ID   A0A0R2HZR2_9LACO        Unreviewed;       558 AA.
AC   A0A0R2HZR2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Acetolactate synthase, catabolic {ECO:0000313|EMBL:KRN58184.1};
GN   ORFNames=IV45_GL000627 {ECO:0000313|EMBL:KRN58184.1};
OS   Limosilactobacillus secaliphilus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=396268 {ECO:0000313|EMBL:KRN58184.1, ECO:0000313|Proteomes:UP000050934};
RN   [1] {ECO:0000313|EMBL:KRN58184.1, ECO:0000313|Proteomes:UP000050934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17896 {ECO:0000313|EMBL:KRN58184.1,
RC   ECO:0000313|Proteomes:UP000050934};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRN58184.1}.
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DR   EMBL; JQBW01000010; KRN58184.1; -; Genomic_DNA.
DR   RefSeq; WP_057741357.1; NZ_JQBW01000010.1.
DR   AlphaFoldDB; A0A0R2HZR2; -.
DR   STRING; 396268.IV45_GL000627; -.
DR   PATRIC; fig|396268.3.peg.635; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000050934; Unassembled WGS sequence.
DR   GO; GO:0003984; F:acetolactate synthase 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: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; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000050934};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          4..118
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          195..330
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          391..538
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   558 AA;  60586 MW;  2DAB3059EC3484D9 CRC64;
     MKKMTGADVV IDSLRKHGVD MVFGIPGAKI DRLFEALDGQ DSKDSPKLIV TRHEQNAVFM
     AQAYGRLTGK TGVAISTSGP GVGNLTTGIM TANAEGDPVL AIGGQVQRKD LHRATHQSTP
     STEIMAPITQ YSAEIQDPDN ISEIMANAFE ASQNGHKGTA FVSLPQDVDD ATVTEPALPI
     YQTPRMGPAD PQDLRKLVDL IKSAKLPVIL VGQRGADEEI TAALRRLMTD YHFPVVETYQ
     AAGVVSRDLE AQSYFGRVGL FRNQVGDQLL AASDLVLAVG YDAIEYEPRN WNANDDLRIV
     NLDTLPAQID NHYTPIMQLI GNIATSLQEL DSLLSGYSYP QAAKGTLAKF KQQLDADKQL
     QVPKEHGANH PLAIVQAIQE NVTDDMTVAV DVGSHYIWMA RHFRCYEPRH LLISNGMQTL
     GVGLPWAMVA AMLHPEHQAV AVVGDGGFLF SGAELATAVQ HHLNVVVIVW NDGGHYDMVK
     FQEEMKYPQA AGVTFGAVDI VKYAESCGAT GLRVNKPTEL KDTLQKAFKT DGPVVVDVPV
     DYSRNRDLAA KLISSQLG
//