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Database: UniProt
Entry: V6MDD2_9BACL
LinkDB: V6MDD2_9BACL
Original site: V6MDD2_9BACL 
ID   V6MDD2_9BACL            Unreviewed;       561 AA.
AC   V6MDD2;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:EST53398.1};
GN   ORFNames=T458_21540 {ECO:0000313|EMBL:EST53398.1};
OS   Brevibacillus panacihumi W25.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1408254 {ECO:0000313|EMBL:EST53398.1, ECO:0000313|Proteomes:UP000017973};
RN   [1] {ECO:0000313|EMBL:EST53398.1, ECO:0000313|Proteomes:UP000017973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W25 {ECO:0000313|EMBL:EST53398.1,
RC   ECO:0000313|Proteomes:UP000017973};
RX   PubMed=24459276;
RA   Wang X., Jin D., Zhou L., Wu L., An W., Chen Y., Zhao L.;
RT   "Draft Genome Sequence of Brevibacillus panacihumi Strain W25, a
RT   Halotolerant Hydrocarbon-Degrading Bacterium.";
RL   Genome Announc. 2:e01215-13(2014).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:EST53398.1}.
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DR   EMBL; AYJU01000017; EST53398.1; -; Genomic_DNA.
DR   RefSeq; WP_023558096.1; NZ_KI629785.1.
DR   AlphaFoldDB; V6MDD2; -.
DR   STRING; 1408254.T458_21540; -.
DR   PATRIC; fig|1408254.3.peg.4229; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_1_9; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000017973; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd00568; TPP_enzymes; 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:SF13; ACETOLACTATE SYNTHASE, CHLOROPLASTIC; 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:UP000017973};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          10..129
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          201..331
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          394..534
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   561 AA;  59106 MW;  27C097C0E52C6605 CRC64;
     MTTNGQMEYT TADAVVAELV RAGVEVVFGV VSIHNMPIYD ALLREGSIRI VCSRGESGAA
     NMADGYARST GKLGVVITST GSGAANAAGS LVEAWAAGTP VLHLTGEVGS KYLGTGRGYI
     HECKDQLSMM KGCCKEAYRL RKPEQAASVV RQAIVTATTA PAGPVSLEIP IDFQSAIIPQ
     SKIESVQVAC ATQAAPVIPA EVVDQLANSR RPVIWAGGGV ISAGASKELT KLAELTGAAV
     ITSQSGKGSI PEDHPQCIGH FAAYEAVKEL LKNADLLVSV GVRFRGNETV NWKVTAPEAH
     ISIDADLSAF NRNYEVTHGL LGEAKPILAA LNEALQAKSV APEAAYVEEV KSVREKVRAI
     LRETLGPYEA IVDGMRRVLP KDAILVRDVT VPANVWGSRL FEIYEPRTSI HASGGGIGQG
     LPTALGAQMG QQDRVVVLMA GDGGYMLNVG EMPVAVQENL PLIVLLFDDA GYGVLRNIQD
     AAYGRQVAVD LVSPDFVMLA KSMGYESNRV GSPEELVNEL EAAVARRKPT MIVVDMNAVG
     PMAKPFGGPP GAADAFKPKK L
//
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