ID A0A011Q6M2_9PROT Unreviewed; 424 AA.
AC A0A011Q6M2;
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 1 large subunit {ECO:0000313|EMBL:EXI74309.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:EXI74309.1};
GN Name=ilvB_2 {ECO:0000313|EMBL:EXI74309.1};
GN ORFNames=AW07_01851 {ECO:0000313|EMBL:EXI74309.1};
OS Candidatus Accumulibacter sp. SK-11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1454000 {ECO:0000313|EMBL:EXI74309.1, ECO:0000313|Proteomes:UP000020226};
RN [1] {ECO:0000313|EMBL:EXI74309.1, ECO:0000313|Proteomes:UP000020226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-11 {ECO:0000313|Proteomes:UP000020226};
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}.
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:EXI74309.1}.
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DR EMBL; JFAW01000011; EXI74309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A011Q6M2; -.
DR STRING; 1454000.AW07_01851; -.
DR PATRIC; fig|1454000.3.peg.1553; -.
DR Proteomes; UP000020226; 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 CDD; cd00568; TPP_enzymes; 1.
DR Gene3D; 3.40.50.970; -; 1.
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; 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 SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000020226};
KW Transferase {ECO:0000313|EMBL:EXI74309.1}.
FT DOMAIN 25..159
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 235..379
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 424 AA; 47052 MW; 6341055387DD0F97 CRC64;
MEPASMRRFL PPHGPDHRAS GVELDALIER LHQARRPVII AGTGIRAAHA SKEFATLIRR
LGIPVTTAWT HDLIASDNPL FCGRPGTIGT RAGNFTVQNA DLLLILGSRL NIRQVSYNWQ
AFAPRAFKIQ VDIDPAELAK PTVRPDLAIC CDLRDFLAQM NARLARQPLP PNPEHDRWLA
WCRQRLIDYP VVLPKHREFN GRINPYHFIE ALFERLTEDD IIACGNATAT IVPFQAAALK
QGQRLFSNSG SASMGYDLPA AIGAWFGALA ARGSQRRIIC LAGDGSIMMN LQELQTIAQH
RLPIKIFVLD NRGYLSIRTS QANFFGRLAG ADPDSGVTLP DFVAVARAFG IRASRLDSGD
FAQRLPAILE TSEPHLCQVV LDETQQFEPR TSSRRLPGGQ IVSAPLEDMY PFLERDELAR
NMID
//