ID R7ILB7_9BURK Unreviewed; 838 AA.
AC R7ILB7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=BN620_02176 {ECO:0000313|EMBL:CDE52251.1};
OS Sutterella sp. CAG:351.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=1262975 {ECO:0000313|EMBL:CDE52251.1, ECO:0000313|Proteomes:UP000018107};
RN [1] {ECO:0000313|EMBL:CDE52251.1, ECO:0000313|Proteomes:UP000018107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:351 {ECO:0000313|Proteomes:UP000018107};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDE52251.1}.
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DR EMBL; CBJA010000383; CDE52251.1; -; Genomic_DNA.
DR AlphaFoldDB; R7ILB7; -.
DR STRING; 1262975.BN620_02176; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000018107; 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..90
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 838 AA; 95256 MW; E682887164968C4E CRC64;
MLITKRSGQT EEYDRKKIAL AITKAFKSTG IEQPDDLDEL LDLVEKQILV TPGCSVETIQ
DRVEEALMQR GHYQVAKNFI LYREKRTELR TCRLALSVAT GDSDLDGCLF EIQNDFKAPE
YSLEVLTAKF NSQVSPTASV DEKLDTLIRS AVELTTQNAP RYEQIAGRLL CHSFKRKLAQ
RKQNLGLTDF YTKLMFLTEH GLYGKYILEN YTKEEIDEAA GLIDENRNKL FNYSGLQLVL
ERYVIKSHNN EILESPQELF LGVALHLAMP EKKDVRMQYV KRFYDMLSKL EVTMATPTLA
NARKPYHQLS SCFIDTVPDS LAGIYRSLDN FAQVSKFGGG MGLYFGKVRA RGSDIRGFKG
AAGGVSRWIK LVNDTAVAVD QLGVRQGSVA VYLDIWHRDI PEFLQMRTNN GDDRLKAHDT
FPALCVPDYF WQQVRDNFNG VWYLMCPHEI SQVRGYNLED SFGEEWTKRY LECVHDNRIT
KREISLKDLV RLFLKSVVET GTPFIFNRDL VNAMNPNAHC GHIYSSNLCT EIAQNTAPIQ
SVSREIKTSE GTVEVVTTTK PGDFVVCNLA SLNLGRIPVD EPGYLEHLTS SVVRALDNVI
DLNFYPTPYA EITSKRYRAI GLGVSGYHHM LAKHGIRWES EEHLAFVDKV FERIAHSAIE
TSALNAKDKG TYGMYKGSDW DTGAFFEKRG YNTPYWDDVK ADVAKYGMRN GYLMAIAPTG
STSIIAGTTP GIDPIMNRYF LEEKKNGLLP RVAPDLSSDT WWLYKNAHLI DQNWSIRACG
VRQRHIDQAQ SINLYITNDF TMRKVLNLYL EAWKCGVKTI YYIRSKSLEV EECESCSS
//
