ID A0A0M2S314_9ACTN Unreviewed; 540 AA.
AC A0A0M2S314;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=LQ51_00225 {ECO:0000313|EMBL:KKK07862.1};
OS Micromonospora sp. HK10.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1538294 {ECO:0000313|EMBL:KKK07862.1, ECO:0000313|Proteomes:UP000034330};
RN [1] {ECO:0000313|EMBL:KKK07862.1, ECO:0000313|Proteomes:UP000034330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK10 {ECO:0000313|EMBL:KKK07862.1,
RC ECO:0000313|Proteomes:UP000034330};
RA Talukdar M., Das D., Borah C., Deka Boruah H.P., Bora T.C., Singh A.K.;
RT "Draft genome sequence of Micromonospora HK10, isolated from Kaziranga
RT National park, Assam, India.";
RL Submitted (NOV-2014) 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 -!- 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:KKK07862.1}.
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DR EMBL; JTGL01000002; KKK07862.1; -; Genomic_DNA.
DR RefSeq; WP_046564579.1; NZ_KQ058771.1.
DR AlphaFoldDB; A0A0M2S314; -.
DR STRING; 1538294.LQ51_00225; -.
DR PATRIC; fig|1538294.3.peg.2175; -.
DR HOGENOM; CLU_013748_3_3_11; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000034330; Unassembled WGS sequence.
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 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 193..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; 56430 MW; AC7CB14625333B46 CRC64;
MTERVEGHGG ELALAALRAH GVREMFTLSG GHVFPLYDAA HRTGFPIYDV RHEQSAVFAA
EAVAKLQRRP GLAVLTAGPG VTNGVSGLTS AYFNASPVLV LGGRAPQFRW GSGSLQEMDH
LPLVAPVTKH AETVFGADDI PRAVSAALTT ALTPHRGPVF LDFPLEAVFS VGDAELPAVT
PVTPIEADPE EVSTAARLIA AASRPVIIAG SDVYAGDAVD ALRAAAESLQ VPVFTNGMGR
GALPPEHPLA FAKARRVALK GADLVVVIGT PLDFRLAFGD FGDARVVHVV DAPSQRAGHV
TPAAAPAGDL RLILTAFAEH PGDRADHAGW IAELRTAEDA AKARDAEAMA ADSDPIRPAR
VYGELRKVLA PDAITIGDGG DFVSYAGKYL EPAQPGTWLD PGPYGCLGTG LGYAMGARVS
HPDRQICVLM GDGAAGFSLM DVESLARQRL PVVIVVGNNG IWGLEKHPMR AMYGYDVAAD
LQPGLRYDRV VEALGGAGET VEKAADLGPA LTRAFDAGVP YLVNVLTDPA DAYPRSSNLA
//
