ID A0A0F5N0U1_9MYCO Unreviewed; 519 AA.
AC A0A0F5N0U1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN ORFNames=WR43_04240 {ECO:0000313|EMBL:KKC00674.1};
OS Mycolicibacter arupensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacter.
OX NCBI_TaxID=342002 {ECO:0000313|EMBL:KKC00674.1, ECO:0000313|Proteomes:UP000034416};
RN [1] {ECO:0000313|Proteomes:UP000034416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GUC1 {ECO:0000313|Proteomes:UP000034416};
RA Greninger A.L., Cunningham G., Chiu C.Y., Miller S.;
RT "Genome sequence of Mycobacterium arupense GUC1.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2;
CC Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000673};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004974}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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:KKC00674.1}.
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DR EMBL; LASW01000009; KKC00674.1; -; Genomic_DNA.
DR RefSeq; WP_046188348.1; NZ_MVHH01000021.1.
DR AlphaFoldDB; A0A0F5N0U1; -.
DR STRING; 342002.BST15_11745; -.
DR PATRIC; fig|342002.3.peg.951; -.
DR OrthoDB; 2443624at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000034416; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02002; TPP_BFDC; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF86; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVX-RELATED; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 3..107
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 376..512
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 519 AA; 52962 MW; 507EBA6F23F13568 CRC64;
MTNGAQALIA TLVDSGVQVC FANPGTSEMH FVAALDSVPQ MRGVLCLFEG VVTGAADGYA
RVAEKPAATL LHLGPGLGNG LANLHNARRA HVPMVNVIGD HATYHKKYDA PLESDIEPLT
DWTHGWSRRT GAGGDVGRDA AEAVAASMAS PAVVANLILP ADISWEDGAQ AAGPVDPVPA
AAPDPQAVAE VAAVLGSGEP VALLIGGPAV ADVRAMEAAD RIAAATGARA LVETFPARLV
RGAGVPAIDR LGYLAEQAAF QLDGIRHLVV AGTRSPVSFF AYPGKPSDLV PEGCVVHNLA
GLETDVVAAL EQLAEAVAAG VQPRPAPAAV PELPSGQLTP QNWVQVVGAL LPENAIISDE
ANTSGLMLPA ATAGAPRHDV LTLTGGAIGQ GLPVALGAAV AAPDRPVIAL QADGSAAYTI
SALWTMAREN LNVTTVLINN SAYAILRLEL ARVGAEGGGP KANDLLDLSR PNMDFAKIAE
GFGVPATVAT TCEELAEQFS RAIAEPGPHL IDARIPTLF
//
