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Database: UniProt
Entry: A0A108U532_9GAMM
LinkDB: A0A108U532_9GAMM
Original site: A0A108U532_9GAMM 
ID   A0A108U532_9GAMM        Unreviewed;       647 AA.
AC   A0A108U532;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Epi-inositol hydrolase {ECO:0000313|EMBL:KWS02715.1};
DE            EC=3.7.1.- {ECO:0000313|EMBL:KWS02715.1};
GN   ORFNames=AZ78_0259 {ECO:0000313|EMBL:KWS02715.1};
OS   Lysobacter capsici AZ78.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1444315 {ECO:0000313|EMBL:KWS02715.1, ECO:0000313|Proteomes:UP000023435};
RN   [1] {ECO:0000313|EMBL:KWS02715.1, ECO:0000313|Proteomes:UP000023435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AZ78 {ECO:0000313|EMBL:KWS02715.1,
RC   ECO:0000313|Proteomes:UP000023435};
RX   PubMed=24762937;
RA   Puopolo G., Sonego P., Engelen K., Pertot I.;
RT   "Draft Genome Sequence of Lysobacter capsici AZ78, a Bacterium Antagonistic
RT   to Plant-Pathogenic Oomycetes.";
RL   Genome Announc. 2:0-0(2014).
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:KWS02715.1}.
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DR   EMBL; JAJA02000001; KWS02715.1; -; Genomic_DNA.
DR   RefSeq; WP_051547032.1; NZ_JAJA02000001.1.
DR   AlphaFoldDB; A0A108U532; -.
DR   OrthoDB; 9785953at2; -.
DR   Proteomes; UP000023435; 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; 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:KWS02715.1};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          22..149
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          237..352
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          437..591
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          628..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   647 AA;  69001 MW;  DCC6B3FF991779DE CRC64;
     MNATSSPASA TASGSGGAVR LTMAQALVRY LAAQYTIDPD SGERVRLFGG VFAIFGHGNV
     AGLGEALYQH RDALPTYRAH SEQGMANAAI AYAKAHMRRR MMAVTASIGP GSTNLVTSAA
     LAHVNRLPVL LLPGDIFVSR APDPVLQQLE DFADGTVSVN DCLRPVSRYF DRIVKPEQLL
     RALPRAMRAL TDPALCGPVT LALPQDVQTE AWDWPQAFFA PRLHAFRAPA PQADEVATLA
     AALREAQRPV LIAGGGVLYG RAGDELRRFA DLHRVPVAET QAGKGALAWD HPLQLGAAGV
     CGSSAANALL AQADLVLAVG TRLQDFTTGS NALYAGARIA TINVNAYDAL KGGGPELICD
     AGLGLRALSA SLSDWHAPVP WAARARDEAQ AWRAIVDAVT GRRELPAGTL PYDGEVIGAV
     QRSGARSDRD DIVVCAAGTL PAELEKLWRT RTPGGYHMEY GYSCMGYEIA GGLGVKMARP
     EREVVVMVGD GSYLMLNAEI ASSVMLGMKL IVVVLDNRGF GCINRLQQAC GGAAFNNMWD
     DCLHAGDGAP PIDFAAHARA MGAQAEHVAD IDALEQAMRR ARAARGTYLI SIDTDHRRTT
     EHGGCWWEVA VPQVSERDAV RQARRDYEIA KQRQQPRPPA AQGDCDV
//
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