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
//