLDYGVQIN KLMYQRLLER KEITLFSPSD
VPDLYNSFFE NQINFENLYV MYEKNSKIRQ KKIKAVDLFS LMMQERASTG RIYIQHVDHC
NTHSPFDSKI APIRQSNLCM EVLLPTKPLQ NINDDSGEIA LCTLSAFNLG AIDDLKDLSK
LSILLIRALD ELLDYQNYPI RSAKYSAIKR RSLGIGVINY AYYLAKNKVR YSDGSANNLT
HRTFEALQYY LLSASNTLAK ERGTCSLFHE TTYSKGILPI DTYKKDVDTL TNEKLYYNWT
KLRMNIQKYG LRHSTLSALM PSETSSQISN ATNGIEPPRG FVSIKTSKDG ILRQTVPESI
NLKNEYELLW DIPNNNGYLQ LVSIMQKFID QSISANTNYD PSRFSNSKIP MKQLLSDLLL
AYKYGIKTLY YHNTRDNAND TQQTTTQHDN PQNMCTGNAC II
//
