ID G4Q589_ACIIR Unreviewed; 760 AA.
AC G4Q589;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
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 Name=nrdA {ECO:0000313|EMBL:AEQ23267.1};
GN OrderedLocusNames=Acin_2064 {ECO:0000313|EMBL:AEQ23267.1};
OS Acidaminococcus intestini (strain RyC-MR95).
OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Acidaminococcus.
OX NCBI_TaxID=568816 {ECO:0000313|EMBL:AEQ23267.1, ECO:0000313|Proteomes:UP000007093};
RN [1] {ECO:0000313|EMBL:AEQ23267.1, ECO:0000313|Proteomes:UP000007093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RyC-MR95 {ECO:0000313|EMBL:AEQ23267.1,
RC ECO:0000313|Proteomes:UP000007093};
RX PubMed=22123762; DOI=10.1128/JB.06301-11;
RA D'Auria G., Galan J.C., Rodriguez-Alcayna M., Moya A., Baquero F.,
RA Latorre A.;
RT "Complete genome sequence of Acidaminococcus intestini RYC-MR95, a Gram-
RT negative bacterium from the phylum Firmicutes.";
RL J. Bacteriol. 193:7008-7009(2011).
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; CP003058; AEQ23267.1; -; Genomic_DNA.
DR RefSeq; WP_009014632.1; NC_016077.1.
DR AlphaFoldDB; G4Q589; -.
DR STRING; 568816.Acin_2064; -.
DR GeneID; 72311610; -.
DR KEGG; ain:Acin_2064; -.
DR PATRIC; fig|568816.4.peg.2000; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_9; -.
DR InParanoid; G4Q589; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000007093; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007093}.
FT DOMAIN 3..105
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 760 AA; 86739 MW; F8DD3556B223366E CRC64;
MDIMIRKRDG HFEPLSVEKT KRMIAFACLG LDSCDPMELE MDSKLQFVDG MTTKQIQQTL
IRTAIEKVIP SRHEGGGVPL QEMNPDWQFV AARLFLFDLY KEAAIQRRYK AFGYGNFSNL
IHMLVDKKKY ADFFVTDYTE DELQELGDYI KPKRDYLFNY EGLKLLADRY LVRGFNKEVY
ELPQERFMAI AMHLALVEGK NKVAYAKKFY DLMSELKMTT ATPTLANAGT PFHQLSSCFV
AGVDDNLWSI YDVNSKFSRV SKHGGALGIY LGKVRALNSD IRGFKNSSGG VIPWVRLYND
TAVAVDQLGR RKGGATVTLD IWHKDFYEFV ELRTNNGDDR RKAHDIFPSI SVPNLFMERL
IKRENFTLFD PHEVNTVMGF ALEDFYDTEE DKAFTEHYLA CEKDSRLHGI SVPALEMMKK
IMKSAVETGT PFIFFRDTVN EANPNKHAGM IYASNLCHEI AQNVGFTNLK KEILEDDGTI
TTVTAPGDMV TCNLNSINLG KIDEDFLEEQ IALQVRMLDN VITINQTPVP ESRLTCDKYR
AIGLGTSGYH HYLVKHGLRW ESKEHIAAAD ALFEKIAYYA IKASMELSKE KGAYPAFKGS
EWDTGKYFTR RGYTSEKWQR LAADVHKYGM RNGYLLAVAP TGSTSNIANT TAGIDPIFKK
FFIEEKQGSF TPKTAPDLNP KTFWLYKEAH TIDQQWSIRA NAARQRHIDQ AQSFNLYITP
RMKASEILNL YIEAYKQGIK TIYYVRNQSL EMDECTSCSS
//
