ID A0A1R4HW71_9MICO Unreviewed; 544 AA.
AC A0A1R4HW71;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:SJN11785.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:SJN11785.1};
GN ORFNames=FM113_13050 {ECO:0000313|EMBL:SJN11785.1};
OS Leucobacter sp. 7(1).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1255613 {ECO:0000313|EMBL:SJN11785.1, ECO:0000313|Proteomes:UP000195513};
RN [1] {ECO:0000313|EMBL:SJN11785.1, ECO:0000313|Proteomes:UP000195513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7(1) {ECO:0000313|Proteomes:UP000195513};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUID01000067; SJN11785.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4HW71; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000195513; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
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:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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:UP000195513};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:SJN11785.1}.
FT DOMAIN 6..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 191..322
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 384..529
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 544 AA; 57436 MW; F7D27AA55CBF507A CRC64;
MTYSRSAGHL IVETLASHGV ERVYSVPGES FLDVLDGLHD SPITNVVCRQ EGGVGFMALA
EGRLTGRPGV AMVTRGPGAA NFFIAAHCAY QDATPLVCFI GLVPIADRRR ESFQEFSIDS
WFGSTAKRVL TIENADQAGA IVAEAMHVAA SGRPGPVIVG LPEDLLRELT DAAAPAPRAI
AAPAPSRTDL AALRDRIAAA ERPFLLVGGD SFVGETGREL ADWALANHIP VAADWRNYDA
VPNTHAAYIG WPGYGRRDSI VDALREADLF IGVGAVRSDV MSEGYTVGLD TETVLISTDA
QLLQHAGRVD QLITATPAGF VSELAELGDV RGERTGERVT ALRASQERFT AVTEHAPVTT
GVDLELVFAE LEQQLGDERV LTYGAGNATI WGHRQLTHNV PNSLVGSRNG AMGMAVPAAV
AAALVFPERH AVAVCGDGDF LMNGQEVATL VAQGGRALFV VVDNGKYATI VEHQERWYPG
RPSGTGMANP DFAAWMESFG GRGARLESND GIAETVAELL AHDGPALLHL VIDPSTPSPS
GAGL
//
