ID   A0A2G9N1X0_9ARCH        Unreviewed;       548 AA.
AC   A0A2G9N1X0;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=COV47_03920 {ECO:0000313|EMBL:PIN85097.1};
OS   Candidatus Diapherotrites archaeon CG11_big_fil_rev_8_21_14_0_20_37_9.
OC   Archaea; Candidatus Diapherotrites.
OX   NCBI_TaxID=1974407 {ECO:0000313|EMBL:PIN85097.1, ECO:0000313|Proteomes:UP000229477};
RN   [1] {ECO:0000313|EMBL:PIN85097.1, ECO:0000313|Proteomes:UP000229477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG11_big_fil_rev_8_21_14_0_20_37_9
RC   {ECO:0000313|EMBL:PIN85097.1};
RA   Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.,
RA   Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M.,
RA   Klingl A., Woyke T., Ryan C.M., Banfield J.F.;
RT   "Depth-based differentiation of microbial function through sediment-hosted
RT   aquifers and enrichment of novel symbionts in the deep terrestrial
RT   subsurface.";
RL   Submitted (SEP-2017) 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:PIN85097.1}.
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DR   EMBL; PCWY01000049; PIN85097.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G9N1X0; -.
DR   Proteomes; UP000229477; 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:0006082; P:organic acid metabolic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0044272; P:sulfur compound biosynthetic 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; 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   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          3..117
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          188..318
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          383..526
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   548 AA;  60174 MW;  96CBB1F99ECF7C4C CRC64;
     MLVEEVIVKT LEANGVQNAF GFPGETTLPL YKALKESSIK HYLARDERCA AHMADGYARI
     TNKIGVCDAP AGMGVPFLCP ALLEAYNSST PMLAIVSDTP KELKGKWATS ELDQETMLKP
     VTKQQYVVSI PNNAAALTAK AIKESISGRS RPTLLQISYN LFGQTSKYST LKLLQKKGKT
     ISSNLAIKAI AMLLNAQKPL ILAGGGVFLS GAENELIRFA EQTMVPVATT LTGKGAIPEI
     HPLSLGVVGG KGRDYSNEYA MQADCVLILG SKLGEKSTNS WTFFKKTKLI RVDIDKKELN
     NNYNAEIKFN STVKLALQTF LKCLTLNIKH QKNKFLNQKK SWSTNFDKQC EYNSSVVKPQ
     FIIKKLQELS PKNTILVADG STASGWTGVH WICTDIGRKF IASRGTGMIG FSLPASIGAK
     IGASHDKVIS ISGDGGFMFS CHELETAHRY NIPIVQIILN NQSLRLLQQH GKYFLGDEII
     SNYDNVDFVK LSESCKVTAL EITRKSQVQN ALKTALAAEE PIVLDFKIDR NELSPDFVNT
     LKRKKIVA
//