ID A0A429X2N6_9BACI Unreviewed; 531 AA.
AC A0A429X2N6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:RST57585.1};
GN ORFNames=D5F11_021965 {ECO:0000313|EMBL:RST57585.1};
OS Siminovitchia terrae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Siminovitchia.
OX NCBI_TaxID=1914933 {ECO:0000313|EMBL:RST57585.1, ECO:0000313|Proteomes:UP000287296};
RN [1] {ECO:0000313|EMBL:RST57585.1, ECO:0000313|Proteomes:UP000287296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29736 {ECO:0000313|EMBL:RST57585.1,
RC ECO:0000313|Proteomes:UP000287296};
RA Sun L., Chen Z.;
RL Submitted (DEC-2018) 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:RST57585.1}.
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DR EMBL; QYTW02000031; RST57585.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A429X2N6; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000287296; 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; 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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF129; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..111
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 187..320
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 380..526
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 531 AA; 58029 MW; 618F7F064E1CDB57 CRC64;
MKATDVLVQC LENEGVEYVF GIVGKETLDL VESISRSQQI QFIPVRHEQG AAFMAGVYGK
LAKRPGVCTA TLGPGAGNLL TGLATAQLDG SPVVAIAGQA GLGMQHKHSH QFIEMTDVME
PVTKWSAQIK EADTIPEMIR KAFKTAYEGK HGAVFLELPE NLAVKPVPPK VLPIMNEQPV
LPSLQTIQCA ISSLKQSERP FVIIGQKVIK QEACAEVLAF ISKLQAPVTH SFMAKGVLPK
DAPNNYFTFG FNENDLVLSG IDEADLLIVI GFDTIERLPK EWNRRRIPIL HIDSELPEPD
EYYPVATQVM GHIKNSLQML NSLDVPVKSW VPSGNLKKNI EQSYQITLEF SNIAQSPLSI
EKILHIIEKQ TSDNAVVVSD VGAHKISIAR TYQPKEPGSL IISNGLASMG IAIPGSIGAK
LACPNAPVIC ITGDGGAMMT FSELEVAKRI GLPVVIIVLN DQVLKLEQKM MNKKFGKSFN
VTFGNPDFLI LADSFGIKGF RPESMRDFEE VFQTAISLQE PVLFDIQLPH S
//
