ID A0A1E3L9D3_9BACL Unreviewed; 591 AA.
AC A0A1E3L9D3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:ODP29570.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:ODP29570.1};
GN Name=ilvB {ECO:0000313|EMBL:ODP29570.1};
GN ORFNames=PTI45_01053 {ECO:0000313|EMBL:ODP29570.1};
OS Paenibacillus nuruki.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1886670 {ECO:0000313|EMBL:ODP29570.1, ECO:0000313|Proteomes:UP000094578};
RN [1] {ECO:0000313|EMBL:ODP29570.1, ECO:0000313|Proteomes:UP000094578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TI45-13ar {ECO:0000313|EMBL:ODP29570.1,
RC ECO:0000313|Proteomes:UP000094578};
RA Kim S.-J.;
RT "Genome sequencing of Paenibacillus sp. TI45-13ar, isolated from Korean
RT traditional nuruk.";
RL Submitted (AUG-2016) 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:ODP29570.1}.
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DR EMBL; MDER01000030; ODP29570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3L9D3; -.
DR STRING; 1886670.PTI45_01053; -.
DR PATRIC; fig|1886670.3.peg.1075; -.
DR Proteomes; UP000094578; 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 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:UP000094578};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:ODP29570.1}.
FT DOMAIN 3..111
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..334
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 396..546
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 591 AA; 65757 MW; 948D1B9AB34F8054 CRC64;
MKMRVADYIT NALYEAGGKN VFLVTGGMIM HLTDALYQHP EQTYTCCHHE QAVAMAAEAY
GRYTGELGVA YVTAGPGALN TITGVAGAYI DSSPSIVVAG NSKVSLAKIK GPRQFPLQGF
DSLPIFEKIT KYAVMLDDLA QVKYEVQKCI HIAKTNRVGP VYLEVPVDIQ GATFDPDLYE
DYIPKEVSVQ YSISDQQIKE VIESLKSAKR PCLLIGAGVR LSKGMQSVFD FLEKTGIPII
TSRLGMDLID HDHPLFVGRP GTYGDRASNF TIQNCDVFIN VGCRLGIGLV GYDYQEFAQD
AKKIIVDVDD NELSKPSIIP DIRIQEDAKL FFDKINIALQ DVTFNFSDWV QQTQLWKTKY
PVDLPEYLDE TEGINSYHFM TKFSEKAKSD TSFVVDTGSC FHVHAQAFKV KWGQRHIITG
GLSTMGYTPA SVGVSMAKDR GEVYCVTGDG SFQMNLQELQ TISHNKLPIK FILFNNNGYL
LIRHTQINHM EGRMIGESAE SGLGFASFDK VADTFGLAYM KISNLTDMDT QIKQLIDYQG
PMICEITTPT NQLLIPRVAS QKLADGSMKS MAYDDMYPFL SREEYAENCL K
//
