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Database: UniProt
Entry: A0A0L0MKS9_9MOLU
LinkDB: A0A0L0MKS9_9MOLU
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ID   A0A0L0MKS9_9MOLU        Unreviewed;       809 AA.
AC   A0A0L0MKS9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
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};
DE   Flags: Fragment;
GN   Name=nrdA {ECO:0000313|EMBL:KND62589.1};
GN   ORFNames=AlmWB_02190 {ECO:0000313|EMBL:KND62589.1};
OS   Candidatus Phytoplasma phoenicium.
OC   Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Phytoplasma; 16SrIX (Pigeon pea witches'-broom group).
OX   NCBI_TaxID=198422 {ECO:0000313|EMBL:KND62589.1, ECO:0000313|Proteomes:UP000037086};
RN   [1] {ECO:0000313|EMBL:KND62589.1, ECO:0000313|Proteomes:UP000037086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA213 {ECO:0000313|EMBL:KND62589.1,
RC   ECO:0000313|Proteomes:UP000037086};
RX   PubMed=26223451; DOI=10.1186/s12866-015-0487-4;
RA   Quaglino F., Kube M., Jawhari M., Abou-Jawdah Y., Siewert C., Choueiri E.,
RA   Sobh H., Casati P., Tedeschi R., Molino Lova M., Alma A., Bianco P.A.;
RT   "'Candidatus Phytoplasma phoenicium' associated with almond witches'-broom
RT   disease: from draft genome to genetic diversity among strain populations.";
RL   BMC Microbiol. 15:148-148(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}.
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:KND62589.1}.
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DR   EMBL; JPSQ01000044; KND62589.1; -; Genomic_DNA.
DR   RefSeq; WP_050337264.1; NZ_JPSQ01000044.1.
DR   AlphaFoldDB; A0A0L0MKS9; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000037086; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN 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   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   Gene3D; 1.10.1650.20; -; 1.
DR   Gene3D; 3.20.70.20; -; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
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; IPR004465; RNR_NrdI.
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; PF07972; Flavodoxin_NdrI; 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; SSF52218; Flavoproteins; 1.
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:UP000037086}.
FT   DOMAIN          681..703
FT                   /note="Ribonucleotide reductase large subunit"
FT                   /evidence="ECO:0000259|PROSITE:PS00089"
FT   NON_TER         809
FT                   /evidence="ECO:0000313|EMBL:KND62589.1"
SQ   SEQUENCE   809 AA;  93150 MW;  C7F2E1E17A8C1414 CRC64;
     MKIVFDSSEK GNVYDFVKKL EHKYKIEEIK NFKNDEKDIF LVTKTIKFGE ISEITESFLK
     KYFYLVIGIA VSGNKNFGKN FAKAGDLISE KFNIPLILKF EGKGFEEDVL FLKNWLEENE
     KIKRKNKKIP NWIILNNQIL DEEGNIKNLQ KDKEAIESFL NEEIKPKTKK FPSLKEKLNF
     LIENNFYEKN FLEKYNYKEI KKVFDIAYNE KFIFPSFIGA FKFYNGYSLK TRDKKEYLET
     YEDRLAINAL YHASGNKELA INLIKNLIKQ NFTPATPTLL NTGLKKRGEF VSCFLLEGGD
     SLNDISRIVE FSMQLSKIGG GVSINLSNLR AKGESIKEIS NTCKGVIGVA KLLDYSFRYA
     DQMGQRLGAG VAYLNVFHAD IEDFLNSKKL NADEDIRLKT LSLGVVIPDK MIELARKKEK
     MAIFFPHTVF KAYGLNFADI SIEMDKWYDV LLKNPDVRKK FIDPRRLLEL IALLQGESGY
     PYIMFCDNVN RDNTSINKVK FSNLCTEILQ PSITSHYAPY DKREMDEIGM DISCNLSSGH
     MGNMIKNKTI KETIFAAFEI MNSVSLKTNI NYVPGIAKAN RLNRSVGFGI MGHHGFIAEK
     LIEFGSEEDI ELIDVFFSAV NYYSLLHSNL EAKKTGQKFY KFEESTYANG EYFKNRKAIL
     PKKSKIKEIF EEIELPTDND WLVLAENIKK YGLYNSHRLA VAPNGTIGYI MSATPSLTPI
     KQLVEERTYG NSKTYFPVPA LKDFAFMYQT AYRMDKKKII DVIATAQKHI DQGISFELCI
     TSNTTTRELV KYYLYAHKKG IKTLYYTRT
//
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