ID   DODEC_HALHL             Reviewed;          70 AA.
AC   A1WUH0;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Dodecin;
GN   OrderedLocusNames=Hhal_0546;
OS   Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS   halophila (strain DSM 244 / SL1)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Halorhodospira.
OX   NCBI_TaxID=349124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 244 / SL1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W.,
RA   Richardson P.;
RT   "Complete sequence of Halorhodospira halophila SL1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH RIBOFLAVIN,
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=19224924; DOI=10.1074/jbc.m808063200;
RA   Grininger M., Staudt H., Johansson P., Wachtveitl J., Oesterhelt D.;
RT   "Dodecin is the key player in flavin homeostasis of archaea.";
RL   J. Biol. Chem. 284:13068-13076(2009).
CC   -!- FUNCTION: May function as a riboflavin storage protein that binds and
CC       sequesters riboflavin, thereby protecting cells against undesirable
CC       reactions mediated by free riboflavin. Protects bound flavin against
CC       light damage; flavin fluorescence is rapidly quenched by interaction
CC       with Trp-39. {ECO:0000269|PubMed:19224924}.
CC   -!- SUBUNIT: Homododecamer; 12 subunits assemble to form a hollow sphere.
CC       {ECO:0000269|PubMed:19224924}.
CC   -!- SIMILARITY: Belongs to the dodecin family. {ECO:0000305}.
CC   -!- CAUTION: Dodecin family members from different organisms have non-
CC       identical ligand binding specificity. {ECO:0000305}.
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DR   EMBL; CP000544; ABM61332.1; -; Genomic_DNA.
DR   RefSeq; WP_011813355.1; NC_008789.1.
DR   PDB; 2VXA; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L=1-70.
DR   PDBsum; 2VXA; -.
DR   AlphaFoldDB; A1WUH0; -.
DR   SMR; A1WUH0; -.
DR   STRING; 349124.Hhal_0546; -.
DR   EnsemblBacteria; ABM61332; ABM61332; Hhal_0546.
DR   KEGG; hha:Hhal_0546; -.
DR   eggNOG; COG3360; Bacteria.
DR   HOGENOM; CLU_161196_1_1_6; -.
DR   OMA; HYQVGLK; -.
DR   OrthoDB; 2025589at2; -.
DR   EvolutionaryTrace; A1WUH0; -.
DR   Proteomes; UP000000647; Chromosome.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1660.10; -; 1.
DR   InterPro; IPR009923; Dodecin.
DR   InterPro; IPR025543; Dodecin-like.
DR   InterPro; IPR036694; Dodecin-like_sf.
DR   PANTHER; PTHR39324; PTHR39324; 1.
DR   Pfam; PF07311; Dodecin; 1.
DR   SUPFAM; SSF89807; SSF89807; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Flavoprotein; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..70
FT                   /note="Dodecin"
FT                   /id="PRO_0000429119"
FT   BINDING         39
FT                   /ligand="riboflavin"
FT                   /ligand_id="ChEBI:CHEBI:57986"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000269|PubMed:19224924"
FT   BINDING         46
FT                   /ligand="riboflavin"
FT                   /ligand_id="ChEBI:CHEBI:57986"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000269|PubMed:19224924"
FT   BINDING         58
FT                   /ligand="riboflavin"
FT                   /ligand_id="ChEBI:CHEBI:57986"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000269|PubMed:19224924"
FT   STRAND          5..17
FT                   /evidence="ECO:0007829|PDB:2VXA"
FT   HELIX           19..33
FT                   /evidence="ECO:0007829|PDB:2VXA"
FT   STRAND          37..50
FT                   /evidence="ECO:0007829|PDB:2VXA"
FT   STRAND          53..67
FT                   /evidence="ECO:0007829|PDB:2VXA"
SQ   SEQUENCE   70 AA;  7743 MW;  E8C795746C8B588D CRC64;
     MSDHVYKIVE LTGSSPNGIE EAVNNAIARA GETLRHLRWF EVVDTRGHIE GGRVNHWQVT
     VKVGFTLEGG