ID A0A162QGU4_9BACT Unreviewed; 620 AA.
AC A0A162QGU4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (Decyclizing) {ECO:0000313|EMBL:KYP15475.1};
GN ORFNames=A1D16_08245 {ECO:0000313|EMBL:KYP15475.1};
OS Flavihumibacter sp. CACIAM 22H1.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavihumibacter.
OX NCBI_TaxID=1812911 {ECO:0000313|EMBL:KYP15475.1, ECO:0000313|Proteomes:UP000075747};
RN [1] {ECO:0000313|EMBL:KYP15475.1, ECO:0000313|Proteomes:UP000075747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CACIAM 22H1 {ECO:0000313|EMBL:KYP15475.1};
RA Moraes P.G., Lima A.R.;
RT "Draft Genome of Flavihumibacter sp. CACIAM 22H1.";
RL Submitted (MAR-2016) 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:KYP15475.1}.
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DR EMBL; LUKG01000015; KYP15475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162QGU4; -.
DR STRING; 1812911.A1D16_08245; -.
DR Proteomes; UP000075747; 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: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:KYP15475.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 10..131
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 220..354
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 417..574
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 620 AA; 67540 MW; FB5CA9F66B13ABF6 CRC64;
MARKTKRLTT AQATILFLQN QFVERDGKET AFFGGCFGIF GHGNVAGIGQ ALLQYPSFPY
FQSRNEQAMV HTAVAYAKMK NRLGALVCTT SIGPGATNMV TGAATATINR IPVLLLPGDI
FAKRDVAPVL QQLEASYSQD ISVNDCFKPV SKYWDRINRP EQLLTSLPEA MRVLTSPAET
GAVTLCMPQD VQAEAFDFPV EFFAKRVWPV QRNRPDQRAL AKAVDAIRAA RKPVIIAGGG
VLYSEASKEL TELINRTGIP VMETFAGKGS VHYKEPLNLG ACGVTGTPGA ITAAAEADLV
IGIGTRYSDF TTISESAFQH PEVRFININV AEFDAFKHAA IPLVGDAKII LQELLPLLKR
YKVSDAYRTK QERAARQWDK VVSAVYNLEH PVPISQGEVI GAVNTLSADK DIVVCAAGSL
PGDLHKLWRT RNPKGFHLEY GYSCMGYEIA GGLGIKMADP SREVYVMVGD GSYLMMSQEI
ITAVQEDVKL IIVLLNNNGY ASIGGLSESL GTKGFGTRYE YRNKKTGQLN GGILPVDLAA
NAASMGATVL KAETAAELKA ALVQAKKNKN TTVVYIETDR EQRVGGYAWW EVPVAEVSTH
AQVKTAYEKL KKNKARQRTY
//