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Database: UniProt
Entry: H6CDL7_9BACL
LinkDB: H6CDL7_9BACL
Original site: H6CDL7_9BACL 
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
//
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