ID A0A0H5LWT7_YERIN Unreviewed; 646 AA.
AC A0A0H5LWT7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative thiamine pyrophosphate-dependent protein {ECO:0000313|EMBL:CRY55609.1};
DE EC=3.7.1.- {ECO:0000313|EMBL:CRY55609.1};
GN Name=iolD {ECO:0000313|EMBL:CRY55609.1};
GN ORFNames=ERS008476_02610 {ECO:0000313|EMBL:CRY55609.1};
OS Yersinia intermedia.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=631 {ECO:0000313|EMBL:CRY55609.1, ECO:0000313|Proteomes:UP000043316};
RN [1] {ECO:0000313|Proteomes:UP000043316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R148 {ECO:0000313|Proteomes:UP000043316};
RG Pathogen Informatics;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CWJI01000007; CRY55609.1; -; Genomic_DNA.
DR RefSeq; WP_053009749.1; NZ_CWJI01000007.1.
DR AlphaFoldDB; A0A0H5LWT7; -.
DR Proteomes; UP000043316; 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 Hydrolase {ECO:0000313|EMBL:CRY55609.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..135
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 442..601
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 646 AA; 71150 MW; EB14864584759569 CRC64;
MKKIRLTTAQ ALVRFLDNQY LQVDGQEIKF IKGIFAIFGH GNVLGIGQAL EQDCGDLVVH
QGRNEQGMAH AATGFAKQKL RQQIYACTSS VGPGSANMIT AAATATANRI PLLLLPGDVF
ASRQPDPVLQ QIEQSHDLSI STNDAFKPVS KYWDRITRPE QLMSACINAM RVLTDPAETG
AVTLCLPQDV QAEAYEYPDY FFQKRVHRLD RRPASAAMLA DAIALLTSKR KPILVCGGGV
KYSQAGQVLQ RFAECFGVPW VETQAGKGTL SSEHELNLGG IGETGCLAAN TLAQQADLII
GVGTRYSDFT TSSKWLFQNP EVSFLNINVS AFDAGKLDGL QLLADAREAL SALHQKLGIT
GYQASWGSEI SRMRAEQLAE TQRVYQVEYR KDDFIPEIND HLDREQVFAE FMAQTGSLLT
QSQVLGVLNS QLPHDAVIVA AAGSLPGDLQ RVWRTKGENG YHVEYGYSCM GYEVSAALGV
KLAEPSREVY SLVGDGAFMM LHSELVTSIQ ERCKINVILF DNMTNGCINN LQMEHGMDSY
ATEFRFRNQE TGQLDGGFVP VDFAMLAAAY GCKTYRVSTE QQLVDALADA RLQTVSTLID
IKVLPKTMVH KYLSWWRVGV AQVSESERTD AVVRELEKNI AKARDY
//
