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Database: UniProt
Entry: A0A0F4QQX0_9GAMM
LinkDB: A0A0F4QQX0_9GAMM
Original site: A0A0F4QQX0_9GAMM 
ID   A0A0F4QQX0_9GAMM        Unreviewed;       376 AA.
AC   A0A0F4QQX0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE            EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
GN   ORFNames=TW77_07560 {ECO:0000313|EMBL:KJZ10091.1};
OS   Pseudoalteromonas rubra.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=43658 {ECO:0000313|EMBL:KJZ10091.1, ECO:0000313|Proteomes:UP000033452};
RN   [1] {ECO:0000313|EMBL:KJZ10091.1, ECO:0000313|Proteomes:UP000033452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2471 {ECO:0000313|EMBL:KJZ10091.1,
RC   ECO:0000313|Proteomes:UP000033452};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(2015).
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000256|ARBA:ARBA00009303}.
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:KJZ10091.1}.
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DR   EMBL; JXYA01000016; KJZ10091.1; -; Genomic_DNA.
DR   RefSeq; WP_046004363.1; NZ_RHHZ01000005.1.
DR   AlphaFoldDB; A0A0F4QQX0; -.
DR   PATRIC; fig|43658.5.peg.1592; -.
DR   OrthoDB; 9765051at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000033452; Unassembled WGS sequence.
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:InterPro.
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   SUPFAM; SSF47240; Ferritin-like; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000313|EMBL:KJZ10091.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033452}.
SQ   SEQUENCE   376 AA;  43333 MW;  52366F67690AE024 CRC64;
     MSYSTFNRTH NNQLQEPMFF GQSVNVSRYD QQKYPIFEKL IEKQLSFFWR PEEVDVSKDR
     LDFQALPEHE KHIFLSNLKY QTLLDSVQGR SPNVALLPIV SIPELETWIE TWAFSETIHS
     RSYTHIIRNV TKSPELIFDD IVENDKISER AEAVTKHYDE LIEKVSLYNL YGEGKHEING
     ETVHINLFEL KKMLYLCIMS VNILEAIRFY VSFACSFAFA ERELMEGNAK IIKLIARDEA
     LHLSGTQHIL NIMQDGKDDP EMAIVAAQCQ EQAIQMFVEA AEQEKEWAEY LFKDGSMIGL
     NKDILCQYVE YITNVRMTAV GLPAQFESNS NPIPWINAWL VSDNVQVAPQ EAEISSYLVG
     QIDSEVDASD FGDFDL
//
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