ID A0A075LIU1_9BACI Unreviewed; 547 AA.
AC A0A075LIU1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:AIF66314.1};
GN ORFNames=GZ22_06540 {ECO:0000313|EMBL:AIF66314.1};
OS Terribacillus goriensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Terribacillus.
OX NCBI_TaxID=386490 {ECO:0000313|EMBL:AIF66314.1, ECO:0000313|Proteomes:UP000027980};
RN [1] {ECO:0000313|EMBL:AIF66314.1, ECO:0000313|Proteomes:UP000027980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP602 {ECO:0000313|EMBL:AIF66314.1,
RC ECO:0000313|Proteomes:UP000027980};
RA Wang Y., Lu P., Zhang L.;
RT "Complete genome sequence of a moderately halophilic bacterium
RT Terribacillus aidingensis MP602, isolated from Cryptomeria fortunei in
RT Tianmu mountain in China.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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; CP008876; AIF66314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A075LIU1; -.
DR KEGG; tap:GZ22_06540; -.
DR HOGENOM; CLU_013748_3_1_9; -.
DR Proteomes; UP000027980; 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; 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:SF13; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000027980};
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 188..321
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 377..525
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT COILED 338..365
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 547 AA; 59710 MW; C10CE56F0D1E4880 CRC64;
MKAARVVLEY IQANGIKHIF GIPAGSVNAF FDELYDMPEL TPIVTKHEGA ASYMAAAYAK
YSNQLSVCIG CSGPGATNLV TGAANAMREH LPVLFITGAV PVDTVGLNAS QELDVEPVFR
SVTKYSVTVS DAKDLLREVE IATEIAISGV PGPVHIAIPI DIQHAALNHT ELHNPPKRLP
MVPEHDTIKT VARELLKRES GYIFAGQGVR NSIEALIELA ELLNWPIITS PQAKGYIPEQ
HPLLVGVFGF AGHEAASELI NEGDGQALLI VGSSLGETAT NNYNGNLLRN RFSVQMDFDR
SVFNRKYEID IPVLGDIDLS LLHLIVELKA LGLQSKSTEL AVEKNNEAEE HMEEYNTKNV
LLSIQKYVPT STRYTIDIGE FMSYVIHHMK VLDSDTYNIN VHFGAMGSGI GAAIGSKLAE
PERPVVCITG DGCFFMHGME IATAKEYNLP ILFVVMNNAR LGMVYHGHAL QFKRTHTSFE
QEPINISAMA AAMNIPSYRV SDLEDINQNV IDSLTNLNGP SVLEIALVDN NTPPMGDRVK
FLSSFGK
//
