ID X4ZE62_9BACL Unreviewed; 564 AA.
AC X4ZE62;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:AHV95757.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:AHV95757.1};
GN ORFNames=PSAB_04105 {ECO:0000313|EMBL:AHV95757.1};
OS Paenibacillus sabinae T27.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1268072 {ECO:0000313|EMBL:AHV95757.1, ECO:0000313|Proteomes:UP000019772};
RN [1] {ECO:0000313|EMBL:AHV95757.1, ECO:0000313|Proteomes:UP000019772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T27 {ECO:0000313|EMBL:AHV95757.1,
RC ECO:0000313|Proteomes:UP000019772};
RX PubMed=24651173;
RA Xie J.B., Du Z., Bai L., Tian C., Zhang Y., Xie J.Y., Wang T., Liu X.,
RA Chen X., Cheng Q., Chen S., Li J.;
RT "Comparative Genomic Analysis of N2-Fixing and Non-N2-Fixing Paenibacillus
RT spp.: Organization, Evolution and Expression of the Nitrogen Fixation
RT Genes.";
RL PLoS Genet. 10:E1004231-E1004231(2014).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP004078; AHV95757.1; -; Genomic_DNA.
DR RefSeq; WP_025333331.1; NZ_CP004078.1.
DR AlphaFoldDB; X4ZE62; -.
DR STRING; 1268072.PSAB_04105; -.
DR KEGG; psab:PSAB_04105; -.
DR PATRIC; fig|1268072.3.peg.847; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_2_9; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000019772; Chromosome.
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:0034077; P:butanediol metabolic process; IEA:InterPro.
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; IPR012782; Acetolactate_synth_catblc.
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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR02418; acolac_catab; 1.
DR PANTHER; PTHR18968:SF129; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:AHV95757.1}.
FT DOMAIN 17..131
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 202..337
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 398..544
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 564 AA; 60918 MW; 27A82AEDA205526D CRC64;
MSAEAESTLS TAIAATNGAN LVVDSLISQG VRYIFGIPGA KIDAVFDVLR ERGPELIVCR
HEQNAAFMAA AVGRLTGKPG VCLVTSGPGA SNLVTGLATA NSESDPVVAL AGAVSRADRL
KHTHQSMDNA GLFKPVTKYS VEVEHPDNIA EAITNAFREA STAQPGAAFV SLPMDVLHGE
AAPFSFGPLN TPQLGTAPSV LIEAAADKLR NAKLPVILLG MKASSPEVTS AIRNLIRGTD
IPVVETFQAA GVISRDLEEH FMGRVGLFSN QPGDLLLKEA DAVLTIGYNP IEYDPYLWNR
EGVRQVYHLD NRHADFDQDY QPVIELIGNI ALTVEALTSH LASYHLPPES LSLLNGLRQK
LDQDGTGVRS PHAERVHPLD FILTLRKLID DQVTVTCDVG SHYIWMARYF RCYEPRRLLF
SNGMQTLGVA MPWAIAAALV RPGEKVVSIS GDGGFLFSSM ELETAVRLKL PLVHIVWSDG
SYNMVAFQQI GKYGRTSGVD FGSIDVVQYA ESFGAVGLRV NKPEQLEEVL RCALDQIGPV
VVDIPIDYRD SGKLGEKLLP DKAN
//
