ID A0A2W2DI15_9ACTN Unreviewed; 534 AA.
AC A0A2W2DI15;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:PZF92443.1};
DE Flags: Fragment;
GN ORFNames=C1I93_19395 {ECO:0000313|EMBL:PZF92443.1};
OS Micromonospora endophytica.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=515350 {ECO:0000313|EMBL:PZF92443.1, ECO:0000313|Proteomes:UP000248627};
RN [1] {ECO:0000313|EMBL:PZF92443.1, ECO:0000313|Proteomes:UP000248627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45430 {ECO:0000313|EMBL:PZF92443.1,
RC ECO:0000313|Proteomes:UP000248627};
RA Sahin N., Ay H., Saygin H.;
RT "Draft genome sequence of Jishengella endophytica.";
RL Submitted (JAN-2018) 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:PZF92443.1}.
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; POTX01000141; PZF92443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W2DI15; -.
DR Proteomes; UP000248627; 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 192..317
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"
FT NON_TER 534
FT /evidence="ECO:0000313|EMBL:PZF92443.1"
SQ SEQUENCE 534 AA; 55945 MW; B58D86D3E6E73911 CRC64;
MTERIEGHGG DLALAALRAY GVREMFTLSG GHVFPLYDAA HKADFPLYDV RHEQSAVFAA
EAVAKLQRRP GLAVLTAGPG VTNGISGLTS AYFNASPVLV LGGRAPQFRW GSGSLQEMDH
LPLVAPVTKH AETVFAADDI PRAVAAALET ALTPHRGPVF LDFPLEAIFS TGDADAPAGP
TLAPIEADPD EVATAARLIA GAARPVIVAG SDVYAGDAVD ALRAAAEALT VPVFTNGMGR
GALPPEHPLA FAKARRVALS GADVVVVVGT PLDFRLSFGD FGDATVVHIV DAPSQRASHL
QPAVSPAGDL RAILTALAEH PGDRVDHGDW VAQLRTAEDA AKARDAEEMA AETDPIRPAR
IYGELRKVLA RDAVTIGDGG DFVSYAGRYL EPAEPGTWLD PGPYGCLGTG MGYAMGARVT
HPDRQICVLM GDGAAGFSLM DVESLVRQKL PVVIVVGNNG IWGLEKHPMR AMYGYDVAAD
LQPELRYDQV VTALGGAGET VAKPTDLAPA LQRAFTAGVP YLLNVLTDPT DAYP
//
