ID A0A222VVU1_9PSEU Unreviewed; 517 AA.
AC A0A222VVU1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SDD25579.1};
GN ORFNames=DES30_106429 {ECO:0000313|EMBL:PWV75810.1},
GN SAMN05421630_10712 {ECO:0000313|EMBL:SDD25579.1};
OS Prauserella marina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Prauserella.
OX NCBI_TaxID=530584 {ECO:0000313|EMBL:SDD25579.1, ECO:0000313|Proteomes:UP000199494};
RN [1] {ECO:0000313|EMBL:SDD25579.1, ECO:0000313|Proteomes:UP000199494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5506 {ECO:0000313|EMBL:SDD25579.1,
RC ECO:0000313|Proteomes:UP000199494};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PWV75810.1, ECO:0000313|Proteomes:UP000246674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45268 {ECO:0000313|EMBL:PWV75810.1,
RC ECO:0000313|Proteomes:UP000246674};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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; QGTN01000006; PWV75810.1; -; Genomic_DNA.
DR EMBL; FMZE01000007; SDD25579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222VVU1; -.
DR STRING; 530584.SAMN05421630_10712; -.
DR KEGG; pmad:BAY61_25755; -.
DR OrthoDB; 2443624at2; -.
DR Proteomes; UP000199494; Unassembled WGS sequence.
DR Proteomes; UP000246674; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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 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:SF86; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVX-RELATED; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000199494}.
FT DOMAIN 1..106
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 374..510
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 517 AA; 52785 MW; FB56AB2133B52706 CRC64;
MNGAQSLIRT LVDAGVDVCF SNPGTSEMHF VAALDTVPEM RGVLGLAEGV VTGAADGYAR
IAGKPAATLL HLGPGLGNGL ANLHNARRAN TPVVNVIGDH ATYHKRYDAP LESDIEAVAG
SLEGWVRRSE SSADVGADAA AAVAAAMDAP GRVATLILPA DVSWSDGGVV CAPVPGRTPK
PVADTTVKAI AEVLGTGEPT ALLIGGAACR EAGLRAASRI ATATGATPFI ETFPRKLERG
AGLPAIDRLG YLAEQVAYQL DGVRHVIIAG TKSPVSFFAY PGKESDLVPE GAGVHTLAEG
ADDVVAALSQ LADLVAPDTE PVLAEPRRPE LPSGELTAQN WVDVIGALLP ENAIISDEAN
TSGLLLPAAT AGAPRHDVLT LTGGAIGQGI PAATGAAIAA PDRPVISLES DGSALYTISA
LWTQARENLD VTTVILNNRA YAILRMELQR VGAEGSGPKA NSLLDLSTPD LNFVSIAEGL
GVPATRATTA EELAEQFAAA IAEPGPHLIE AMVPPLL
//
