ID   D5E116_PRIM1            Unreviewed;       559 AA.
AC   D5E116;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Acetolactate synthase, catabolic {ECO:0000313|EMBL:ADE67822.1};
DE            EC=2.2.1.6 {ECO:0000313|EMBL:ADE67822.1};
GN   Name=alsS {ECO:0000313|EMBL:ADE67822.1};
GN   OrderedLocusNames=BMQ_0789 {ECO:0000313|EMBL:ADE67822.1};
OS   Priestia megaterium (strain ATCC 12872 / QMB1551) (Bacillus megaterium).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=545693 {ECO:0000313|EMBL:ADE67822.1, ECO:0000313|Proteomes:UP000000935};
RN   [1] {ECO:0000313|EMBL:ADE67822.1, ECO:0000313|Proteomes:UP000000935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12872 / QMB1551 {ECO:0000313|Proteomes:UP000000935};
RX   PubMed=21705586; DOI=10.1128/JB.00449-11;
RA   Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA   Koenig S.S., Huot Creasy H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA   Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA   Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA   Bremer E., Jahn D., Ravel J., Vary P.S.;
RT   "Genome sequences of the biotechnologically important Bacillus megaterium
RT   strains QM B1551 and DSM319.";
RL   J. Bacteriol. 193:4199-4213(2011).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP001983; ADE67822.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5E116; -.
DR   STRING; 545693.BMQ_0789; -.
DR   KEGG; bmq:BMQ_0789; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_2_9; -.
DR   Proteomes; UP000000935; Chromosome.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0034077; P:butanediol metabolic process; IEA:InterPro.
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; IPR012782; Acetolactate_synth_catblc.
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; IPR000399; TPP-bd_CS.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   NCBIfam; TIGR02418; acolac_catab; 1.
DR   PANTHER; PTHR18968:SF129; ACETOLACTATE SYNTHASE; 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.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000935};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000313|EMBL:ADE67822.1}.
FT   DOMAIN          12..125
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          197..330
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          393..539
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   559 AA;  60864 MW;  0CC0779D986A9BB1 CRC64;
     MMSNADTTET KKGADLLVES LASQNVPYIF GIPGAKIDGV FDVLKEKGPE VIVCRHEQNA
     AFMAAAMGRL TGTPGVCLVT SGPGAANLAT GLVTATSEGD PVVALAGAVP RADRLKKTHQ
     SMDNEGLFKS IAKFSVEVED AANVPEVITD AFREAVSSPS GASFVSLPQD VMDNETSAST
     LSVLKAPTIG AANLDAVAQA IHTIRTAKLP VLLLGMRASK SKAVESIRQL IAEHDLPVVE
     TFQGAGAVSR ELETHFFGRV GLFRNQPGDV LLKHADVVLT IGYDPVEYPP SLWNSESQRS
     IIHLDDLQAQ ADHHYQPEIE LVGDIPSTID ILADKLPHLI RSKESASFLK TLKSKLEQPD
     DQYEFSNDTH LHPLQLIEAL QNFVEDDTTI TCDVGSHYIW MARYFRSYEP QHLLFSNGMQ
     TLGVALPWAI SAALVRPHKK VLSLSGDGGF LFSAMELETA VRLNLPIVHI IWNDQTYDMV
     GFQQQIKYGR KSAVEFGSVD FVTLAESFGA KGFRVNSPEE FSDTLASAFR EQGPVIIDVP
     VDYKDNEKLN TQLLPDQIN
//