ID F9PTB7_9FIRM Unreviewed; 841 AA.
AC F9PTB7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=HMPREF9127_1236 {ECO:0000313|EMBL:EGV08793.1};
OS Parvimonas sp. oral taxon 393 str. F0440.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Parvimonas.
OX NCBI_TaxID=944565 {ECO:0000313|EMBL:EGV08793.1, ECO:0000313|Proteomes:UP000005419};
RN [1] {ECO:0000313|EMBL:EGV08793.1, ECO:0000313|Proteomes:UP000005419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0440 {ECO:0000313|EMBL:EGV08793.1,
RC ECO:0000313|Proteomes:UP000005419};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUL-2011) 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:EGV08793.1}.
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DR EMBL; AFUS01000005; EGV08793.1; -; Genomic_DNA.
DR AlphaFoldDB; F9PTB7; -.
DR STRING; 944565.HMPREF9127_1236; -.
DR eggNOG; COG0209; Bacteria.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000005419; 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..95
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 841 AA; 97012 MW; 48D7A328BDD80E2B CRC64;
MRIIKRDLSE VSFDISKIEN AIYKAFISVG DEDKKVLSKQ LAEEVFESIL QDKDENSSIS
VEEVQDYVEK TLTKNNHYET LKSYILYREK RNSLRKELNS FREYIEDESL IEVLAKIQKD
FSTEGYELDR LCRKFLSFVK PSSTLNEKVE LLIKASSELT SKENPNWEYI SARIYAYKIH
KEISNYEKEW HIVDFKSKIQ VLTKANLYGE YILENYSNDD IDELEKYIDN SRDELFTYSS
LDLVYKRYLI CDSHKKVIET MQEMFMGIAM HLAIPEKDRV SFAKKVYDVL SNLKATVATP
TMSNARKPFH QLSSCFIDTV PDTLKGIYRS IDNFAQVSKH GGGMGLYFGK VRANGSDIRG
FKGVAGGVIR WIKLANDTAV AVDQLGVRQG SCAVYLDVWH RDIPEFLNLR TNNGDDRMKA
HDVFPAICFP NLFWRLAKEN INSNWYLFCP HEVKEVMGFC LEDFYGEEWE EKYRLCIKEP
RLDKRILTVK DLVKLILKSQ VETGTPFIFN RDNANNANPN SHKGMIYSSN LCTEIMQNMK
EILDVEDKIL QIDGEDHVVT DVKAGDFVVC NLASLVLGNI DLKNDEEMEF VVSTMIRALD
NVIDLNYYPT PFAKITNAKY RAIGLGTSGY HHALVKNKIM WQTEEHLEFM DKVYEKINYF
AIKESSKIAE EKGSYKYFEG SEWQNGKYFE KREYNSEEWI ELKEKVAKNG LRNAYLLAVA
PTGSTSIIAG TTAGVDPVMM RYFLEEKKGS IIPRVAPDLT PETFWLYENA HEVDQTWSIK
AGGVRQRHID QGQSLNLYIT TDYKMSQILN LLILSCEVGL KSIYYIRSKS LDIEECDSCS
A
//
