UniProt: A0A0K9XF46

Database: UniProt
Entry: A0A0K9XF46_9ACTN

LinkDB:  A0A0K9XF46_9ACTN 
Original site:  A0A0K9XF46_9ACTN

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (1)   
All databases (15)   

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ID   A0A0K9XF46_9ACTN        Unreviewed;       793 AA.
AC   A0A0K9XF46;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=AC230_16295 {ECO:0000313|EMBL:KNB51863.1};
OS   Streptomyces caatingaensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1678637 {ECO:0000313|EMBL:KNB51863.1, ECO:0000313|Proteomes:UP000037288};
RN   [1] {ECO:0000313|Proteomes:UP000037288}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMAA 1322 {ECO:0000313|Proteomes:UP000037288};
RA   Santos S.N., Gacesa R., Taketani R.G., Long P.F., Melo I.S.;
RT   "Draft genome sequence of Streptomyces sp. CMAA 1322, a bacterium isolated
RT   from Caatinga biome, from dry forest semiarid of Brazil.";
RL   Submitted (JUL-2015) 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:KNB51863.1}.
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DR   EMBL; LFXA01000009; KNB51863.1; -; Genomic_DNA.
DR   RefSeq; WP_049716874.1; NZ_LFXA01000009.1.
DR   AlphaFoldDB; A0A0K9XF46; -.
DR   STRING; 1678637.AC230_16295; -.
DR   PATRIC; fig|1678637.3.peg.3511; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000037288; Unassembled WGS sequence.
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:UP000037288}.
FT   DOMAIN          592..614
FT                   /note="Ribonucleotide reductase large subunit"
FT                   /evidence="ECO:0000259|PROSITE:PS00089"
SQ   SEQUENCE   793 AA;  86929 MW;  3A78B36A0ACBB9B1 CRC64;
     MTIAPVDPVS EQAAVSADGP GTALLRTLTE LTADLPATDP GKVAAAALRG RHAGSDEAEL
     RSLATEAAAG LIGEEPEYSR LAARLLTLAI AEEAAGQGAV SFSASVATGH REGLIADETA
     AFVRTHAERL DALVDAALAD GADDRFGYFG LRTLHSRYLL RHPITRNVIE TPQHFLLRVA
     CGLAEDHSVR ALEDVAELYR LTSTLSYLPS SPTLFNSGTR HPQMSSCYLL DSPLDELDSI
     YNRYHQVARL SKHAGGIGLS YSRIRSRGSL IRGTNGHSNG IVPFLRTLDA SVAAVNQGGR
     RKGAACVYLE TWHADIEEFL ELRDNTGEEA RRTHNLNIAH WIPDEFMRRV EADADWSLFS
     PADTPDLVDL YGDEFDAAYR RYEAEGKAVK TIPARVLYAR MMRTLAQTGN GWMTFKDAAN
     RTANQTAEPG QVVHSSNLCT EILEVTNDGE TAVCNLGSVN LAAHLGEDGE MDWERLDRTV
     RTAVTFLDRV VDINFYPTEQ AGASNSRWRP VGLGLMGLQD VFFRLRLPFD SPEAKALSTR
     ISERIMLAAY EASADLAERH GPHPAWSATR TARGVLHPDH YPNTEPTWAE RWDALRARIA
     AVGMRNSLLL AIAPTATIAS IAGVYECIEP QVSNLFKRET LSGEFLQVNT YLVEDLKKLG
     VWDRTTRDAL TDANGSVQDM RWIPQDVRDL YRTAWEIPQR ALIDMAAART PYLDQSQSLN
     LFMAAPTIGK LSSMYAYAWK QGIKTTYYLR SRPATRIARS AGAAATVPVQ QSAPDADAIA
     CSLENPESCE ACQ
//

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