DODEC_THET8
ID DODEC_THET8 Reviewed; 69 AA.
AC Q5SIE3;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Dodecin;
GN OrderedLocusNames=TTHA1431;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH FAD.
RA Kumei M., Inagaki E., Nakano N., Shinkai A., Yokoyama S.;
RT "Crystal structure of TT0972 protein from Thermus thermophilus.";
RL Submitted (FEB-2006) to the PDB data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-45 AND
RP ALA-65 IN COMPLEXES WITH COENZYME A AND FMN, FUNCTION, SUBUNIT, AND
RP MUTAGENESIS OF ARG-45 AND ARG-65.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=17855371; DOI=10.1074/jbc.m704951200;
RA Meissner B., Schleicher E., Weber S., Essen L.O.;
RT "The dodecin from Thermus thermophilus, a bifunctional cofactor storage
RT protein.";
RL J. Biol. Chem. 282:33142-33154(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH COENZYME A AND FMN.
RA Gurzadyan G.G., Meissner B., Sander B., Essen L.-O., Michel-Beyerle M.E.;
RT "Ultrafast charge transfer dynamics in flavoprotein dodecin.";
RL Submitted (JUL-2008) to the PDB data bank.
CC -!- FUNCTION: May function as storage protein that sequesters various
CC flavins and other cofactors, thereby protecting the cell against
CC undesirable reactions mediated by the free cofactors. Binds and
CC sequesters FMN, FAD, lumiflavin and lumichrome, and can also bind
CC coenzyme A. {ECO:0000269|PubMed:17855371}.
CC -!- SUBUNIT: Homododecamer; four homotrimers assemble to form a dodecameric
CC hollow sphere with an outer diameter of about 60 Angstroms. Flavin
CC dimers are bound between subunits with a stoichiometry of 6 flavin
CC dimers per dodecamer. Besides, trimeric coenzyme A molecules can be
CC bound between subunits. A dodecamer can bind simultaneously 12 flavin
CC and 12 coenzyme A molecules. {ECO:0000269|PubMed:17855371,
CC ECO:0000269|Ref.2, ECO:0000269|Ref.4}.
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; AP008226; BAD71254.1; -; Genomic_DNA.
DR RefSeq; WP_011173482.1; NC_006461.1.
DR RefSeq; YP_144697.1; NC_006461.1.
DR PDB; 2CZ8; X-ray; 1.50 A; A/B/C/D/E/F/G/H=1-69.
DR PDB; 2DEG; X-ray; 1.70 A; A/B/C/D/E/F=1-69.
DR PDB; 2UX9; X-ray; 1.40 A; A/B/C/D/E/F=1-69.
DR PDB; 2V18; X-ray; 2.59 A; A/B/C/D/E/F/G/H/I/J/K/L=2-69.
DR PDB; 2V19; X-ray; 2.59 A; A/B/C/D/E/F/G/H/I/J/K/L=2-69.
DR PDB; 2V21; X-ray; 2.40 A; A/B/C/D/E/F=1-69.
DR PDB; 2VYX; X-ray; 1.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-69.
DR PDBsum; 2CZ8; -.
DR PDBsum; 2DEG; -.
DR PDBsum; 2UX9; -.
DR PDBsum; 2V18; -.
DR PDBsum; 2V19; -.
DR PDBsum; 2V21; -.
DR PDBsum; 2VYX; -.
DR AlphaFoldDB; Q5SIE3; -.
DR SMR; Q5SIE3; -.
DR STRING; 300852.55772813; -.
DR EnsemblBacteria; BAD71254; BAD71254; BAD71254.
DR GeneID; 3168700; -.
DR KEGG; ttj:TTHA1431; -.
DR PATRIC; fig|300852.9.peg.1405; -.
DR eggNOG; COG3360; Bacteria.
DR HOGENOM; CLU_161196_1_1_0; -.
DR OMA; HYQVGLK; -.
DR PhylomeDB; Q5SIE3; -.
DR EvolutionaryTrace; Q5SIE3; -.
DR Proteomes; UP000000532; 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; FAD; Flavoprotein; FMN; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..69
FT /note="Dodecin"
FT /id="PRO_0000429122"
FT BINDING 3..5
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 6
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 28
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 32..34
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT BINDING 37
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 38
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 45
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 57
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 65..67
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT BINDING 65
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.4"
FT SITE 65
FT /note="May be important for ligand binding specificity and
FT FMN binding"
FT MUTAGEN 45
FT /note="R->A: No effect on the orientation of the bound
FT flavin."
FT /evidence="ECO:0000269|PubMed:17855371"
FT MUTAGEN 65
FT /note="R->A: No effect on the orientation of the bound
FT flavin."
FT /evidence="ECO:0000269|PubMed:17855371"
FT STRAND 5..16
FT /evidence="ECO:0007829|PDB:2UX9"
FT HELIX 18..32
FT /evidence="ECO:0007829|PDB:2UX9"
FT STRAND 36..49
FT /evidence="ECO:0007829|PDB:2UX9"
FT STRAND 52..65
FT /evidence="ECO:0007829|PDB:2UX9"
SQ SEQUENCE 69 AA; 7748 MW; CC1510FD521FA4D9 CRC64;
MGKVYKKVEL VGTSEEGLEA AIQAALARAR KTLRHLDWFE VKEIRGTIGE AGVKEYQVVL
EVGFRLEET
