ID Q67QP4_SYMTH Unreviewed; 551 AA.
AC Q67QP4;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Acetolactate synthase-like TPP-requiring enzyme {ECO:0000313|EMBL:BAD39999.1};
GN OrderedLocusNames=STH1014 {ECO:0000313|EMBL:BAD39999.1};
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459 {ECO:0000313|EMBL:BAD39999.1, ECO:0000313|Proteomes:UP000000417};
RN [1] {ECO:0000313|EMBL:BAD39999.1, ECO:0000313|Proteomes:UP000000417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863 {ECO:0000313|Proteomes:UP000000417};
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(2004).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; AP006840; BAD39999.1; -; Genomic_DNA.
DR AlphaFoldDB; Q67QP4; -.
DR STRING; 292459.STH1014; -.
DR KEGG; sth:STH1014; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_3_9; -.
DR Proteomes; UP000000417; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02004; TPP_BZL_OCoD_HPCL; 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; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF166; 2-HYDROXYACYL-COA LYASE 2; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000417};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 12..124
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..537
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 551 AA; 58735 MW; 8F6D32615600E965 CRC64;
MKGEREMSFA HAGKLVARAL RNEGVEVVFT LCGGHVMSIY DGCLDEGIRV VDVRHEQTAA
FAADAWSRLT GRPGVAILTA GPGVTNAVTG IANAYRAQSP MVVIGGQGPR SLAGKGALQE
MDVLSVIRPI TKGQVSISDP ARIPEIVSWA FRTAMSGVPG PVYLEMPLDL LFAPWEDGGS
RLPAPYPGRP AMPGDESRVA AAAELLRAAE RPVVLIGSQV RWSPHWQAAR EFAEKVGAPV
YVSGMARGLL PPRWARSRKA ALAEADVALV FGTPLDFRLG YGGSPVWNEQ CRLIQVDLDP
AEPGRNRDAA VAIPGDSGTV MMQLLALGDL GAGRPARRAW LERLEAEEEK RLARMQPDLT
SEAMPVNPLR LCAEIDRALP EDAILIGDGG DFVATAANVV RVRRYPAGWM DPGPLGTLGI
GMGFAMAARL AHPDVPVVLL LGDGTAGLNL MEVEAAVRQN LPFVVVVGND AGWTQIRRGQ
VEMFGSERAP ATALSYTRYE RVAEALGGHG IWVERPEEIG PALRQALAAD RLTVINVKMG
GSDFRAGAIS V
//
