ID A0A0P9CU71_9GAMM Unreviewed; 545 AA.
AC A0A0P9CU71;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Acetolactate synthase, large subunit {ECO:0000313|EMBL:SCX84353.1};
GN ORFNames=SAMN05661077_0645 {ECO:0000313|EMBL:SCX84353.1};
OS Thiohalorhabdus denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalorhabdales;
OC Thiohalorhabdaceae; Thiohalorhabdus.
OX NCBI_TaxID=381306 {ECO:0000313|EMBL:SCX84353.1, ECO:0000313|Proteomes:UP000183104};
RN [1] {ECO:0000313|Proteomes:UP000183104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL 19 {ECO:0000313|Proteomes:UP000183104};
RA Varghese N.;
RL Submitted (OCT-2016) 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; FMUN01000001; SCX84353.1; -; Genomic_DNA.
DR RefSeq; WP_054966234.1; NZ_LJCP01000010.1.
DR AlphaFoldDB; A0A0P9CU71; -.
DR STRING; 381306.AN478_08795; -.
DR PATRIC; fig|381306.5.peg.409; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000183104; 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 GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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:UP000183104};
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 378..524
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 545 AA; 59519 MW; F205AF003C97F6D6 CRC64;
MNSAECLVTC LENENTRFVF GLPGEETLAL YEALRESSIR VVTCRHEQGA AFMADVHGRL
TGKPGVCIST LGPGATNLIT GVADADLDRA PLVAITGQAS LDRTHKESHQ YLDLVSLFRP
ITKWNAQIKR GEVVPEMVRH AFREAALEKP GATHLDLPED VADAPVRADA TPLSSQPLPR
PEPPMQELEQ AADFLSRSRN ALILAGNGVI RAGASDALRY FARSLNIPVA HTFMAKGVFP
YNDPLAIMTA GIQARDYVAC GFEAADAIIC VGYDATEYAP KSWNPNREKP ILHIAQTPAE
LDSHYTTEVE VVGDLESALN YLAEAVAPRA DNIIPQLHDP VMRELRAHNE DTSVPFKPQR
VLWDLHRVLD PRDIVVSDVG AHKVWVARMF PSSVPNTCII SNGFASMGIA LPGAIAAKLT
RPERRVVAVA GDGGALMNIQ ELETAVRLGT PFVLLVFSDG MYGLIEWKQQ RRYGHSTEVG
FGNPDWVKLA ESFGALGARV TTSEELRPAL QWAVDQDRPV IMEVPIDARE NLKLTEQLGD
LVCPI
//
