ID A0A1E5IPH0_SHECO Unreviewed; 762 AA.
AC A0A1E5IPH0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=BEL05_05625 {ECO:0000313|EMBL:OEG72451.1};
OS Shewanella colwelliana (Alteromonas colwelliana).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=23 {ECO:0000313|EMBL:OEG72451.1, ECO:0000313|Proteomes:UP000095230};
RN [1] {ECO:0000313|EMBL:OEG72451.1, ECO:0000313|Proteomes:UP000095230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSB03KR {ECO:0000313|EMBL:OEG72451.1,
RC ECO:0000313|Proteomes:UP000095230};
RA Hong H.-H., Choi H., Cheon S., Oh J.-S., Lee H.-G., Park C.;
RT "Whole-genome of two Shewanella species isolated from a digestive organ of
RT sea cucumber Apostichopus japonicus Selenka 1867.";
RL Submitted (JUL-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:OEG72451.1}.
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DR EMBL; MCBT01000048; OEG72451.1; -; Genomic_DNA.
DR RefSeq; WP_028763881.1; NZ_MCBT01000048.1.
DR AlphaFoldDB; A0A1E5IPH0; -.
DR STRING; 23.BEL05_05625; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000095230; 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"
SQ SEQUENCE 762 AA; 85810 MW; D75C45B902FF30D9 CRC64;
MNSNMQVTKR SGERETIDLD KIHRVITWAA KGLKNVSVSE VELRSHLQFY DGIPTEAIHE
TIIKAAADLI SPESPDYQFL SARLAIFHLR KKAFGQFEPP KLYDHVVKLV ELGKYDTHIL
NDYSREEIDI LGSYIDHWRD MNFSYAAVKQ LEGKYLVQNR VTHDIYESAQ FLYILVAACL
FAKYPKDTRL QYVKDFYDAT STFKISLPTP IMAGVRTPTR QFSSCVLIEC GDSLDSINAT
ASSIVKYVSQ RAGIGVNAGR IRALGSPIRG GEAFHTGCLP FYKYFQTAVK SCSQGGVRGG
AATLFYPMWH LEVESLLVLK NNRGVDDNRI RHLDYGVQIN KLMYQRMIQG GVISLFSPSD
VPGMYDAFFE DQQEFERLYL KYEADKSIRR KEVKAVELFA LMMQERASTG RIYIQNVDHC
NTHSPFDSKV APVRQSNLCL EIALPTKPLN NINDPDGEIA LCTLSALNLG AIKKLEELEP
LADLAVRALD NLLDYQDYPI TSAHKASMNR RTLGIGVINF ANYLAKEGVR YSDGSANGIT
HKTFEAIQYY LLKASVNLAK EQGACPLFHE TNYAKGILPI DTYKRDLDKI CDEPLHMDWE
TLREEIKTHG LRNSTLSALM PSETSSQISN ATNGIEPPRG LISVKSSKDG QLKQVVPDFD
KYQYSYELLW QMPNNDGYLQ LVGLMQKFVD QSISANTNYD PSRFPGNKVP MQVLLKDLLT
AYKYGVKTLY YHNTRDGASD SHDDITAIEK EDDSCAGGAC KI
//
