ID A0A1T4SE24_9ACTN Unreviewed; 553 AA.
AC A0A1T4SE24;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SKA26138.1};
GN ORFNames=SAMN02745673_03389 {ECO:0000313|EMBL:SKA26138.1};
OS Marinactinospora thermotolerans DSM 45154.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Marinactinospora.
OX NCBI_TaxID=1122192 {ECO:0000313|EMBL:SKA26138.1, ECO:0000313|Proteomes:UP000190637};
RN [1] {ECO:0000313|EMBL:SKA26138.1, ECO:0000313|Proteomes:UP000190637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45154 {ECO:0000313|EMBL:SKA26138.1,
RC ECO:0000313|Proteomes:UP000190637};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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}.
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DR EMBL; FUWS01000009; SKA26138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4SE24; -.
DR STRING; 1122192.SAMN02745673_03389; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000190637; 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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000190637};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 15..128
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..330
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 391..538
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 553 AA; 57389 MW; 102B13312DA6A295 CRC64;
MSPSPSPGRL RGHGGTHAVD VALHHGVDTM FTLSGGHVFP LYDGAVKPEP RMRLLDVRHE
QTAVFAAEGI GKLTRRAGWA VLTAGPGVTN GVSGVTTAHF NGSPLVVLGG RAPDGRWGQG
LLQELDQPPL LAPVTKSART VHETAGIGAA VHEAFVLANT AHRGPVFLDI PMDRLYDQAE
VEAPASAPAP DRTPDPDAVA AAARLIGEAK RPLFVFGSDV WLDHAEQAAL EVAEELGVPV
ITNGQGRGVL PGGHPLLVTR ARGLAFGQAD LVVVVGTPLD FRIGHGLFGG RDGAPLAKVV
HIADSPGQIA AHLTLAASVA GDLSTILRGL GDTAAPGASV KAWRTQLAEA NAAAVAADAE
ALDSDADPIH PARVYGELNR LLADDAVVIG DGGDFVSYAG KYVEPARPGN WLDPGPFGCL
GTGMGYSIAA RLARPSSQVV TLLGDGAAGF SLMDVDTLVR HGLPVVMVCG NNGIWGLEKA
PMQMIYGYDV IAELAPQTRY DEVVRALGGG GELVTDPREI GPALRRAFDS GVPYLVNIAT
DPDNVYPRKT MGV
//
