ID C7BPL9_PHOAA Unreviewed; 649 AA.
AC C7BPL9;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE SubName: Full=Similar to myo-inositol catabolism iold of bacillus subtilis {ECO:0000313|EMBL:CAQ84801.1};
GN OrderedLocusNames=PAU_02710 {ECO:0000313|EMBL:CAQ84801.1};
OS Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77)
OS (Xenorhabdus luminescens (strain 2)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=553480 {ECO:0000313|EMBL:CAQ84801.1, ECO:0000313|Proteomes:UP000002747};
RN [1] {ECO:0000313|EMBL:CAQ84801.1, ECO:0000313|Proteomes:UP000002747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43949 / 3105-77 {ECO:0000313|Proteomes:UP000002747};
RX PubMed=19583835; DOI=10.1186/1471-2164-10-302;
RA Wilkinson P., Waterfield N.R., Crossman L., Corton C.,
RA Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L.,
RA Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Churcher C.,
RA Harris D., Thompson N.R., Quail M., Parkhill J., ffrench-Constant R.H.;
RT "Comparative genomics of the emerging human pathogen Photorhabdus
RT asymbiotica with the insect pathogen Photorhabdus luminescens.";
RL BMC Genomics 10:302-302(2009).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; FM162591; CAQ84801.1; -; Genomic_DNA.
DR AlphaFoldDB; C7BPL9; -.
DR STRING; 291112.PAU_02710; -.
DR KEGG; pay:PAU_02710; -.
DR eggNOG; COG3962; Bacteria.
DR OMA; PNTYHLE; -.
DR Proteomes; UP000002747; Chromosome.
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 11..138
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 224..357
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 445..603
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 649 AA; 72145 MW; BDBE52A2160A5787 CRC64;
MGFCDMNKST MTTAQALVKF LNQQYVEIDD EQYPFIKGIF TIFGHGNVVG LGQALEQDSG
HLTVYQGCNE QGMAHIATGF AKQKKRKQIF AVTSSVGPGS ANMVTAAATA TANRIPLLLL
PGDLFACRQP DPVLQQVEQF HDYTISTNDC FRPVSRYWDR ISRPEQLMSA MINAMRVLTD
PADAGAVTIC LPQDVQGEIW DFPDYFFQKR FHRIERRPAS VAMINDAVAL INRKQKPLLI
CGGGVRYSEA HEAFRQFAEN FNIPFAETQA GKSAVIADHP LNCGGLGTTG CLAANLIAKE
ADLIIGIGTR FTDFTTASKS LFQHPDVEFL TINVAEFDAC KLDAVPVVAD AREGLNAIAE
KLTQLSYRSG YQNEISQVRE AWRKELNRLF EIQYQQGFIP EISGHLDNKL EEYSQALQTQ
LTQTRVLGLL DKYLEPEAII VGASGSLPGD LQRLWQPKQP DTYHLEYGYS CMGYEIAAAI
GAKLACPNQP VYAIAGDGAY MMLHSELQTA VQENIKITVL LFDNAGFGCI NNLQMSQGMG
SFGTENRYRN PESNNMDGSL IKVDFAKNAE SYGCKSYRVH DEQQLLYALQ EARKQTLPVL
IDIKVLPKTM THDYESWWRT GTAQIAKNPA VESASDKIKE IIATKIRQY
//