ID A0A0R2DL15_9LACO Unreviewed; 559 AA.
AC A0A0R2DL15;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KRN04792.1};
GN ORFNames=FC86_GL001149 {ECO:0000313|EMBL:KRN04792.1};
OS Holzapfeliella floricola DSM 23037 = JCM 16512.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Holzapfeliella.
OX NCBI_TaxID=1423744 {ECO:0000313|EMBL:KRN04792.1, ECO:0000313|Proteomes:UP000051378};
RN [1] {ECO:0000313|EMBL:KRN04792.1, ECO:0000313|Proteomes:UP000051378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23037 {ECO:0000313|EMBL:KRN04792.1,
RC ECO:0000313|Proteomes:UP000051378};
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:KRN04792.1}.
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DR EMBL; AYZL01000006; KRN04792.1; -; Genomic_DNA.
DR RefSeq; WP_056974108.1; NZ_AYZL01000006.1.
DR AlphaFoldDB; A0A0R2DL15; -.
DR STRING; 1423744.FC86_GL001149; -.
DR PATRIC; fig|1423744.4.peg.1179; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000051378; 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:UP000051378};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 197..331
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; 61866 MW; A19906070398BF51 CRC64;
MKIEKNGSNA LIQTMINQGI DYIFGIPGAK IDQLFNDLKN YPDSKKPKLI VARHEQNAAF
MASGIGRLTE KPGVVLVTSG PGVSNLATGL ITATSEGDPV IALGGQVPRN DISRLTHQSI
PSRELLSEAT KSSYEVEMAD NISEVFISAY IAATSPKAGA SFISIPQDVL SAPVEKEAIK
RFDLPDENAE ATTASLKKVI SKIKNADFPV ILAGMRSSEQ RVTDALHQLL SRFSIPIVET
FQAAGILSHK YEHNYFGRVG LFRNQIGDTV LKQSDLVITI GYDPVEYEAR NWNSSGYREI
INIDTVDPEI TNEYQPSLII KTDLANTINK LAQLLPEGLK IKATSNQIIQ KLRYQFDYEE
SDFKFKNPDL LNPLQIVETL QQFADDSNIV TVDVGSHYIW MARYFRSYQP RQLLFSNGMQ
TLGVALPWAI SASILNPDKK IISVSGDGGF LFSGQELETA VRLQSNIIHL IWEDNAYDMV
KFQEEIKYNQ SSGVDFGPVD YMKYAQAFGA EGIKVNSQQE LAEALNQANE IQGPVIIVIP
VDYSANIQLK TSLIENTTN
//
