ID A1B2M8_PARDP Unreviewed; 609 AA.
AC A1B2M8;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:ABL69772.1};
DE EC=3.7.1.- {ECO:0000313|EMBL:ABL69772.1};
GN OrderedLocusNames=Pden_1675 {ECO:0000313|EMBL:ABL69772.1};
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL69772.1, ECO:0000313|Proteomes:UP000000361};
RN [1] {ECO:0000313|Proteomes:UP000000361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000489; ABL69772.1; -; Genomic_DNA.
DR RefSeq; WP_011747970.1; NC_008686.1.
DR AlphaFoldDB; A1B2M8; -.
DR STRING; 318586.Pden_1675; -.
DR EnsemblBacteria; ABL69772; ABL69772; Pden_1675.
DR GeneID; 75501158; -.
DR KEGG; pde:Pden_1675; -.
DR eggNOG; COG3962; Bacteria.
DR HOGENOM; CLU_013748_6_0_5; -.
DR OrthoDB; 3194735at2; -.
DR Proteomes; UP000000361; Chromosome 1.
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:ABL69772.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 32..130
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 218..350
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 412..563
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 609 AA; 65044 MW; DC5B4A58CDE08C67 CRC64;
MSGTIRLTAA QAMMRWLSVQ MTEEGERFIE AVWAIFGHGN VAGIGEALHG IGDALPTLRG
QNEQTMAHAA IAWTKTRKRR RAMAVTSSIG PGATNMVTAA ALAHVNRLPL LLIPGDVFAN
RRPDPVLQQI EDFGDGTVSA NDCFRPVSRY FDRISRPEHL LTALPRAMQV MTDPANCGPV
TLAFCQDVQA EAYDWPEAFF APKVWRIRRP EPDAAELAEV VALIRKAERP VIVSGGGVIY
SGAEATLLDF ARHHRIPVVE TQAGKGAIDW REELNLGSPG VTGTDAGNAA CARADLIIGV
GTRFQDFTTG SWTAFANPAR RLVSINLTGY DAAKHGAVPL VADARVALER IGAALGAHRF
AEPDAAPRAD WFALADKAMA APNHDGLPSD AQVIGAVQRV AGENTVVMCA AGTMPGALQV
LWRASPGGYH MEYGYSCMGY EVAGALGIAM ARPEAEVICM VGDGSYMMAN SELATAVMLK
VPFTVVLTDN RGYGCINRLQ QECGGEEFNN MYASSNVVEE PQIDFVAHAA SMGAHAEKVS
DIAALEAAIR AARGRDIPSV VVIDTEALTG AGIGGGWWDV AVPQTGQGDK LGAARERYET
WMQKQQLVN
//
