ID A0A0M2LZZ0_9MICO Unreviewed; 641 AA.
AC A0A0M2LZZ0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-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:KKI21224.1};
GN ORFNames=XM48_05865 {ECO:0000313|EMBL:KKI21224.1};
OS Leucobacter sp. Ag1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1642040 {ECO:0000313|EMBL:KKI21224.1, ECO:0000313|Proteomes:UP000033836};
RN [1] {ECO:0000313|EMBL:KKI21224.1, ECO:0000313|Proteomes:UP000033836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI21224.1,
RC ECO:0000313|Proteomes:UP000033836};
RA Pei D., Kukutla P., Yu W., Xu J.;
RT "Draft Genome Sequences of Leucobacter sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-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:KKI21224.1}.
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DR EMBL; LAYO01000085; KKI21224.1; -; Genomic_DNA.
DR RefSeq; WP_046454868.1; NZ_LAYO01000085.1.
DR AlphaFoldDB; A0A0M2LZZ0; -.
DR STRING; 1642040.XM48_05865; -.
DR PATRIC; fig|1642040.3.peg.407; -.
DR OrthoDB; 3194735at2; -.
DR Proteomes; UP000033836; 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; 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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KKI21224.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033836};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..142
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 229..363
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 426..594
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 641 AA; 68406 MW; 25432E0AA8926A90 CRC64;
MTARRMTVGQ ALIEFLANQW TVDRDASGAE IRERTVPGVF GIFGHGNVAG VGQALQQLNA
QDPALMPYYQ ARNEQAMVHQ AVGYARMHRR RGTFAAAASV GPGATNLLTG AALATTNRLP
ALLLPSDTFA TRVADPVLQQ LEQPHDIGLT VNDAFRPLSR FFDRVQRPEQ LFSIALGAMR
VLTDPAETGA VTISLPEDVQ AEAFDVPAEF LQPREWRIRR PRPERDALAA AVAAIRSAKR
PFIVAGGGVI YSGAEDALRE LAEATGIPVG TTQAGGGSLP WDHPQYLGGV GATGTTAANR
LAAEADLVIG IGTRYSDFTT ASRTAFQDPG VRFVNINVAA FDAVKHGSQL PVVADARETL
LELAPLLADW RLGADSAERL AREKGEWDGV VDAALAPTGA ELPGQSEIIG AVHAASDPRD
VIVQAAGSLP GDLHKLWRVR DPLGYHVEYA YSCMGYEIAG GLGAKRGLDA AGDDRDVIVM
VGDGSYLMLS TELATAVAEG IKLVVVIVQN HGYASIGHLS ETVGSERFGT KYRRYDAEAR
NFQGDEVLPV DLAMNARSYG VDVVEIPVAP GAAEALREAV VAAKASPRST VIHINSDPLV
YAPDGEGWWD VPVAEVSELE STQRARAEYE EHVRAQRPLL G
//
