ID A0A1A9A9P4_9ACTN Unreviewed; 540 AA.
AC A0A1A9A9P4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SBT52892.1};
GN ORFNames=GA0070611_5847 {ECO:0000313|EMBL:SBT52892.1};
OS Micromonospora auratinigra.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=261654 {ECO:0000313|EMBL:SBT52892.1, ECO:0000313|Proteomes:UP000199385};
RN [1] {ECO:0000313|Proteomes:UP000199385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44815 {ECO:0000313|Proteomes:UP000199385};
RA Varghese N.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT594323; SBT52892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A9A9P4; -.
DR STRING; 261654.GA0070611_5847; -.
DR PATRIC; fig|261654.4.peg.5919; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000199385; Chromosome i.
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; cd02004; TPP_BZL_OCoD_HPCL; 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:SF166; 2-HYDROXYACYL-COA LYASE 2; 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:UP000199385};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 9..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..316
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 378..525
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 540 AA; 56214 MW; 719442C869499827 CRC64;
MTERVEGHGG ELALAALRAH GVREMFTLSG GHVFPLYDAA HKAGFPLYDV RHEQSAVFAA
EAVAKLQRRP GLAVLTAGPG VTNGISGLTS AYFNASPVLV LGGRAPQFRW GSGSLQEMDH
LPLVAPVTKH AETVFSADDI PRAVAAALTT ALTPHRGPVF LDFPLEAVFS VGDAELPAAA
APAPIEPDPD EVTRAAALIA AASRPVIIAG SDVYAGDAVD ALRAAAESLQ VPVFTNGMGR
GALPPQHPLA FAKARRVALK GADVVVVIGT PLDFRLAFGD FGDAKVVHVV DAPSQRAGHV
QPAAAPAGDL RLILTAFADH PGDRAGHADW IVELRTAEDA AKARDAEEMA AETDPIRPAR
VYGELRRVLA PDAITIGDGG DFVSYAGKYL EPAQPGTWLD PGPYGCLGTG MGYAMGARVS
HPDRQICVLM GDGAAGFSLM DVESLARQGL PVVIVVGNNG IWGLEKHPMR AMYGYDVAAD
LQPGLRYDSV VEALGGAGET VAKAADLGPA LTRAFDAGVP YLVNVLTDPT DAYPRSSNLA
//
