ID   A0A2T1CSN5_9CYAN        Unreviewed;       601 AA.
AC   A0A2T1CSN5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:PSB11246.1};
GN   ORFNames=C7B62_06165 {ECO:0000313|EMBL:PSB11246.1};
OS   Pleurocapsa sp. CCALA 161.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Hyellaceae;
OC   Pleurocapsa.
OX   NCBI_TaxID=2107688 {ECO:0000313|EMBL:PSB11246.1, ECO:0000313|Proteomes:UP000239836};
RN   [1] {ECO:0000313|EMBL:PSB11246.1, ECO:0000313|Proteomes:UP000239836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCALA 161 {ECO:0000313|EMBL:PSB11246.1,
RC   ECO:0000313|Proteomes:UP000239836};
RA   Cohen D.B., Kent A.D.;
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PSB11246.1, ECO:0000313|Proteomes:UP000239836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCALA 161 {ECO:0000313|EMBL:PSB11246.1,
RC   ECO:0000313|Proteomes:UP000239836};
RA   Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT   "The ancient ancestry and fast evolution of plastids.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:PSB11246.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; PVWF01000017; PSB11246.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T1CSN5; -.
DR   InParanoid; A0A2T1CSN5; -.
DR   OrthoDB; 9785953at2; -.
DR   Proteomes; UP000239836; 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   CDD; cd00568; TPP_enzymes; 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; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000239836};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          36..149
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          241..364
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          419..562
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          571..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   601 AA;  63700 MW;  4F3596EB510061DF CRC64;
     MQLSSSKAKK TADRDGNNKA IASPTQKFKE IPQLCVAQAI VKVLENLGVR EAFGVSGGAM
     ATLWGALSNS ILIDVLHCRH EGGAAFAAAE AHFASDRPIV VFTTAGPGIT NAITGLWAAR
     DEGAKVIYLS ACTSATQRGR WAIQETSDQT IPQSGIFTSG ALFNYATVLE SPQQLPQIAR
     RLALGLAQPG GFVAHLSIPT GVQSIPIETH IPEVNLAPAL SVPSQETIET IAQLLCEGSF
     AIWAGFGARR ASAAILKLAE RTGSAVMCSP RGKGIFPEKH PQYVGVTGVG GHESVMNYMQ
     EFSPQRILVL GTRLGEPTSF WSKDMVPAKG FIHVDVDPKV PGVAFPFADT LPIIADADIF
     VKALLKHFPE QTEQNITLPN PELNAIAPAE SNLVRPEILM QAIQRIVVDG SDAVVLSESG
     NSFTWTTNML RFPQANRYRV STGVGSMGHN VTGVVGAARG RNGKAVAVVG DGSMLMNSEV
     STAVKYQLPT VWIVLNDAYY NMCNQGMTLL GMKGADAKLP DTDFSLIARG MGAEGIRVEA
     EVNLESALER AMAATGPVVV DVTIDPTRFA PSKGRNKSLS AQGVKSSTEP AKGTQVSFPL
     V
//