ID R3TLP6_9ENTE Unreviewed; 554 AA.
AC R3TLP6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Acetolactate synthase, catabolic {ECO:0000313|EMBL:EOL41933.1};
GN ORFNames=UC3_02281 {ECO:0000313|EMBL:EOL41933.1};
OS Enterococcus phoeniculicola ATCC BAA-412.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158610 {ECO:0000313|EMBL:EOL41933.1, ECO:0000313|Proteomes:UP000013785};
RN [1] {ECO:0000313|EMBL:EOL41933.1, ECO:0000313|Proteomes:UP000013785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-412 {ECO:0000313|EMBL:EOL41933.1,
RC ECO:0000313|Proteomes:UP000013785};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus phoeniculicola BAA-412.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:EOL41933.1}.
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DR EMBL; AJAT01000017; EOL41933.1; -; Genomic_DNA.
DR RefSeq; WP_010768925.1; NZ_KB946329.1.
DR AlphaFoldDB; R3TLP6; -.
DR STRING; 154621.RV11_GL001732; -.
DR PATRIC; fig|1158610.3.peg.2257; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_2_9; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000013785; 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:UP000013785};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..327
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..534
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 554 AA; 60598 MW; 57DE155CAAE16700 CRC64;
MGEKIKHGSD QVVESLKNHQ VPYIFGIPGA KIDGVFNALK EDGPELIVTR HEQNAAFMAQ
AVGRITGEPG LVIATSGPGA SNLATGLVTA TAEGDPVVAL GGQVKRGDLS KQTHQSMNNA
ALFEPITKYS VEVQDPETIS EIIANAYRIA KSSKKGASFI SIPQDVVDAP VKSQAIKPLS
DPELGSASPK AIQSLAQKIK GAKLPVLLVG MRASSLKESE AIRQLVSKTH LPVVETFQAA
GVISRKLEDH FFGRVGLFRN QPGDMLLKRS DLVIAVGYDP IEYEARNWNA EKDARMIVID
ETPAEIDQYL QPESELIGSI AGTLHALTEE IGSYQLTEDS QAYLATLQER LTARDSVSPR
EETGELHPLE VIRILQEHVT DEMTVTVDVG SHYIWMARHF RSYEPRHLLF SNGMQTLGVA
LPWAIAAALV RPKTQIVSVS GDGGFLFSAQ DLETAVRKNL NIVHLIWNDG HYNMVEFQEQ
MKYNQTSGVD FGPVDFVKYA EAFGAKGLRA TTAEELSQAI QEGFDTQGPV IIDIPIDYRD
NEKLGETILP DQFY
//
