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Database: UniProt
Entry: A0A0R1JMB6_9LACO
LinkDB: A0A0R1JMB6_9LACO
Original site: A0A0R1JMB6_9LACO 
ID   A0A0R1JMB6_9LACO        Unreviewed;       557 AA.
AC   A0A0R1JMB6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KRK72462.1};
GN   ORFNames=FD02_GL001434 {ECO:0000313|EMBL:KRK72462.1};
OS   Lacticaseibacillus nasuensis JCM 17158.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1291734 {ECO:0000313|EMBL:KRK72462.1, ECO:0000313|Proteomes:UP000051804};
RN   [1] {ECO:0000313|EMBL:KRK72462.1, ECO:0000313|Proteomes:UP000051804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 17158 {ECO:0000313|EMBL:KRK72462.1,
RC   ECO:0000313|Proteomes:UP000051804};
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:KRK72462.1}.
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DR   EMBL; AZDJ01000022; KRK72462.1; -; Genomic_DNA.
DR   RefSeq; WP_056950936.1; NZ_AZDJ01000022.1.
DR   AlphaFoldDB; A0A0R1JMB6; -.
DR   STRING; 1291734.FD02_GL001434; -.
DR   PATRIC; fig|1291734.4.peg.1477; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000051804; 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; 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:UP000051804};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          7..122
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          198..328
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          391..537
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   557 AA;  60412 MW;  EB80459BB8176401 CRC64;
     MTNKRYGADL IVESLINHDV KYVFGIPGAK IDRVFERLEH PQSDHAPQLI VARHEQNAAF
     MAAGIGRLTG KPGVVITTSG PGASNLATGL VTATAEGDPV LAISGQVKRA DLLRSSHQSM
     KNAELFAPIT KYSAEVQDPD NVSEIIANAY QAAESGKQGA SFVSVPQDVT DAEVASQPIR
     RLTAPKLGPA SPADMTYLAR AIKEAQLPVL LLGMRASAEP ITRALRDLLS VTELPVVETF
     QGAGIVSREL EDNFFGRVGL FRNQPGDQLL KAADLVITIG YDPVEYEPRN WNAEGDARII
     DIDSAPAEID HNFQPETELI GDIEQTLDIL TPLLRGYQVA PSAKHFLSEL QAKLQQRDVP
     PVDADAKRSH PLAIVAELQQ RVTDDMTVAV DVGSFYIWMA RHFRSYQPRR LLFSNGMQTL
     GVALPWAIAA TLVRPGEKAV SISGDGGFLF SGQELETAVR LHANLVHIIW NDGHYDMVKF
     QEEMKYGQSA GVNFGPVDFV KYAESFGAKG LRVNTPAELG AVLDEAFAAD GPVVVDIPVD
     YSHNQALGQA MLPDQLV
//
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