DODEC_HALS3
ID DODEC_HALS3 Reviewed; 68 AA.
AC B0R5M0;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Dodecin;
GN OrderedLocusNames=OE_3073R;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH RIBOFLAVIN, PARTIAL
RP PROTEIN SEQUENCE, SUBUNIT, SUBCELLULAR LOCATION, AND FUNCTION.
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=12679016; DOI=10.1016/s0969-2126(03)00048-0;
RA Bieger B., Essen L.O., Oesterhelt D.;
RT "Crystal structure of halophilic dodecin: a novel, dodecameric flavin
RT binding protein from Halobacterium salinarum.";
RL Structure 11:375-385(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.27 ANGSTROMS) IN COMPLEXES WITH LUMICHROME;
RP LUMIFLAVIN AND RIBOFLAVIN, FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-45 AND
RP GLN-55.
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=16460756; DOI=10.1016/j.jmb.2005.12.072;
RA Grininger M., Zeth K., Oesterhelt D.;
RT "Dodecins: a family of lumichrome binding proteins.";
RL J. Mol. Biol. 357:842-857(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH FAD, FUNCTION, AND
RP SUBUNIT.
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=17027852; DOI=10.1016/j.jmb.2006.08.083;
RA Grininger M., Seiler F., Zeth K., Oesterhelt D.;
RT "Dodecin sequesters FAD in closed conformation from the aqueous solution.";
RL J. Mol. Biol. 364:561-566(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH RIBOFLAVIN ANALOG,
RP FUNCTION, AND MUTAGENESIS OF TRP-36 AND GLN-55.
RX PubMed=20408700; DOI=10.1116/1.2965134;
RA Grininger M., Noll G., Trawoger S., Sinner E.K., Oesterhelt D.;
RT "Electrochemical switching of the flavoprotein dodecin at gold surfaces
RT modified by flavin-DNA hybrid linkers.";
RL Biointerphases 3:51-58(2008).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH RIBOFLAVIN,
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC 29341 / DSM 671 / R1;
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 storage protein that sequesters riboflavin
CC and related compounds, thereby protecting the cell against undesirable
CC reactions mediated by the free flavins. Binds and sequesters
CC riboflavin, lumiflavin and lumichrome. Can also bind FAD and FMN (in
CC vitro), but has low affinity for FAD and even lower affinity for FMN.
CC Protects bound flavins against light damage; Trp-36 rapidly quenches
CC the flavin excited state. Promotes the conversion of bound riboflavin
CC to lumichrome. {ECO:0000269|PubMed:12679016,
CC ECO:0000269|PubMed:16460756, ECO:0000269|PubMed:17027852,
CC ECO:0000269|PubMed:19224924, ECO:0000269|PubMed:20408700}.
CC -!- SUBUNIT: Homododecamer; four homotrimers assemble to form a dodecameric
CC hollow sphere. Except for FAD, flavin dimers are bound between subunits
CC with a stoichiometry of 6 flavin dimers per dodecamer. In contrast, FAD
CC molecules are bound as monomers, where each FAD molecule forms
CC intramolecular stacking interactions between the adenine group and the
CC isoalloxazine group. {ECO:0000269|PubMed:12679016,
CC ECO:0000269|PubMed:16460756, ECO:0000269|PubMed:17027852,
CC ECO:0000269|PubMed:19224924, ECO:0000269|PubMed:20408700}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12679016,
CC ECO:0000269|PubMed:19224924}.
CC -!- INDUCTION: Up-regulated upon transition to the exponential growth phase
CC (at protein level). Not up-regulated at the RNA level.
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; AM774415; CAP14037.1; -; Genomic_DNA.
DR RefSeq; WP_012289329.1; NC_010364.1.
DR PDB; 1MOG; X-ray; 1.70 A; A=1-68.
DR PDB; 2CC6; X-ray; 1.27 A; A=1-68.
DR PDB; 2CC7; X-ray; 1.80 A; A=1-68.
DR PDB; 2CC8; X-ray; 1.90 A; A=1-68.
DR PDB; 2CC9; X-ray; 1.55 A; A=1-68.
DR PDB; 2CCB; X-ray; 1.65 A; A=1-68.
DR PDB; 2CCC; X-ray; 1.70 A; A=1-68.
DR PDB; 2CIE; X-ray; 1.80 A; A=1-68.
