ID H6CDL7_9BACL Unreviewed; 777 AA.
AC H6CDL7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=WG8_0531 {ECO:0000313|EMBL:EHS59578.1};
OS Paenibacillus sp. Aloe-11.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1050222 {ECO:0000313|EMBL:EHS59578.1, ECO:0000313|Proteomes:UP000005078};
RN [1] {ECO:0000313|Proteomes:UP000005078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aloe-11 {ECO:0000313|Proteomes:UP000005078};
RX PubMed=22461553; DOI=10.1128/jb.00087-12;
RA Li N.Z., Xia T., Xu Y.L., Qiu R.R., Xiang H., He D., Peng Y.Y.;
RT "Genome Sequence of Paenibacillus sp. Strain Aloe-11, an Endophytic
RT Bacterium with Broad Antimicrobial Activity and Intestinal Colonization
RT Ability.";
RL J. Bacteriol. 194:2117-2118(2012).
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 -!- PATHWAY: Genetic information processing; DNA replication.
CC {ECO:0000256|ARBA:ARBA00005160, 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; JH601043; EHS59578.1; -; Genomic_DNA.
DR RefSeq; WP_007428521.1; NZ_JH601043.1.
DR AlphaFoldDB; H6CDL7; -.
DR HOGENOM; CLU_000404_3_0_9; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000005078; 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:UniProtKB-UniPathway.
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; 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.
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 3..94
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 777 AA; 88065 MW; 19DFFF8F2DA0044A CRC64;
MPQLVTKPNN RQLAFDEIRI SVYADRVLSG LEKLDKDRLI RGVTSKLRRD EVTGDEISNA
FVMAALELVS KEEPDWKFAA ARALLTSLYK KAATHRRYKS YADEPYGAFY PLITELVEKG
IYRQELLDYY TKEQIDELGA SILPKNDLLF DYIGLLTLSE RYLANDFDGR VMELPQERYM
IIAMYLMHQE PADKRMELVK EAYWAMSNMY MTAATPTMSN AGKKVAGQLS SCFIDTVDDS
LEGIFDSNTD VARLSKMGGG IGVYLGKVRA RGSDIRGHKN TSSGVIPWIR QLNNTAVSVD
QLGTRKGAIA VYLDVFHKDI LAFLDLKLNN GDERMRAHDV FHGVCLPDLF MEQVEARGEW
NLFCPHEVKK VMGWTDEKGR PLGLEDFYDE SFGAGSFREK YEEASQHPIL SRITVPAIDI
MKRLMKSQLE TGTPYMFYRD TVNRANPNRA HGMVYSSNLC TEIMQNQSPT VVEKEELVTK
DGQTRIVISK IPGDFVVCNL NSIHLARAVP AGVLDRLVPI QVRMLDNVID INNIEVLQAQ
YTNSQYRAVG LGTFGLHHLL ALEGIRWESD EAVTYNDHLY EKINYLAVKS SMELAKEKGR
YAKFEGSDWS TGHYFTSRGY TDGTREGKFV TSSEWSELAE EVKQNGIRNA WLFAIAPNGS
TSIIAGSTAS IDPLYELLSY EEKTTYKIAN PAPDLNEKTI WYYKTAFLLD QHASINMASA
RQRHIDQGQS FNLYVRPDIK ATEFLELHIH AWKSGMKSTY YVRSRALTIE ECESCAS
//