ID A0A0C2Y9Y2_BACBA Unreviewed; 565 AA.
AC A0A0C2Y9Y2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:KIL78323.1};
GN ORFNames=SD77_4003 {ECO:0000313|EMBL:KIL78323.1};
OS Bacillus badius.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1455 {ECO:0000313|EMBL:KIL78323.1, ECO:0000313|Proteomes:UP000031982};
RN [1] {ECO:0000313|EMBL:KIL78323.1, ECO:0000313|Proteomes:UP000031982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MTCC 1458 {ECO:0000313|EMBL:KIL78323.1,
RC ECO:0000313|Proteomes:UP000031982};
RA Verma A., Khatri I., Mual P., Subramanian S., Krishnamurthi S.;
RT "Genome Assembly of Bacillus badius MTCC 1458.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:KIL78323.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JXLP01000009; KIL78323.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2Y9Y2; -.
DR STRING; 1455.SD78_0846; -.
DR PATRIC; fig|1455.5.peg.2072; -.
DR Proteomes; UP000031982; 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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF169; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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 21..135
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 208..344
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 395..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 565 AA; 61602 MW; B61630F2F0764C0D CRC64;
MSSDSIFIRR TNSKRMGEDV MKAVHTVLQY LRGIGIKHVF GIPAGSVNAF FDELYDMPDI
TPVIAKHEGA AAYMAASYAK YSKQLSVCIG CSGPGATNLV TGAANAMREH LPVLFLTGAV
PVNTVGLNAS QELNAEPIFR PVTKYSITVT DAKDLLAEVV KATEIAVSGV PGPVHIAMPI
DVQQGMAENA DIPSLPARTP MIPDSQLIKT TAKEIAARES GYIFAGQGAR DSIELVTELA
ELLDWPIVVT PQAKGLIPDN HPLLAGVFGF AGHESASALM NDGEGETLLI VGSSLGETAT
NNYNENLTKN RFTVQMDFDK SVFHRKYPID LPVLGDIHVS LSALIQELKE LGLSKKENRP
IEKSSELPNI EEYNTKNVLS MLQHYLPLTT RYTVDIGEFM SYVIHHMNVF DSHTYDINVH
FGAMGSGIGS AIGSKLAEPE RPVVCITGDG CFFMHGMEIL TAKEHRLPIL FVVMNNARLG
MVYHGHTLQY HRSHSAFEQQ PVNIAALAEA MNIPSFRIES MEDVNQEAIE RLTDLDGPAL
LEVSLVDNNI PPMGDRVKFL SSFSK
//