ID A0A3T0HYL1_9BACI Unreviewed; 528 AA.
AC A0A3T0HYL1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:AZU62234.1};
GN ORFNames=CHR53_13590 {ECO:0000313|EMBL:AZU62234.1};
OS Neobacillus mesonae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1193713 {ECO:0000313|EMBL:AZU62234.1, ECO:0000313|Proteomes:UP000282892};
RN [1] {ECO:0000313|EMBL:AZU62234.1, ECO:0000313|Proteomes:UP000282892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H20-5 {ECO:0000313|EMBL:AZU62234.1,
RC ECO:0000313|Proteomes:UP000282892};
RA Kim S.Y., Song H., Sang M.K., Weon H.-Y., Song J.;
RT "The complete genome sequence of Bacillus mesonae strain H20-5, an
RT efficient strain improving plant abiotic stress resistance.";
RL Submitted (JUL-2017) 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; CP022572; AZU62234.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3T0HYL1; -.
DR STRING; 1193713.GCA_001636315_05156; -.
DR KEGG; nmk:CHR53_13590; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000282892; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000282892};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 189..319
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 377..516
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 528 AA; 57426 MW; 70C979B1D129C173 CRC64;
MKVTDVLVKC LENEGVEYIF GIVGSETLDL ADSLSKSTKI QLINVRHEQG AAFMADVYGR
TAKKTGVCLS TLGPGASNLL TGIASAQLDH SPVVALVGQA GIDRHHKESH QYVDLVKLFE
PVTKWCTQIQ ASPTVPSAVR NAFRTAAMEK PGAAAIVLPE NFSAQMIANE PLMVSPLPVT
EPAMESVYAA KSLIEQHIKP LLVIGNGVVR QDAVFELQLL VEQLESPAFH SFMAKGVLPK
DHPQNFYTFG FNENDLVLSG LQEADLLIVI GFDFVEKLPK DWNKKKIPVL HIDSLPAETN
DYYPAKVELV GNIKQTLQLL NQTSLTKKPW EPTGNLKEVI KTAYHLNPES GNMTFTIKNM
LHSIERLTND DTIIISDVGA HKVSIARTYQ PKKPNGLIIS NGLASMGIAI PGAIGAKLAA
PDAPVICITG DGGAMMNFSE IETAKRLGVS FIIIVLNDSV LKLEVQQMDK KFGESYGAAF
TNPDFAKLAD SFSIQGRRAK TLADFKAVLT EALERPNEIF LIDTVLEG
//
