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Database: UniProt
Entry: A0A011MXF9_9PROT
LinkDB: A0A011MXF9_9PROT
Original site: A0A011MXF9_9PROT 
ID   A0A011MXF9_9PROT        Unreviewed;       600 AA.
AC   A0A011MXF9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Acetolactate synthase isozyme 2 large subunit {ECO:0000313|EMBL:EXI67256.1};
DE            EC=2.2.1.6 {ECO:0000313|EMBL:EXI67256.1};
GN   Name=ilvG {ECO:0000313|EMBL:EXI67256.1};
GN   ORFNames=AW08_02091 {ECO:0000313|EMBL:EXI67256.1};
OS   Candidatus Accumulibacter adjunctus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=1454001 {ECO:0000313|EMBL:EXI67256.1, ECO:0000313|Proteomes:UP000020218};
RN   [1] {ECO:0000313|EMBL:EXI67256.1, ECO:0000313|Proteomes:UP000020218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-12 {ECO:0000313|Proteomes:UP000020218};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) 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:EXI67256.1}.
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DR   EMBL; JFAX01000011; EXI67256.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A011MXF9; -.
DR   STRING; 1454001.AW08_02091; -.
DR   PATRIC; fig|1454001.3.peg.2136; -.
DR   Proteomes; UP000020218; 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   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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:UP000020218};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000313|EMBL:EXI67256.1}.
FT   DOMAIN          3..107
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          202..335
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          411..555
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   600 AA;  65418 MW;  69ADE0402EF8C70D CRC64;
     MTTVAIYLAQ RLSADGPRHV FLVSGGGAMF LNDALCHQVG LTPIFFQHEQ AAAMAAEACA
     RISSTPPIVN LTTGPGGINA INGVFGAWTD SIPMIILSGQ VKRATCLATM RVPGLRQLGD
     QESDIVSMVR GITKYAALIE NPEDTAWHLD QALHLATSGR PGPVWLDVPI DVQSAPIDPT
     GLRRFVPAAI AEERHPATQA TAIVDRLRSS RRPVILAGSG VRAARATTEF ATVIRRLGVP
     VTTAWTHDLI ATDDPLFCGR PGTIGTRAGN FTVQNADLLL ILGSRLNIRQ VSYNWQAFAP
     RAFKIQVDID PAELAKPVVR PDLAICCDLR GFLAQMNARL AQQPLPPNPE HDRWLAWCRQ
     RLIDYPVVLP KHREFNGRIN PYHFIEALFD RLGEDDIVAC GNATATIVPF QAAALKQGQR
     LFSNSGSASM GYDLPAAIGA WFGALAARGQ QRRIICLAGD GSIMMNLQEL QTIVQHRLPI
     KIFVLDNRGY LSIRTSQANF FGRLAGADPD SGVTLPDFVA VARAFGISAS RLDTADFAQR
     LPAILETSEP HLCQVVLDET QQFEPRTSSR RLPDGQIVSA PLEDMFPFLE RDELARNMID
//
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