ID A0A1N7PYR2_9BACT Unreviewed; 800 AA.
AC A0A1N7PYR2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN05421761_12319 {ECO:0000313|EMBL:SIT15726.1};
OS Belliella pelovolcani.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Belliella.
OX NCBI_TaxID=529505 {ECO:0000313|EMBL:SIT15726.1, ECO:0000313|Proteomes:UP000186026};
RN [1] {ECO:0000313|EMBL:SIT15726.1, ECO:0000313|Proteomes:UP000186026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46698 {ECO:0000313|EMBL:SIT15726.1,
RC ECO:0000313|Proteomes:UP000186026};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-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}.
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DR EMBL; FTOP01000023; SIT15726.1; -; Genomic_DNA.
DR RefSeq; WP_076502991.1; NZ_FTOP01000023.1.
DR AlphaFoldDB; A0A1N7PYR2; -.
DR STRING; 529505.SAMN05421761_12319; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000186026; 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..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 800 AA; 90551 MW; B0FB32683AFB1622 CRC64;
MLVIKRDGRR ESVRFDKITA RIENLCYGLD NRYIQPIEVA KKVIDGLYDG VTTTELDNLA
AEICASLTVK HPEYATLAAR IAISNLHKTT SQSFSNTMKR LYTYINPKTG ENAALIAQDV
YGIIKKNAAK LDEAIDYNRD FSYDYFGFKT LERSYLTRLD GKVVERPQHM LMRVSVGIHK
EDIEAAIETY NLLSEKWFTH ATPTLFNAGT PKPQLSSCFL LTMKDDSIDG IYDTLKQCAK
ISQSAGGIGL SIHNVRAKGS YIKGTNGVSN GIVPMLRNFD MTARYVDQGG GKRKGSFAIY
LEPWHADVKD FLELKRNHGK EEMRARDLFY AMWIPDLFMK RVEQNESWSL FCPNEAPGLA
DCYGAEFEKL YEKYEREGIA RETVKAQELW FEILESQIET GTPYMLYKDA ANMKSNQKNL
GTIKSSNLCT EIIEYTAPDE VAVCNLASIA LPKFVLEGKD GVKYFDHQKL YEITKVATRN
LNKVIDVNYY PVEEARRSNF RHRPIGLGVQ GLADAFILLR MPFDSEEAKR LNEDIAETMY
FAAMETSMEL AKVEGTYETY EGSPVSQGLF QFDHWNVTPK SGRWNWSELK AKVKKYGIRN
SLLVAPMPTA STSQILGNNE CFEPYTSNIY TRRTLSGEFI VVNKHLMRDL INLGLWNDNL
KNRLIAANGS VQNIPGIPQN IKDLYKTVWE ISQKNIIDMA ADRGAYICQS QSMNVFLQDP
NFGKLTSMHF YAWKKGLKTG MYYLRSQAAT SAIQFTVDKA ALNVDSQAQP VSSDLTMTQQ
KQDAIACSLD NPDDCEMCGS
//
