ID   A0A385BP76_9FLAO        Unreviewed;       825 AA.
AC   A0A385BP76;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
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   ORFNames=CJ739_1853 {ECO:0000313|EMBL:AXP80938.1};
OS   Mariniflexile sp. TRM1-10.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Mariniflexile.
OX   NCBI_TaxID=2027857 {ECO:0000313|EMBL:AXP80938.1, ECO:0000313|Proteomes:UP000259852};
RN   [1] {ECO:0000313|Proteomes:UP000259852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TRM1-10 {ECO:0000313|Proteomes:UP000259852};
RA   Kim J.F., Kwak M.-J.;
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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; CP022985; AXP80938.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A385BP76; -.
DR   KEGG; marf:CJ739_1853; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000259852; 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   CDD; cd01679; RNR_I; 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:UP000259852}.
FT   DOMAIN          1..91
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   825 AA;  93695 MW;  4E34937431AAE143 CRC64;
     MYVVKRNGRK EQIMFDKITA RVRKLCYGLN ELVDPLKVTM RVIEGLYDGV TTSELDNLAA
     EISATMTTAH PDYARLAARI SVSNLHKNTK KTFSEVMHDL YTYINPRTGK DAPLLADDVY
     EVIMKNKDVL DSTIIYNRDF GYDYFGFKTL ERSYLLKLNG QIAERPQHML MRVAVGIHLD
     DLESVIETYE LMSKKYFTHA TPTLFNSGTP KPQMSSCFLL TMKDDSIDGI YDTLKQTAKI
     SQSAGGIGLA IHNIRATGSY IAGTNGTSNG IVPMLQVFND TARYVDQGGG KRKGSFAIYI
     ETWHADIFDF LDLKKNHGKE EMRARDLFYA MWISDLFMKR VQEDGPWTLM CPNECPGLDE
     VHSDAFEALY LRYEAEGKGR KTIKARELWE KILESQIETG TPYMLYKDAA NRKSNQQNLG
     TIRSSNLCTE ILEYTSPDEV AVCNLASIAL PMFVKNGEFD HKELFRITKR VTKNLNRVID
     RNYYPVKEAE NSNMRHRPIG LGVQGLADTF IQLRMPFTSD EAKKLNQDIF ETLYFAAVTA
     SMEEAKVDGP YQSYKGSPIS KGEFQHNLWG LKDEELSGMW EWAKLRKQVL KHGVRNSLLV
     APMPTASTSQ ILGNNECFEP YTSNIYTRRV LSGEFIVVNK HLLEDLVELG LWNDGLKQEI
     MRANGSVQGI EIIPQEIKEL YKTVWELSMK DIIDMSRQRG YFIDQSQSLN LFMEGATMAK
     LTSMHFYAWK SGLKTGMYYL RTKSAVDAIK FTLQTTKKEE PTTEGVEVVN QDVVQKQKKH
     IAEKTAVKFA KQQAPEIEPM SAEEMKILIA QAKAAEGDDC LMCGS
//