ID A0A0F5PBU3_9SPHN Unreviewed; 549 AA.
AC A0A0F5PBU3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KKC25109.1};
GN ORFNames=WP12_15620 {ECO:0000313|EMBL:KKC25109.1};
OS Sphingomonas sp. SRS2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=133190 {ECO:0000313|EMBL:KKC25109.1, ECO:0000313|Proteomes:UP000033680};
RN [1] {ECO:0000313|EMBL:KKC25109.1, ECO:0000313|Proteomes:UP000033680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRS2 {ECO:0000313|EMBL:KKC25109.1,
RC ECO:0000313|Proteomes:UP000033680};
RA Nielsen T.K., Sorensen S.R., Hansen L.H.;
RT "Draft genome sequence of isoproturon-mineralizing Sphingomonas sp. SRS2,
RT isolated from an agricultural field in the United Kingdom.";
RL Submitted (MAR-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:KKC25109.1}.
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DR EMBL; LARW01000104; KKC25109.1; -; Genomic_DNA.
DR RefSeq; WP_046194612.1; NZ_LARW01000104.1.
DR AlphaFoldDB; A0A0F5PBU3; -.
DR STRING; 133190.WP12_15620; -.
DR PATRIC; fig|133190.4.peg.142; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000033680; 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; 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; 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:UP000033680};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 189..321
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 381..527
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 549 AA; 60388 MW; 831053871BFE2547 CRC64;
MGTKASDLFI QCLEEEGCEY IFGVPGEENL DMLDSLSRSK TIKLILTRHE QGAGFMAATY
GRHTGKTGVC MATLGPGATN FVTAAAYAYL GGMPILMVTG QKPIKKSKQG RFQILDVVDM
MRPITKFTHQ LASADNIPSK VREAYRLAEE EKPGATHIEF PEDIADEHTD EVPLKPSLAR
RPTADTKAVR AAVKMIEEAK SPILVIGAGG NRKLTGRMLL QFVEKTGIPF VTTQLGKGVV
DETHPKFLGC AALSAGDFVH RSIEHADLIV NIGHDVIEKP PFFMKTGGTP VIHISTKTAE
VDPVYFPQVE VIGDIANAIW QMKEDIVPSG KWNFDFMFKA RKAEVEHTAS LDGDTRFPIF
PPHLVKEIRS AMPSDGIICL DNGVYKIWFA RNYNARQANT VLLDNALATM GAGLPSAMAS
AMVYPDRKVM AICGDGGFMM NSQEMETAVR LGLNITVLIL NDNSYGMIRW KQANMGFKDW
GLTYGNPDFV KYAEAYGAFG HRVESADHLT KLLKHCLDTP GVHLIDCPVD YSENDQILNK
DIKDLSKKV
//
