ID A0A0C3HRU4_9VIBR Unreviewed; 760 AA.
AC A0A0C3HRU4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=SU60_10510 {ECO:0000313|EMBL:KIN10916.1};
OS Vibrio mytili.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=50718 {ECO:0000313|EMBL:KIN10916.1, ECO:0000313|Proteomes:UP000031977};
RN [1] {ECO:0000313|EMBL:KIN10916.1, ECO:0000313|Proteomes:UP000031977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 528 {ECO:0000313|EMBL:KIN10916.1,
RC ECO:0000313|Proteomes:UP000031977};
RA Gonzalez-Castillo A., Gomez-Gil B., Enciso-Ibarra J.;
RT "Draft genome of Vibrio mytili type strain CAIM 528.";
RL Submitted (JAN-2015) 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:KIN10916.1}.
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DR EMBL; JXOK01000037; KIN10916.1; -; Genomic_DNA.
DR RefSeq; WP_041155464.1; NZ_JXOK01000037.1.
DR AlphaFoldDB; A0A0C3HRU4; -.
DR STRING; 50718.SU60_10510; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000031977; 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 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}.
FT DOMAIN 5..95
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 737..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 760 AA; 85669 MW; 4209CB2749F98D9C CRC64;
MNQQLTVTKR DGRKESIDLD KIHRVITWAA EGLHNVSVSQ VELRAHIQFY DGITTSDIHE
TIIKSAADLI SEETPDYQYL AARLAVFHLR KKAYGQYEPP TLYNHVARLV DMGKYDKHIL
EDYTQAELEE LNSYIDHKRD LNFSYAAVKQ LEGKYFVQNR VTGQIYESAQ FLYILVAACL
FAKYPKETRL DYIKRFYDAT STFKISLPTP IMSGVRTPTR QFSSCVLIEC GDSLDSINAT
ASSIVRYVSQ RAGIGINAGR IRALGSEIRG GEAFHTGCIP FYKYFQTAVK CCSQGGVRGG
AATVFYPMWH GEARSLLVLK NNRGVEENRV RHMDYGVQLN KLMYQRLVEG GNITLFSPSD
VPGLYDAFFE NQVEFERLYV KYENDPSIKK ETVKAIEMFS LLMQERASTG RIYIQNVDHC
NTHSPFDSEV APVRQSNLCL EIALPTKPLS NVEDNEGEIA LCTLSAFNLG SIKSLDDFEE
LSDLVVRALD ALLDYQDYPL PAAYKSTMNR RTLGVGVINF AYYLAKNGVK YSDGSANGLT
HRTFEAMQYY LLKASVALAK EQGKCPSFDE TNYAKGLLPI DTYKKDIDLI CDEELHYDWD
GLRKEIMEHG LRNSTLTALM PSETSSQISN ATNGIEPPRG YVSVKASKDG ILKQVVPEFA
ELKNNYELLW NIGSNDGYLH LVGIMQKFVD QAISANTNYD PSRYETGKVP MKKLLQDLLT
AYKFGVKTLY YHNTRDGAKD EQKDAVQPEE EDCAGGGCKI
//