ID A0A2A7UZ87_COMTR Unreviewed; 963 AA.
AC A0A2A7UZ87;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=CRM82_20430 {ECO:0000313|EMBL:PEH90649.1};
OS Comamonas terrigena.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=32013 {ECO:0000313|EMBL:PEH90649.1, ECO:0000313|Proteomes:UP000220246};
RN [1] {ECO:0000313|Proteomes:UP000220246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_394 {ECO:0000313|Proteomes:UP000220246};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (SEP-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}.
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:PEH90649.1}.
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DR EMBL; PDEA01000001; PEH90649.1; -; Genomic_DNA.
DR RefSeq; WP_066537600.1; NZ_UIGV01000001.1.
DR AlphaFoldDB; A0A2A7UZ87; -.
DR STRING; 1219032.GCA_001515545_02197; -.
DR GeneID; 80803003; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000220246; 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; 2.
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:UP000220246}.
FT DOMAIN 23..123
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 144..233
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 125..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 106862 MW; 9D4761E770F85977 CRC64;
MQDAPNTLSA DQPTTTQVAL ETYQVIRRSG DVVPFAPQKI ATAATKAFLA VRGAQGAASA
SVRETVDSLT HAVIRALVRS RPGGGTFHIE DIQDHVELGL MRGGHQDVAR AYVLYREARN
QERAAAKKKA EEEAAAAAAP KPTLHVTDNG QRQPLDQERL QALFEAACRN LNPDISAAPI
LSETLRNLYD GVPLAEVYKA AILAARTLIE TDPDYTYVTA RLLLHTIVRE VMGRDVQPAD
MDAAYADYFP GFIQKGVDNE LLNPELLKFD LPRLGKALKA ERDQQFDYLG LQTLYDRYFL
HVRKTRIELP QSFFMRVAMG LALQESDRDA RAIEFYELLS SFDFMSSTPT LFNSGTLRSQ
LSSCYLTTVS DDLGGIYDAI KENALLSKFA GGLGNDWTNV RALGARIKGT NGESQGVVPF
LKVVNDTAVA VNQGGKRKGA VCAYLETWHL DIEEFLELRK NTGDDRRRTH DMNTANWIPD
LFMKRVVENG EWTLFSPSDV PELHDLFGQA FEKAYTAYEA KTQTGEITLF KRVPAVDVWR
KMLSMLFETG HPWITFKDPC NIRSPQQHVG VVHSSNLCTE ITLNTSDSET AVCNLGSVNL
ARHITNGAID HAKLRKTITT AMRMLDNVID INYYAVDKAR DSNMRHRPVG MGIMAFQDAL
YEMRTPYASQ AAVEFADAAM EAVCYYAYWA STELAKERGT YSSYQGSLWS QGILPLDSLN
LLEKERGGYV DVDRTVRLDW EALRAKIQAD GMRNSNCVAI APTATISNIV GVDASIEPSF
GNLSVKSNLS GEFTVINQFL VRDLKKLGLW DEVMVMDLKH FDGSLRPIER VPHDLKQLYA
TAFEVEPHWL VEAASRRQKW IDQAQSLNIY MAGASGKKLH DTYLLAWQRG LKTTYYLRTI
SATHVEKSTV QSRVLNAVSA NAPAAMASMS ALEKAAAAAR AQQAPATDIK FCAIDDPGCE
ACQ
//
