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Entry: A0A2T5PE53_9PSED
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ID   A0A2T5PE53_9PSED        Unreviewed;       411 AA.
AC   A0A2T5PE53;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Ribonucleoside-diphosphate reductase subunit beta {ECO:0000256|PIRNR:PIRNR000355};
DE            EC=1.17.4.1 {ECO:0000256|PIRNR:PIRNR000355};
GN   ORFNames=DBO85_02745 {ECO:0000313|EMBL:PTU76016.1};
OS   Pseudomonas mangrovi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=2161748 {ECO:0000313|EMBL:PTU76016.1, ECO:0000313|Proteomes:UP000244064};
RN   [1] {ECO:0000313|EMBL:PTU76016.1, ECO:0000313|Proteomes:UP000244064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC-11 {ECO:0000313|EMBL:PTU76016.1,
RC   ECO:0000313|Proteomes:UP000244064};
RA   Chen C.;
RT   "Pseudomonas sp. nov., isolated from mangrove soil.";
RL   Submitted (APR-2018) 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|PIRNR:PIRNR000355}.
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|PIRNR:PIRNR000355};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000355,
CC         ECO:0000256|PIRSR:PIRSR000355-2};
CC       Note=Binds 2 iron ions per subunit. {ECO:0000256|PIRNR:PIRNR000355,
CC       ECO:0000256|PIRSR:PIRSR000355-2};
CC   -!- PATHWAY: Genetic information processing; DNA replication.
CC       {ECO:0000256|ARBA:ARBA00005160, ECO:0000256|PIRNR:PIRNR000355}.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000256|ARBA:ARBA00009303,
CC       ECO:0000256|PIRNR:PIRNR000355}.
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:PTU76016.1}.
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DR   EMBL; QASN01000003; PTU76016.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T5PE53; -.
DR   OrthoDB; 9766544at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000244064; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; cd01049; RNRR2; 1.
DR   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR033909; RNR_small.
DR   InterPro; IPR000358; RNR_small_fam.
DR   PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1.
DR   PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1.
DR   Pfam; PF00268; Ribonuc_red_sm; 1.
DR   PIRSF; PIRSF000355; NrdB; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
PE   3: Inferred from homology;
KW   Deoxyribonucleotide synthesis {ECO:0000256|PIRNR:PIRNR000355};
KW   Iron {ECO:0000256|PIRNR:PIRNR000355, ECO:0000256|PIRSR:PIRSR000355-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000355,
KW   ECO:0000256|PIRSR:PIRSR000355-2};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000355};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244064};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        249..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        190
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-1"
FT   BINDING         152
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         183
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         183
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         186
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         256
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         290
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         293
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
SQ   SEQUENCE   411 AA;  46641 MW;  88568277C0CC0F89 CRC64;
     MLSWDEFDKP EETTAAAPGR MAAAQLASED DAPSSVQDAR AVSADDSDAV ARAKAALDAL
     DIQEGLDDLE GASARVQVGD KQMINARADL NQLVPFKYDW AWQKYLDGCA NHWMPQEVNM
     TADIALWKSK DGLTEDERRI VKRNLGFFST ADSLVANNLV LAVYRLITNP ECRQYILRQA
     FEEAIHTHAY QYCIESLGMD EGEIFNMYHE IPSVAKKASW GLKYTRSISD PTFTTGTVDT
     DKQFLRNLIA YYCVLEGVFF YCGFTQILSM GRRNKMTGTA EQFQYILRDE SMHLNFGIDM
     INQIKIENPH LWDAAMKDEA TQMILQGTQL EIEYARDTMP RGVLGMNAAM MEDYLKFIAN
     RRLTQIGLPE QYAGASNPFP WMSEIMDLKK EKNFFETRVI EYQTGGALSW D
//
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