ID A0A0W0VPQ8_9GAMM Unreviewed; 553 AA.
AC A0A0W0VPQ8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KTD22103.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:KTD22103.1};
GN Name=budB_2 {ECO:0000313|EMBL:KTD22103.1};
GN ORFNames=Llan_1366 {ECO:0000313|EMBL:KTD22103.1};
OS Legionella lansingensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45067 {ECO:0000313|EMBL:KTD22103.1, ECO:0000313|Proteomes:UP000054869};
RN [1] {ECO:0000313|EMBL:KTD22103.1, ECO:0000313|Proteomes:UP000054869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49751 {ECO:0000313|EMBL:KTD22103.1,
RC ECO:0000313|Proteomes:UP000054869};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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:KTD22103.1}.
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DR EMBL; LNYI01000028; KTD22103.1; -; Genomic_DNA.
DR RefSeq; WP_028373789.1; NZ_LT906451.1.
DR AlphaFoldDB; A0A0W0VPQ8; -.
DR STRING; 45067.Llan_1366; -.
DR PATRIC; fig|45067.4.peg.1432; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000054869; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR CDD; cd02010; TPP_ALS; 1.
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; 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 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:UP000054869};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:KTD22103.1}.
FT DOMAIN 8..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 386..532
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 553 AA; 60792 MW; D17071E17D27427A CRC64;
MNKLNEQKVA ELIVKCLEEE GVEYIFGLPG EENIDFIEAL SHSKKIRFIL TRHEQAASFM
ADIYGRLTGK AGVCLATLGP GAINLLLGTA DANLDSSPLV AIMAQASLDR LNKESHQIID
LVRLFSPVTK WSAMISLPSV APELVRKAFK LAQAERTGAV ALVIPEDIAK EPTPSTLPLK
PQSPKLTMPN QDQIKKAANY INDAKNAIIL AGAGIYRQEA EEGLTRFVNQ TKIPVATTFM
AKGVVSSHNP LVIGTIGFMR HDYTNFGFDE ADVVITVGYD LVEYSPKSWN PKGDKKIIHI
HGSVAEVDTN YVLAVGIEGS ITAALDALAK EIKPREHLAS HTRSLRKMTE KEISEHEQDE
SFPLKPQRII SDLRKAAGES DIVLCDTGAL KMWMARLYPC YHSNTCIISN SLATMGFSLP
GALAAKLVHR DKKVIAVMGD GSFLMNSQEI ETAKREKIPF VILIWRDDAY GLIEWKQDLE
FGHSSHVTFT NPDFVKYAQS FGIQAHSIRS AKELLPTLNA ALSSNEIVLI DCPVDYSENV
KLTDKLGQLT ATI
//
