ID   A0A1H8QPT9_9PROT        Unreviewed;       577 AA.
AC   A0A1H8QPT9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SEO55884.1};
GN   ORFNames=SAMN02990966_02291 {ECO:0000313|EMBL:SEO55884.1};
OS   Rhodospirillales bacterium URHD0017.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales.
OX   NCBI_TaxID=1380357 {ECO:0000313|EMBL:SEO55884.1, ECO:0000313|Proteomes:UP000198826};
RN   [1] {ECO:0000313|EMBL:SEO55884.1, ECO:0000313|Proteomes:UP000198826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URHD0017 {ECO:0000313|EMBL:SEO55884.1,
RC   ECO:0000313|Proteomes:UP000198826};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812}.
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DR   EMBL; FODP01000004; SEO55884.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8QPT9; -.
DR   STRING; 1380357.SAMN02990966_02291; -.
DR   OrthoDB; 7534569at2; -.
DR   Proteomes; UP000198826; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd02002; TPP_BFDC; 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; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF164; PYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 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.
PE   3: Inferred from homology;
FT   DOMAIN          10..141
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          427..570
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   577 AA;  62114 MW;  6BCD4854F79583FE CRC64;
     MDSINEARRS AAHYFLEGLT EIGCDYIFCN FGTDHAPIIE AMAAFKRDGR KAPKTVICPH
     EITAAHMAAG YFLATGRGQG VMVHVDSGTA NSAMALHNIC RARIPVLLMA GRAPYTTRGE
     LLGTRDTYVH FIQEPFDQAA LVRPYTKWEY NLPSGVVAKE ALRRAHTVMM SDPKGPVYMT
     FARETLTELW SEGQIRSYPE ERFRAAPAGA VDRQSVDAIA TRLLTAEHPL LITAYSGRNP
     DAVALLDELA QFAGIRVVEF SPVHLNLPHD SPCHGGFVPT KALADADVGL QVDVDVPWIP
     KDMPENPSTW WAHVDVDPEK RAIPMWTFPA NLRLRGDSCL FYAELLAVLK ARADTGFKAR
     AAARVKEIAA EGVARREQAA KLAAEPGVAG EINPHHLCAK LVKALGPSGV VINEAIRNIP
     TVLAQMPRTE PGTLVGLAGA GLGFSASVAL GLKLAMPDRI VMPIMGDGTF YFSNPQSVLA
     VSQNYGLPVF MVVLDNSGWG AVKEATLRVY PAGEAKAGDD YGANFGMNMD FGKIAEAAGA
     HGEFLSEPAD VDGAIERCLA AVRSGRAAVL HAKVTKI
//