ID A0A084JRK8_9FIRM Unreviewed; 644 AA.
AC A0A084JRK8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KEZ91592.1};
GN ORFNames=IO98_02655 {ECO:0000313|EMBL:KEZ91592.1};
OS Lacrimispora celerecrescens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lacrimispora.
OX NCBI_TaxID=29354 {ECO:0000313|EMBL:KEZ91592.1, ECO:0000313|Proteomes:UP000028525};
RN [1] {ECO:0000313|EMBL:KEZ91592.1, ECO:0000313|Proteomes:UP000028525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=152B {ECO:0000313|EMBL:KEZ91592.1,
RC ECO:0000313|Proteomes:UP000028525};
RA Honkalas V.S., Dabir A.P., Arora P., Dhakephalkar P.K.;
RT "Draft genome of Clostridium celerecrescens 152B isolated from sediments
RT associated with methane hydrate from Krishna Godavari basin.";
RL Submitted (JUL-2014) 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:KEZ91592.1}.
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DR EMBL; JPME01000003; KEZ91592.1; -; Genomic_DNA.
DR RefSeq; WP_038277608.1; NZ_JPME01000003.1.
DR AlphaFoldDB; A0A084JRK8; -.
DR STRING; 29354.IO98_02655; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000028525; Unassembled WGS sequence.
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; cd00568; TPP_enzymes; 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:SF142; ACETOLACTATE SYNTHASE; 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:UP000028525};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 230..365
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 444..594
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 644 AA; 70769 MW; 673FA427462E2310 CRC64;
MRMKVSNYIS QKLVDSGITQ VFTVTGGGAM HLNDALGHQE GMHCLYNHHE QACAIAAESY
ARIKDRIAAV CVTTGPGGTN AITGVLGGFL DSIPMLILSG QVRYDTTARW SGVGIRAMGD
QEFDITKAID CMTKYSEMVI DPMRIRYTLE KAIYLALSGR PGPTWLDIPL NVQGAYIETE
DLIGFSPENY EQGGDGWSSE TNAKIKQDDP GFGENRQILP EKVTADAARA ILEKIKSSSR
PVINAGNGIR IGQAHEIFLR VVDKLGIPVV TGWNSQDCIE EEHPLYTGRG GGMGDRAGNF
AIQNSDLVLS LGSRLSIRQV GYNYTTWARE AYVIVNDIDP EELKKPSVHA DMKIQADVKV
LLTALDELLD SEYKASLKQP LFSGGKGLDS MTWNETCRMW KKKYPVVLPK HYRSGEDEEA
NVYAFIKELS TRVPEDRVTV VGNGSACVVG GHAYIIKKGQ RFISNSAVAS MGYDLPAAIG
ASVAEQGEDV ILVTGDGSIQ MNLQELQTII HHHMPVKIFL INNGGYHSIR QTQKNFFGEP
LVGIGVDSRD LSFPDMEKLS AAYGYPYVRA CHNSELKHAI ETALSTKGPV ICEVFVSQDQ
NFEPKSSAKR LPDGTLISPP LEDMSPFLSD EEMNRNMIIP RIRE
//