DR PDB; 2CIF; X-ray; 2.80 A; A=1-68.
DR PDB; 2CJC; X-ray; 1.85 A; A=1-68.
DR PDB; 2VKF; X-ray; 1.70 A; A=1-68.
DR PDB; 2VKG; X-ray; 1.80 A; A=1-68.
DR PDB; 2VX9; X-ray; 1.65 A; A=1-65.
DR PDB; 4B2H; X-ray; 1.60 A; A=1-68.
DR PDB; 4B2J; X-ray; 1.90 A; A=1-68.
DR PDB; 4B2K; X-ray; 1.70 A; A=1-68.
DR PDB; 4B2M; X-ray; 2.00 A; A=1-68.
DR PDBsum; 1MOG; -.
DR PDBsum; 2CC6; -.
DR PDBsum; 2CC7; -.
DR PDBsum; 2CC8; -.
DR PDBsum; 2CC9; -.
DR PDBsum; 2CCB; -.
DR PDBsum; 2CCC; -.
DR PDBsum; 2CIE; -.
DR PDBsum; 2CIF; -.
DR PDBsum; 2CJC; -.
DR PDBsum; 2VKF; -.
DR PDBsum; 2VKG; -.
DR PDBsum; 2VX9; -.
DR PDBsum; 4B2H; -.
DR PDBsum; 4B2J; -.
DR PDBsum; 4B2K; -.
DR PDBsum; 4B2M; -.
DR AlphaFoldDB; B0R5M0; -.
DR SMR; B0R5M0; -.
DR EnsemblBacteria; CAP14037; CAP14037; OE_3073R.
DR GeneID; 5953871; -.
DR GeneID; 62886897; -.
DR KEGG; hsl:OE_3073R; -.
DR HOGENOM; CLU_161196_1_1_2; -.
DR OMA; GREYQAE; -.
DR EvolutionaryTrace; B0R5M0; -.
DR PRO; PR:B0R5M0; -.
DR Proteomes; UP000001321; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein.
FT CHAIN 1..68
FT /note="Dodecin"
FT /id="PRO_0000429120"
FT BINDING 35
FT /ligand="riboflavin"
FT /ligand_id="ChEBI:CHEBI:57986"
FT /evidence="ECO:0000269|PubMed:12679016,
FT ECO:0000269|PubMed:19224924"
FT BINDING 36
FT /ligand="riboflavin"
FT /ligand_id="ChEBI:CHEBI:57986"
FT /evidence="ECO:0000269|PubMed:12679016,
FT ECO:0000269|PubMed:19224924"
FT BINDING 55
FT /ligand="riboflavin"
FT /ligand_id="ChEBI:CHEBI:57986"
FT /evidence="ECO:0000269|PubMed:12679016,
FT ECO:0000269|PubMed:19224924"
FT SITE 45
FT /note="May contribute to ligand binding selectivity"
FT MUTAGEN 36
FT /note="W->A: Abolishes flavin binding; when associated with
FT A-55."
FT /evidence="ECO:0000269|PubMed:20408700"
FT MUTAGEN 45
FT /note="E->A: No effect on lumichrome binding. Increases
FT lumiflavin binding. Decreases riboflavin binding."
FT /evidence="ECO:0000269|PubMed:16460756"
FT MUTAGEN 45
FT /note="E->Q,N: Strongly decreases riboflavin binding."
FT /evidence="ECO:0000269|PubMed:16460756"
FT MUTAGEN 55
FT /note="Q->A: Strongly decreases affinity for riboflavin,
FT lumichrome and lumiflavin. Abolishes flavin binding; when
FT associated with A-36."
FT /evidence="ECO:0000269|PubMed:16460756,
FT ECO:0000269|PubMed:20408700"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:2CC6"
FT HELIX 16..30
FT /evidence="ECO:0007829|PDB:2CC6"
FT STRAND 34..45
FT /evidence="ECO:0007829|PDB:2CC6"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2CC6"
FT STRAND 53..63
FT /evidence="ECO:0007829|PDB:2CC6"
SQ SEQUENCE 68 AA; 7438 MW; BDA46E2D3173EA6D CRC64;
MVFKKVLLTG TSEESFTAAA DDAIDRAEDT LDNVVWAEVV DQGVEIGAVE ERTYQTEVQV
AFELDGSQ
