ID A0A0W7WE10_9RHOB Unreviewed; 609 AA.
AC A0A0W7WE10;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (Decyclizing) {ECO:0000313|EMBL:KUF08702.1};
GN ORFNames=AVJ23_21320 {ECO:0000313|EMBL:KUF08702.1};
OS Pseudoponticoccus marisrubri.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudoponticoccus.
OX NCBI_TaxID=1685382 {ECO:0000313|EMBL:KUF08702.1, ECO:0000313|Proteomes:UP000054396};
RN [1] {ECO:0000313|EMBL:KUF08702.1, ECO:0000313|Proteomes:UP000054396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJ5A-1 {ECO:0000313|EMBL:KUF08702.1,
RC ECO:0000313|Proteomes:UP000054396};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-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:KUF08702.1}.
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DR EMBL; LPXO01000026; KUF08702.1; -; Genomic_DNA.
DR RefSeq; WP_058864262.1; NZ_LPXO01000026.1.
DR AlphaFoldDB; A0A0W7WE10; -.
DR STRING; 1685382.AVJ23_21320; -.
DR OrthoDB; 3194735at2; -.
DR Proteomes; UP000054396; 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:KUF08702.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054396};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..131
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 216..350
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 410..561
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 609 AA; 64987 MW; 5BD60DDC9DF69C69 CRC64;
MGTIRLTAAQ AMVKWLAAQM TEDGERFVEG IWGIFGHGNV AGLGEALEKA RQEFPTWRGQ
NEQTMAHTAI AYAKAKKRTR AMAVTTSIGP GATNLVTAAA VAHVNRLPIL LIPGDVFANR
RPDPVLQQVE DFEDGTVSAN DCLRPVSRYF DRIARPEQLL TALPRALATM TDPASCGPVT
LAFCQDTQAE AHDYPVEFFE PRVWRIRRPH PDAREIAELA GLITQAKRPV IVAGGGVIYA
QAEAALAAFA ETHGIPVVET QAGKSALAQA HPMNYGASGV DGSAAANALS READLVIGVG
TRFQDFTTGS RALFENPARR LVSVNVAAYD AVKHGALPVM GDAKVALEAL SAALGSYRAE
AGDPEARRAW LEAVEAHCRD RKRALPSDAE VIGAVQRATG EDAIAMCAAG TMPGALKLLW
QPSQGGYHME YGFSCMGYEI AGAMGLKLAR PEREVICFVG DGSYMMANSE LATAVMRRVP
FTVVLTDNRG YGCINRLQQG CGGAPFNNLY AHSAVEVQPE IDYAAHAASM GAHAVRAGDI
AALEAEIAAA RGRDIPTVIV IETDPNEGPG FGEAGHWWDV AVPETGSTEA LSRAYAGYLD
NKQRQRLVN
//
