ID A0A317MZF4_9GAMM Unreviewed; 1155 AA.
AC A0A317MZF4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=C7443_10140 {ECO:0000313|EMBL:PWV65556.1};
OS Plasticicumulans acidivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria;
OC Candidatus Competibacteraceae; Plasticicumulans.
OX NCBI_TaxID=886464 {ECO:0000313|EMBL:PWV65556.1, ECO:0000313|Proteomes:UP000246569};
RN [1] {ECO:0000313|EMBL:PWV65556.1, ECO:0000313|Proteomes:UP000246569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23606 {ECO:0000313|EMBL:PWV65556.1,
RC ECO:0000313|Proteomes:UP000246569};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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:PWV65556.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QGTJ01000001; PWV65556.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317MZF4; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000246569; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; 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:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR CDD; cd00081; Hint; 1.
DR Gene3D; 3.20.70.20; -; 2.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
DR Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
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; PF14528; LAGLIDADG_3; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR SUPFAM; SSF55608; Homing endonucleases; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 2.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW Reference proteome {ECO:0000313|Proteomes:UP000246569}.
FT DOMAIN 419..566
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
SQ SEQUENCE 1155 AA; 126849 MW; E9BDC56357B3A3A1 CRC64;
MIHSPPALQP PQAALSAVDA LLAATEAATL ALDLPLLREL AISHGAAQAG AEVHSALLLA
ARTLIERDPA YDALAVRLQL LALGHEVLGA EALTLSALAA HYPAALPAFV TEGIAAEQLD
PRLGEFDLAR LAAALRPERD RQFGYLGLQT LYDRYFLHID GRRIELPQVF FMRVAMGLAL
NEAEREARAI EFYELLSSFA FMCSTPTLFN AGTCHPQLSS CYLTTVDDDL EAIFQAVKEN
ALLQKYAGGL GNDWTPVRAL GSRIRGTNGI SQGVIPFLKV VNDTAVAVNQ CFAPDTVVFT
ADGPRPIREV IAGDLVLGCS GRYREVTQKF TYNQREPMLR LDVTHALAPL HVTTGHPFYA
IRGVPPQQTG AHTRHGLEQG TLRPQWVEAG ALQRGDYVAQ VIPREIVPVA AFDADDARLY
GILLGAGQLS DDVHWHVSGD PQRDTHLAFV RTYLQARGIP CREIHHGEDE LQIHWAIERC
LLREASGGSL SAGSAALSVT QADVVDARGR RRIARRFAHL PLPQTLALLH GLLEAGGSIR
GKVIHFSSAS QPLAEGLRYQ LLRLGVPCAG RYREPPPAPG TQAASAEADG PLPSWALRIP
AVPELAERLG CTPLRRRHWL NHGGRLYSRV RQVSAQAPCP FVIDLKVEGD ASYMTSAGLA
HNGGKRKGAV CAYLETWHLD IEDFLELRKN TGDERRRTHD MNTANWIPDL FMQRVAADAE
WTLFSPSDVP DLHQRYGRDF ARAYEAYEAA AARGEIRLFR RLPARQLWRK MLTMLFETGH
PWLTFKDACN LRSPQQHVGV VHSSNLCTEI TLNTAADETA VCNLGSVNLR AHLRDGALDA
ERLARTVNTA MRMLDNVIDL NYYATPKARN ANLRHRPVGL GIMGFADCLH ALGLPYASDA
AVEFADRSME LVCFHAYRAS SELAVERGCY SSFAGSLWAQ GVLPPDTLAR LRDERGGDVE
LDMSATLDWA ALRAQISEHG MRNSNCVAIA PTATIANIVG VSASIEPEYR NLYVKSNLSG
EFTVVNADLL RELRARGLWD EAMLHELKRA DGALGRIARV PAPLKALYAT AFEIDPEWLV
EAAARRQKWI DQAQSLNLYV AGRSGRQLDA LYQLAWRRGL KTTYYLRTLG ATHTDAATLE
APLCSIDQPD CEACQ
//
