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Database: UniProt
Entry: K8WWR2_9GAMM
LinkDB: K8WWR2_9GAMM
Original site: K8WWR2_9GAMM 
ID   K8WWR2_9GAMM            Unreviewed;       645 AA.
AC   K8WWR2;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=OOA_01200 {ECO:0000313|EMBL:EKT65109.1};
OS   Providencia burhodogranariea DSM 19968.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Providencia.
OX   NCBI_TaxID=1141662 {ECO:0000313|EMBL:EKT65109.1, ECO:0000313|Proteomes:UP000009336};
RN   [1] {ECO:0000313|EMBL:EKT65109.1, ECO:0000313|Proteomes:UP000009336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19968 {ECO:0000313|EMBL:EKT65109.1,
RC   ECO:0000313|Proteomes:UP000009336};
RX   PubMed=23145767; DOI=10.1186/1471-2164-13-612;
RA   Galac M.R., Lazzaro B.P.;
RT   "Comparative genomics of bacteria in the genus Providencia isolated from
RT   wild Drosophila melanogaster.";
RL   BMC Genomics 13:612-612(2012).
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:EKT65109.1}.
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DR   EMBL; AKKL01000002; EKT65109.1; -; Genomic_DNA.
DR   RefSeq; WP_008910289.1; NZ_KB233222.1.
DR   AlphaFoldDB; K8WWR2; -.
DR   STRING; 1141662.OOA_01200; -.
DR   PATRIC; fig|1141662.3.peg.244; -.
DR   eggNOG; COG3962; Bacteria.
DR   HOGENOM; CLU_013748_6_0_6; -.
DR   OrthoDB; 3194735at2; -.
DR   Proteomes; UP000009336; 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   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          6..134
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          220..353
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          440..599
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   645 AA;  70637 MW;  5322CF0E9182F786 CRC64;
     MNKQTMTTAQ ALVKFLNQQY VEVDGEQYPF IQGIFTIFGH GNVVGLGQAL EEAPGHLQVY
     QGCNEQGMAH IATGFAKQKK RKQICAVTSS VGPGAANMVT AAATATANRI PLLLLPGDTF
     ATRQPDPVLQ QVEQYGDGTL STNDCFRPVS RYWDRVSRPE QLMAAMINAM RVLTDPADTG
     AVTICLPQDV QGEAWDYPDY FFAKRVHRIE RRPATTVSLA EAVSLIRRKQ KPLLVCGGGV
     RYSEAHDAFR IFAEHFAIPF GETQAGKSAI VASHPLNVGG IGTTGGLAAN LLAKEADLVI
     GVGTRFTDFT TASKSLFSHP NVEFLNINVA EFDACKLDAL KLVADAKEGL TALDTLLQGS
     GYQAQWGDSI QQAKQQWQTE LTRLFSIQYR PLDFIPEIAG HLDDKIDEYR EALGTELTQT
     RVLGLMQQYM EDDAIVVGAA GSLPGDLQRI WFPKYPDTYH LEYGYSCMGY EIAAAVGAKI
     AAPEQPVYAM VGDGSYLMLH SELQTAIQEN LKITILLFDN AGFGCINNLQ MSQGMGSFGT
     ENRHRNPKTG KMDGPLVKVD FAKNAESYGC KSYRVHDEAQ LIAAIEDAKS HSGCVLIDIK
     VLPKTMTNGY EAWWRTGTAQ VAQNPEIVCA ADKIKEMVAN HVRQY
//
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