ID A0A0J1K816_9GAMM Unreviewed; 660 AA.
AC A0A0J1K816;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:KLV10482.1};
GN ORFNames=ABT57_08045 {ECO:0000313|EMBL:KLV10482.1};
OS Photobacterium ganghwense.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=320778 {ECO:0000313|EMBL:KLV10482.1, ECO:0000313|Proteomes:UP000035909};
RN [1] {ECO:0000313|EMBL:KLV10482.1, ECO:0000313|Proteomes:UP000035909}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22954 {ECO:0000313|EMBL:KLV10482.1,
RC ECO:0000313|Proteomes:UP000035909};
RA Machado H., Gram L.;
RT "Photobacterium galathea sp. nov.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLV10482.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LDOU01000006; KLV10482.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1K816; -.
DR STRING; 320778.ABT57_08045; -.
DR PATRIC; fig|320778.3.peg.1746; -.
DR Proteomes; UP000035909; 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:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR GO; GO:0019310; P:inositol catabolic process; IEA:InterPro.
DR CDD; cd02003; TPP_IolD; 1.
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:KLV10482.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000035909};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 22..150
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 235..368
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 455..614
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 660 AA; 72427 MW; 3F21411E37C64C28 CRC64;
MRMDSATACL IGETVVMSTL RMTTAQALVK FMNQQYVDVD GEQQKFIHGV FTIFGHGNVV
GLGQALEQDA GDLVVHQGCN EQGMAHIAMG YAKQQKRKKI YAVTSSVGPG AANMVTAAAT
ATANRIPVLF LPGDVFASRQ PDPVLQQVEQ YHDCSISTND CFRPVSRYWD RVSRPEQLMS
AMINAMRVLT DPADTGAVTI CLPQDVQGEA YDFPDYFFQK RVHRIERRPA SAAMIEDAVR
LIRSKKKPML VCGGGVRYSE AHEMFRLFAE RFNIPFGETQ AGKSAVVYDH VLNLGGVGTT
GCLAANLIAK EADLVIGVGT RFTDFTTASK SLFQHPDVEF LTINVAEFDA YKLDASAVVA
DAKEALIAIG DQLEQVGYRS GYVDEIRLAK SAWKTELERL FAIEYQDGFS PEIAGHLDDK
LSEYSDALQT RLTQTRVLGL LDEHLEDHAI VVGAAGSLPG DLQRVWQPKQ PDTYHMEYGY
SCMGYEVAAA VGAKLACPEQ PVYAMVGDGS YMMLHSELQT AIQEGLKITV LLFDNAGFGC
INNLQMSQGM GSYGTENRYR DPATGGMTGN LVKVDFAKNA ESYGCKGYTV HTEAELLAAL
EDARKQAVSS LIDIKVLPKT MTHGYEAWWR TGTAQVADDP RIVEAADDIK RVLSEQARQY
//
