ID   A0A2T0SEH2_9ACTN        Unreviewed;       522 AA.
AC   A0A2T0SEH2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:PRY31812.1};
GN   ORFNames=CLV70_10223 {ECO:0000313|EMBL:PRY31812.1};
OS   Pseudosporangium ferrugineum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Pseudosporangium.
OX   NCBI_TaxID=439699 {ECO:0000313|EMBL:PRY31812.1, ECO:0000313|Proteomes:UP000239209};
RN   [1] {ECO:0000313|EMBL:PRY31812.1, ECO:0000313|Proteomes:UP000239209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45348 {ECO:0000313|EMBL:PRY31812.1,
RC   ECO:0000313|Proteomes:UP000239209};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812}.
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:PRY31812.1}.
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DR   EMBL; PVZG01000002; PRY31812.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0SEH2; -.
DR   OrthoDB; 2443624at2; -.
DR   Proteomes; UP000239209; 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:UP000239209}.
FT   DOMAIN          4..109
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          392..515
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   522 AA;  53139 MW;  62FE4A231E381B32 CRC64;
     MSGMTGAEAM ARTLIGGGVE VCFANPGTSE MHFVAALDRL PALRGVLCLF EGVATGAADG
     YGRMARRPAT TLLHLGPGLA NGVANLHNAR RAGTPIVNLV GDHALGHKPL DSLLESDIDA
     LAGTVSAWLR RSSTVDGLGT DVAAAVAASL APGGTGPDRT GTSGAIATLV VPADLSWSAP
     ARLAPPEPVA APAAPSPVEL DPVAAVLRSG EPVALLLDGT ALSGPGLRAA GRIARATGAR
     LLSRNWPARQ RRGAGVPLTE PLAYRGEQIT AQLTGVRHLV LAGAREPVTS FAYPGRTGRP
     TPAGTRIHAL PADFLEALAD EVAPGVTPVV ARLDPPPLPP GELTAGNWAA VVGALLPEEA
     IVCDESITAG LTTLHTATAS SPPHDVLGLT GLSIGQGLPV ALGAAMACPD RPVVCLEADG
     SAMYTLQALW SHAREQLDIT TVILNNRAYA ILRGELDRVG AGAAAAGLAD LSRPDLDFVS
     LATGLGVPAT RAWTTEELAR QFRHALSEPG PHLIEAMLLP GA
//