ID A0A1A9LEL1_9FLAO Unreviewed; 804 AA.
AC A0A1A9LEL1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=A7A78_04995 {ECO:0000313|EMBL:OAD91171.1};
OS Aequorivita soesokkakensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=1385699 {ECO:0000313|EMBL:OAD91171.1, ECO:0000313|Proteomes:UP000077552};
RN [1] {ECO:0000313|EMBL:OAD91171.1, ECO:0000313|Proteomes:UP000077552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSSK-12 {ECO:0000313|EMBL:OAD91171.1,
RC ECO:0000313|Proteomes:UP000077552};
RA Thevarajoo S., Selvaratnam C., Goh K.M., Chan K.-G., Chong C.S.;
RT "Genome sequencing of Vitellibacter soesokkakensis RSSK-12.";
RL Submitted (MAY-2016) 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}.
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:OAD91171.1}.
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DR EMBL; LXIE01000023; OAD91171.1; -; Genomic_DNA.
DR RefSeq; WP_068762260.1; NZ_LXIE01000023.1.
DR AlphaFoldDB; A0A1A9LEL1; -.
DR STRING; 1385699.A7A78_04995; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000077552; Unassembled WGS sequence.
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}.
FT DOMAIN 1..91
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 804 AA; 91393 MW; 514146AF4C810704 CRC64;
MNVVKRDGRK EPMMFDKITA RVRKLCYGLN ELVDPVKVAM RVIEGLYDGV TTSELDNLAA
EIAATMTTSH PDYARLAARI SVSNLHKNTK KSFSEVMTDL YEYVNPRTGK KAPLLSDEVF
EVIKNNAEEL DSTIIYNRDF GYDYFGFKTL ERSYLLKLNG KIAERPQHML MRVSVGIHLD
DLAAVKETYE LMSKKFFTHA TPTLFNSGTP KPQMSSCFLL AMKDDSIDGI YDTLKQTAKI
SQSAGGIGLS IHNVRATGSY IGGTNGTSNG IVPMLRVFND TARYVDQGGG KRKGSFAIYV
EPWHADIFDF LDLKKNHGKE EMRARDLFYA MWIPDLFMER VQTDAEWTLM CPNECPGLFE
CHSEEFEALY HKYEAEGKGR KTVKARELWE KILESQIETG TPYMLYKDAA NRKSNQKNLG
TIKSSNLCTE IMEFTSADEV AVCNLASIAL PMFVKNGEFD HKELFKVTKR VTKNLNRVID
RNYYPVIEAQ NSNFRHRPVG LGIQGLADAF IMLRLPFTSD EAKKLNQEIF ETLYFAAVTA
SMEEAKEDGT YETYKGSPIS EGLFQHNLWG IKDEELSGRW DWGKLRKEVK KHGVRNSLLV
APMPTASTSQ ILGNNEAFEP YTSNIYTRRV LSGEFIVVNQ HLLEDLVELG LWNEDLKEEI
MRANGSIQDV EIIPQDLKEL YKTVWELSMK DIIDMSRQRG YFIDQSQSLN LFMENANMAK
LTSMHFYAWK SGLKTGMYYL RTKSAVDAIK FTLKKEEKKE TVGAEVEANI VEDVSTKPMT
PQELREMLAQ SKNAPDDDCL MCGS
//
