ID H6Q5J6_WIGGL Unreviewed; 704 AA.
AC H6Q5J6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=nrdE {ECO:0000313|EMBL:AFA41479.1};
GN ORFNames=WIGMOR_0677 {ECO:0000313|EMBL:AFA41479.1};
OS Wigglesworthia glossinidia endosymbiont of Glossina morsitans morsitans
OS (Yale colony).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Wigglesworthia.
OX NCBI_TaxID=1142511 {ECO:0000313|EMBL:AFA41479.1, ECO:0000313|Proteomes:UP000009061};
RN [1] {ECO:0000313|EMBL:AFA41479.1, ECO:0000313|Proteomes:UP000009061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WGM {ECO:0000313|EMBL:AFA41479.1};
RX PubMed=22334516;
RA Rio R.V., Symula R.E., Wang J., Lohs C., Wu Y.N., Snyder A.K.,
RA Bjornson R.D., Oshima K., Biehl B.S., Perna N.T., Hattori M., Aksoy S.;
RT "Insight into the transmission biology and species-specific functional
RT capabilities of tsetse (Diptera: glossinidae) obligate symbiont
RT wigglesworthia.";
RL MBio 3:E00240-11(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|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; CP003315; AFA41479.1; -; Genomic_DNA.
DR RefSeq; WP_014354417.1; NC_016893.1.
DR AlphaFoldDB; H6Q5J6; -.
DR STRING; 1142511.WIGMOR_0677; -.
DR KEGG; wgl:WIGMOR_0677; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_4_1_6; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000009061; Chromosome.
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:InterPro.
DR CDD; cd01679; RNR_I; 1.
DR Gene3D; 1.10.1650.20; -; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR026459; RNR_1b_NrdE.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013554; RNR_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR NCBIfam; TIGR04170; RNR_1b_NrdE; 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 Pfam; PF08343; RNR_N; 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}.
FT DOMAIN 556..578
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 704 AA; 80691 MW; 73AF13EE7A4BB702 CRC64;
MHKIDYHALN AMLNLYDDKG HLQLEKDALA IKSYFNKHVL PNTRDFISLQ DRISYLVQEG
YYELKILNNY KKNFVYSLFN QSKKQGFRFQ TFMGVLKFYS SYALKTFDGK YYLENFEDRT
CMVALTLGGG NELFAMNIMK EILSGRFQPA TPTFLNCGKK QRGEYISCFL LRIEDNMESI
GRAINAALQL SKRGGGVSFL LTNLRESGAP IKYVKHQSSG IVPIMKMLED AFSYANQLGA
RQGAGAVYLH AHHPDILKFL DTKKENADEK TRIKTLSLGV IIPDITFQLA KENKEMYLFS
PYDVEKVYHQ PFSELVISEI YHNLSQDKRI KKTTINARNF FQKLAEIQFE SGYPYIMFED
TVNRTNPIFG HINMSNLCSE ILQVNSPSEY NEDLSYKKIG TDISCNLGSL NIANTMESSN
LGRTVEIAIR SLTAVSDISQ IHSVSSILNG NNKSHAIGLG QMNLHGYLAR EKIYYGSPES
IEFTNLYFYI ITYHAIRTSN LLAIERKKKF WGFSKSNYAN GKYFLKYTTQ TWKPKNHRVL
HLFKKNKIHL PTQEEWKALA KSVKKYGLYN QNLQAIPPTG SISYINHSTS SIHPIVSRIE
IRKEGKIGRV YYPAPYMTNN NLCYYKDAYE IGPKKIIDVY AAATQHIDQG LSLTLFFRDN
VTTRDINKAQ IYAWKKGIKT LYYVRIRQLT LKGTEVSGCV SCAL
//
