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
//