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
//