ID A0A0W1E3P3_9SPHN Unreviewed; 548 AA.
AC A0A0W1E3P3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KTE24946.1};
GN ORFNames=ATE62_22385 {ECO:0000313|EMBL:KTE24946.1};
OS Sphingopyxis sp. HIX.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1759074 {ECO:0000313|EMBL:KTE24946.1, ECO:0000313|Proteomes:UP000053691};
RN [1] {ECO:0000313|Proteomes:UP000053691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIX {ECO:0000313|Proteomes:UP000053691};
RA Gomez-Alvarez V., Revetta R.P.;
RL Submitted (NOV-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:KTE24946.1}.
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DR EMBL; LNSB01000079; KTE24946.1; -; Genomic_DNA.
DR RefSeq; WP_058810559.1; NZ_LNSB01000079.1.
DR AlphaFoldDB; A0A0W1E3P3; -.
DR STRING; 1759074.ATE62_22385; -.
DR Proteomes; UP000053691; 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; 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.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 188..320
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 380..526
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 161..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 60304 MW; 3B805FFD2B49FF2D CRC64;
MKKASDLFIE CLEEEGVEYI FGVPGEENLD FLDSLSRSTK IKLILTRHEQ GAGFMAATYG
RHTGKTGVCL ATLGPGATNF VTAAAYAQLG GMPMMMITGQ KPIKKSKQGR FQILDVCSMM
SPITKFTHQM ASSDNIPSRV REAFRLAEEE KPGAVHIELP EDIADEHTDS TPLKRSHSRR
PNADVKSIRE AVKALEEATS PILVIGAGAN RTMTSRMLLQ FIEKTGIPFL TTQLGKGVID
ERHPKFLGCA ALSAGDFVHR AVEASDCIVN LGHDVIEKPP FFMKQGGPKV IHISSKTAEV
DPVYFPDVEV IGDIANAVWQ MKEDIVPNGG WKFDHMLAYR KAEVEHTAPL AADARFPIFP
PHLVQSIRDS MPDDGIICLD NGVYKIWFAR GYTAYRPNTV LLDNALATMG AGLPSAMMSA
MVYPGRKVMA ICGDGGFMMN SQEMETAVRL GLNLTVLILN DSSYGMIRWK QANMGFKDWG
LTYGNPDFVK YAESYGAHGH RVESAAHLKE LLAHTRDTPG VHLIDCPVDY SENDQILNID
IKKLSKEL
//
