ID   A0A2M8ISV2_9RHOB        Unreviewed;       167 AA.
AC   A0A2M8ISV2;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:PJE26464.1};
DE   Flags: Fragment;
GN   ORFNames=CVM52_26485 {ECO:0000313|EMBL:PJE26464.1};
OS   Pseudooceanicola lipolyticus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudooceanicola.
OX   NCBI_TaxID=2029104 {ECO:0000313|EMBL:PJE26464.1, ECO:0000313|Proteomes:UP000231553};
RN   [1] {ECO:0000313|EMBL:PJE26464.1, ECO:0000313|Proteomes:UP000231553}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=157 {ECO:0000313|EMBL:PJE26464.1,
RC   ECO:0000313|Proteomes:UP000231553};
RX   PubMed=29219804; DOI=10.1099/ijsem.0.002521;
RA   Huang M.-M., Guo L.-L., Wu Y.-H., Lai Q.-L., Shao Z.-Z., Wang C.-S., Wu M.,
RA   Xu X.-W.;
RT   "Pseudooceanicola lipolyticus sp. nov., a marine alphaproteobacterium,
RT   reclassification of Oceanicola flagellatus as Pseudooceanicola flagellatus
RT   comb. nov. and emended description of the genus Pseudooceanicola.";
RL   Int. J. Syst. Evol. Microbiol. 68:409-415(2018).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812}.
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:PJE26464.1}.
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DR   EMBL; PGTB01000442; PJE26464.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M8ISV2; -.
DR   Proteomes; UP000231553; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR045229; TPP_enz.
DR   PANTHER; PTHR18968:SF129; ACETOLACTATE SYNTHASE; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000231553}.
FT   DOMAIN          11..147
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PJE26464.1"
FT   NON_TER         167
FT                   /evidence="ECO:0000313|EMBL:PJE26464.1"
SQ   SEQUENCE   167 AA;  17652 MW;  1F9616E300E9D823 CRC64;
     SPVAPQGADL ARAKGWLAGA TRPLAIVGLD MLSGDSGCVL RAFLEHFAIP FITTYKAKGV
     IAEDHPLCLG GAGLSPLADG HLLPLVQQAD LILCIGYDPI EMRPGWREAW DPARQKVIDI
     APVQNDHYMH QAGLSFVADP GATLEALAQG AAARATWPEG EPRATRA
//