ID U5ML89_CLOSA Unreviewed; 743 AA.
AC U5ML89;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, 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 Name=nrdA {ECO:0000313|EMBL:AGX41298.1};
GN ORFNames=CLSA_c02460 {ECO:0000313|EMBL:AGX41298.1};
OS Clostridium saccharobutylicum DSM 13864.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1345695 {ECO:0000313|EMBL:AGX41298.1, ECO:0000313|Proteomes:UP000017118};
RN [1] {ECO:0000313|EMBL:AGX41298.1, ECO:0000313|Proteomes:UP000017118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13864 {ECO:0000313|EMBL:AGX41298.1};
RX PubMed=24285650;
RA Poehlein A., Hartwich K., Krabben P., Ehrenreich A., Liebl W., Durre P.,
RA Gottschalk G., Daniel R.;
RT "Complete Genome Sequence of the Solvent Producer Clostridium
RT saccharobutylicum NCP262 (DSM 13864).";
RL Genome Announc. 1:e00997-13(2013).
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; CP006721; AGX41298.1; -; Genomic_DNA.
DR RefSeq; WP_022743587.1; NZ_AYXL01000187.1.
DR AlphaFoldDB; U5ML89; -.
DR GeneID; 55472822; -.
DR KEGG; csb:CLSA_c02460; -.
DR PATRIC; fig|1345695.10.peg.1483; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_9; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000017118; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 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; 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; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000017118}.
FT DOMAIN 601..623
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 743 AA; 85921 MW; D489EB0E51790621 CRC64;
MSILNKLCKD AVLGIKDEEG IYTEEKLLAA LEHIIREGMD DNEIRKSLIQ VSLELTTELE
PNWQYVAARQ YIYELYDEIR NIRRLHENEN LYKNYYEFIK DLTERGLYGE YILNNYSKED
ILQLENEIKP ERDFLFNYSG ISLLAKRYLV QDYNRKAVEL PQQMFMGIAM HLAIPEDKVN
RVYWAKRFYD VLSSLKATMA TPTMSNARKP FYQLSSCFID TVEDSLQGIY KSLDNFAEVS
KFGGGMGIYM GKVRALGSPI RGFKGASGGI IPWVKLFNDT AIAVDQLGVR NGSVAVWLDA
WHRDIPEFLQ IRTNNGDDRK KAHDVFPGIC YPNLFWRLAE NDIDSNWYMM CPHEIKSVKG
YSLEDFYGEE WEEKYYECVS DERIEKRVMS VKDIVRLIVK SAAETGAPFA FYRDIANKMN
PNKHNGIIYS SNLCTEIMQN MSPMKIKNHE IVNDHDGCTV INKIIPGDFV VCNLSSIVLG
NVDVCSDEEI EYVVETQIRA MDNVIDLNYY SVPFAEVTNK KYRGIGLGTS GYHHMLANNR
IHWTEEKHKV FVDKVYEKIN YYSIKASMKI AKEKGAYELF EGSDWQNGDY FELRDYKDEK
WNKLKSEVRK FGMRNGYLIA VAPNGSTATI AGTSEGVDPI MSRFYLEEKK GSIIPKTAPN
LCEDNYWYYN SAYNIEQTWS VKMNGIRQRH IDQGQSFNLY ITNNYTMRQI MNLYIEACKS
GVKSIYYVRS KSLEVSDCES CSA
//
