ID A0A1X6YLT0_9RHOB Unreviewed; 555 AA.
AC A0A1X6YLT0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:SLN25043.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:SLN25043.1};
GN Name=alsS {ECO:0000313|EMBL:SLN25043.1};
GN ORFNames=ROA7450_01035 {ECO:0000313|EMBL:SLN25043.1};
OS Roseovarius albus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1247867 {ECO:0000313|EMBL:SLN25043.1, ECO:0000313|Proteomes:UP000193061};
RN [1] {ECO:0000313|EMBL:SLN25043.1, ECO:0000313|Proteomes:UP000193061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7450 {ECO:0000313|EMBL:SLN25043.1,
RC ECO:0000313|Proteomes:UP000193061};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-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; FWFX01000002; SLN25043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6YLT0; -.
DR Proteomes; UP000193061; 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 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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000193061};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SLN25043.1}.
FT DOMAIN 22..136
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 208..339
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 398..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 555 AA; 59086 MW; 43A8E7928A880296 CRC64;
MPNLCQAIPV AQTWVYEMTQ KRAADLLAER LYQAGCRHAF GMPGGEVLTL VDALEQAGIK
FTLVKHENAA GFMAEAVWQR TGAPGIVVAT IGPGAMNAVN AVANAMQERV PLIMLSGCVD
ADEAQQYTHQ VMDHSAVFAP ITKATFTLST ASAGLITDKA LGIALEGRPG PVFIDVPISV
ADANVSNAIT PHRAPAGATA PAHGVDLDRA RGWLAKARKP VMIVGVDAMN ERAEEALLQF
ANHHNVPFVT TYKAKGIIAE DHPLCLGGAG LSPLADKHLL PFIQSADLIL CAGYDPIEMR
TGWQNIWDPA QVNVIDISAE PNHHYMHQAT LNFTCDTATG LNTLSDGIAP VQTWTAGEVS
AVKDALSKAF DTSEDWGPAA VIAECQRHLP ANTTATADSG AHRILLSQIW KCSEPRSLLQ
SSALCTMGCA VPLAIGASIV EPERISVSFS GDAGFLMIAG ELASAAELEL KTIFVVFVDR
SLALIELKQR QRQMVNRGVD FAHHDFAAIG RAFGGQGHRV TSRVELAEAL KAAQQADTFT
VIAAEIERGA YDGRI
//
