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Database: UniProt
Entry: X6KRZ1_9RHOB
LinkDB: X6KRZ1_9RHOB
Original site: X6KRZ1_9RHOB 
ID   X6KRZ1_9RHOB            Unreviewed;       625 AA.
AC   X6KRZ1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 2.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:ETA49522.2};
GN   ORFNames=P279_24315 {ECO:0000313|EMBL:ETA49522.2};
OS   Rhodobacteraceae bacterium PD-2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1169855 {ECO:0000313|EMBL:ETA49522.2, ECO:0000313|Proteomes:UP000023196};
RN   [1] {ECO:0000313|EMBL:ETA49522.2, ECO:0000313|Proteomes:UP000023196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PD-2 {ECO:0000313|EMBL:ETA49522.2,
RC   ECO:0000313|Proteomes:UP000023196};
RX   PubMed=25700405;
RA   Zheng L., Cui Z., Xu L., Sun C., Powell R.J., Hill R.T.;
RT   "Draft Genome Sequence of Rhodobacteraceae Strain PD-2, an Algicidal
RT   Bacterium with a Quorum-Sensing System, Isolated from the Marine Microalga
RT   Prorocentrum donghaiense.";
RL   Genome Announc. Announc.3:e01549-14(2015).
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:ETA49522.2}.
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DR   EMBL; AWRV02000017; ETA49522.2; -; Genomic_DNA.
DR   AlphaFoldDB; X6KRZ1; -.
DR   HOGENOM; CLU_013748_6_0_5; -.
DR   OrthoDB; 3194735at2; -.
DR   Proteomes; UP000023196; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:ETA49522.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000023196};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          8..144
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          230..363
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          426..577
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   625 AA;  66649 MW;  031F5E5073875BDF CRC64;
     MSNTIRLTAA QAMVKWLAAQ MIEDDAPDSQ AGGQARAERF IDGIWGIFGH GNVAGLGEAL
     EKARQDFPTW RGQNEQTMAH AAIAYAKAKK RRRAMAVPSS IGPGATTLVT AAALAHVNRL
     PVLLIPGDVF ANRRPDPVLQ QVEDFEDGTV SANDCLRPVS RYFDRISRPE HLLTALPRAL
     ATMTDPATCG PVTLAFCQDT QTEAYDYPAE FFERRVWRIR RPQPDPREVA DLVALIKAAK
     APVIVAGGGV IYAQAEDTLA RFAETHGIPV VETQAGKSAL AQGHPMNFGA SGVDGSAAAN
     ALAAEADLVI GVGTRFQDFT TGSRTLFSNP GRRLVSINVA GYDAVKHGAL PVMGDAKATL
     EALSDALGSH SAGAFDPKAR TAWLDAVTHH CRDRQRAAGD LPTDAEVIGA VQRATGEDSV
     AMCAAGTMPG ALKLLWQPSQ GGYHMEYGFS CMGYEIAGAM GVKLASPERE VICFVGDGSY
     MMANSELATA VMRRVPFTVV LTDNRGYGCI NRLQQGCGGA PFNNLYADSN VEAQPQIDYV
     AHAASMGAHA VKVGSIADLE TRIAEARGRD IPTVIVIETT PHEGPGFGEA GHWWDVAVPE
     VGSTEALNKA YATYLDNKQR QRLVN
//
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