ID A0A1P8WXB1_9SPHN Unreviewed; 610 AA.
AC A0A1P8WXB1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:APZ98684.1};
GN ORFNames=BWQ93_09390 {ECO:0000313|EMBL:APZ98684.1};
OS Sphingopyxis sp. QXT-31.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1357916 {ECO:0000313|EMBL:APZ98684.1, ECO:0000313|Proteomes:UP000188055};
RN [1] {ECO:0000313|EMBL:APZ98684.1, ECO:0000313|Proteomes:UP000188055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QXT-31 {ECO:0000313|EMBL:APZ98684.1,
RC ECO:0000313|Proteomes:UP000188055};
RA Liang J.S.;
RT "Microbe-microbe interactions indirectly alter the fate of arsenic in
RT presence of MnII.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP019449; APZ98684.1; -; Genomic_DNA.
DR RefSeq; WP_077030312.1; NZ_CP019449.1.
DR AlphaFoldDB; A0A1P8WXB1; -.
DR STRING; 1357916.BWQ93_09390; -.
DR KEGG; sphq:BWQ93_09390; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000188055; Chromosome.
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:SF142; 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:UP000188055};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 8..130
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 209..345
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 409..559
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 610 AA; 65922 MW; B6680CEBC21BE6B0 CRC64;
MEKMSQIKLS DWVAQYLADR GIADVFMLTG GGAMHLNHSL GTHPALTTTF THHEQALSMA
AEAYYRLTNR VAVVNVTSGP GGTNAITGVY GAYVDSIGML VISGQVKTET TVRHTGLPLR
QYGDQELDIE ELVRPITKYV TMVTDPRSIR YHLEKALYLA TNGRPGPVWL DIPLDVQAAK
IDPEDLLAGF DPAELDEPWK RADLDVVAAE ILERIAKAER PVVFAGSGVR LSGAHAEFLT
LIERLGVPVV TGWNAHDALR TDHPLNCGKP GTVGDRGGNM VTQSADLLLV LGSRLNIRQV
SYNWKSFARE AYKIWVDIDP VELAKPTVVP DMPVTADLAD LIPALLAQPY AGPSDAQREW
LGWARGRVAA FPAVLPEYRG HDVLVHPYVA MDELFAQLGE DDIVVTGNGS ACVVGFQAAQ
LKHGQRLWTN SGCATMGYDL PAAIGVCAAT RGERRVIAIA GDGSIMMNLQ EMQTIAGYNL
PVKVILINNS GYVSIFQTQR NFFNGQEVGG GPKSNVTFPD FSKIATAFGF AYTRATNHAE
LGDAIAATLA ADGPAFCEIM VDEHVGFAPK LGAKQHADGR ITSPALEDLS PFLPREELAA
NMRIALMDEA
//
