ID A0A0N9HZ78_9PSEU Unreviewed; 536 AA.
AC A0A0N9HZ78;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:ALG11006.1};
GN ORFNames=AOZ06_32660 {ECO:0000313|EMBL:ALG11006.1};
OS Kibdelosporangium phytohabitans.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kibdelosporangium.
OX NCBI_TaxID=860235 {ECO:0000313|EMBL:ALG11006.1, ECO:0000313|Proteomes:UP000063699};
RN [1] {ECO:0000313|EMBL:ALG11006.1, ECO:0000313|Proteomes:UP000063699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLBMP1111 {ECO:0000313|EMBL:ALG11006.1,
RC ECO:0000313|Proteomes:UP000063699};
RA Qin S., Xing K.;
RT "Genome sequencing of Kibdelosporangium phytohabitans.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP012752; ALG11006.1; -; Genomic_DNA.
DR RefSeq; WP_054292908.1; NZ_CP012752.1.
DR AlphaFoldDB; A0A0N9HZ78; -.
DR STRING; 860235.AOZ06_32660; -.
DR KEGG; kphy:AOZ06_32660; -.
DR OrthoDB; 3203527at2; -.
DR Proteomes; UP000063699; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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:UP000063699};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..102
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 185..308
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 371..514
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 536 AA; 55588 MW; 403032D2120861B1 CRC64;
MKVSEAVGRT LAELGVAQAF GVIGSGNFTV TNALRAYGVP FVATRHEAGA ATMADAYSRM
SGRVALVSVH QGCGLTNAMT GIAEAAKSRT PMIVLTADTP GSAVLANFRI DQDAAVTALG
ATSERVHSAE TAVADTIRAY RTAVHERRTV VLNLPLDVQD AEATQTPVGA VEPPLPVRPN
HESAEALAAM IGEASRPVFL AGRGARGAAP QIRELARKTG ALLTTTAVAH GLFNDDPWAL
GISGGFASPL AVDLITDADL VVGWGCAFTK WTTRRGKLIS GKVAHVDIGG TAHRPVDLAV
HGDAGQTAAD VTALVTAREG YRTPSVEARI AAGPGWPTPD LSTGTHIDPR ELSARLDDLL
PRARVVAVDS GNFMGYPSGY LSVPDEFGFC FTQAFQSIGL GLFTAIGAAL AQPDRLPVAA
VGDGGFMMGI ADLETAVRLR LPLVVVVYND SAYGAEIHHF GPDADLSTVT FPDPGIARIA
EGFGCSAVTV RTGDDLAGVT AWLAGPRDRP LVVDARIASD GGSWWLAEAF GQVAES
//
