ID Q74JI3_LACJO Unreviewed; 559 AA.
AC Q74JI3;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:AAS08946.1};
GN OrderedLocusNames=LJ_1124 {ECO:0000313|EMBL:AAS08946.1};
OS Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=257314 {ECO:0000313|EMBL:AAS08946.1, ECO:0000313|Proteomes:UP000000581};
RN [1] {ECO:0000313|EMBL:AAS08946.1, ECO:0000313|Proteomes:UP000000581}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNCM I-1225 / La1 / NCC 533
RC {ECO:0000313|Proteomes:UP000000581};
RX PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT johnsonii NCC 533.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; AE017198; AAS08946.1; -; Genomic_DNA.
DR RefSeq; WP_011161963.1; NC_005362.1.
DR AlphaFoldDB; Q74JI3; -.
DR GeneID; 83570439; -.
DR KEGG; ljo:LJ_1124; -.
DR PATRIC; fig|257314.6.peg.989; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_2_9; -.
DR Proteomes; UP000000581; Chromosome.
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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 8..122
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 201..329
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; 61683 MW; B209199ED4909D11 CRC64;
MAEEKYYGAN AIVDSLINHD VKFVFGIPGA KIDRVFELLE HSKDPRTPKF VLTRHEQNAA
FMAAGVGRIT GKPGVVLTTS GPGASNLATG LVTATAEGDP VLAISGQVQR TDLLRLTHQS
MKNAALFAPI TKYSAEVQEP ENISEVIANA YQEAEASKQG ASFVSVPQDV TDAEVKTSVI
APLEPPKLGP ASPIESTLLS QRIKAAKLPV LLLGMRASDP ETTRAIRRLI AETHLPVVET
FQGAGIIPRE LEDDFFGRVG LFRNQPGDQL LKKSDLVIAI GYDPIEYEPR NWNSDRSANI
VVIDSMRAEI DKNYQPEREL VGDISQTLDF LLPYMKGYSM PNESKEYLDS LRKTLQKRDT
PPAVTKDQVK SHPLSIIQAL QDRVTDDMTV TVDVGSFYIW MARHFRSYEP RHLLFSNGMQ
TLGVALPWAV AAALVRPNTK IVSVSGDGGF MFSSQDLETA VRLGLNIVHI IWNDGNYDMV
KFQEELKYGD SAAVKFGPVD FVKYAESFGA KGYRVEKAAD LDRILDKAFK EDGPTVVDIP
VDYSFNQELG KTILEDQLH
//