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Database: UniProt
Entry: A0A0M6XM36_9RHOB
LinkDB: A0A0M6XM36_9RHOB
Original site: A0A0M6XM36_9RHOB 
ID   A0A0M6XM36_9RHOB        Unreviewed;       623 AA.
AC   A0A0M6XM36;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:CTQ31712.1};
DE            EC=3.7.1.- {ECO:0000313|EMBL:CTQ31712.1};
GN   Name=iolD {ECO:0000313|EMBL:CTQ31712.1};
GN   ORFNames=JAN5088_00471 {ECO:0000313|EMBL:CTQ31712.1};
OS   Jannaschia rubra.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=282197 {ECO:0000313|EMBL:CTQ31712.1, ECO:0000313|Proteomes:UP000048908};
RN   [1] {ECO:0000313|EMBL:CTQ31712.1, ECO:0000313|Proteomes:UP000048908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5088 {ECO:0000313|EMBL:CTQ31712.1,
RC   ECO:0000313|Proteomes:UP000048908};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CXPG01000011; CTQ31712.1; -; Genomic_DNA.
DR   RefSeq; WP_055681199.1; NZ_FOOS01000006.1.
DR   AlphaFoldDB; A0A0M6XM36; -.
DR   STRING; 282197.SAMN04488517_106154; -.
DR   OrthoDB; 3194735at2; -.
DR   Proteomes; UP000048908; Unassembled WGS sequence.
DR   GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:InterPro.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR030817; Myo_inos_IolD.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   NCBIfam; TIGR04377; myo_inos_iolD; 1.
DR   PANTHER; PTHR18968:SF9; 3D-(3,5_4)-TRIHYDROXYCYCLOHEXANE-1,2-DIONE HYDROLASE; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:CTQ31712.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000048908};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          11..135
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          223..355
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          426..575
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          599..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..623
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   623 AA;  67354 MW;  ABF4633E9C22D929 CRC64;
     MTSTGRTVRL TVAQAIVRWL MNQYIEIDGV ETRICGGGFG IFGHGNVPCL GEALYAVHSD
     LPLYRGQNEQ GMGFAAAAYA KYHLRRRFMF CTASAGPGTA NLLTAAALAH ANRLPMLMLC
     GDTFITRLPD PVLQQLEHFG DPTRGLNDAF RAVSRFWDRI THPAQVLQSL PAALATMLDP
     ADCGPAFLGL PQDVQGWAWD YPERFFDRRV HRIRRQAPDT AEVAEVADLL RAARRPVLIA
     GGGIQYSRAV ETLTTFVEAH DIPVIETIAG RANLVDDHPL NIGPVGVTGS DSANAIAAQA
     DLILAVGTRL QDFTTGSWTA FAPDARLVTL NVGRHDAAKH LATTMVGDAR LGLEVLGAAL
     GDHRAPSEWV DLAKAERRAW MRTVSETVRP GNRPNSYAQA IGVVNDLCDP SDRIVAAAGG
     LPAEVTANWR TLKPGTVDVE FGFSCMGYEI AGGWGARIAQ AEAEPDRDTI VFCGDGSYLL
     MNSDIYSSVL TRKKLIVLVL DNGGFAVINK LQNNTGQESF NNLIADCPTV PEPFTVDFAA
     HAAAMGANVE TVENPAGLAE AFRRAQAADK TSVIVMKVDP YEGWTTGGHA WWEIGTPEVS
     ETESVREAHE ETEAMRDRQR QGV
//
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