ID A0A143QB24_9NOCA Unreviewed; 566 AA.
AC A0A143QB24;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN Name=xsc {ECO:0000313|EMBL:AMY20064.1};
GN ORFNames=A3Q40_02697 {ECO:0000313|EMBL:AMY20064.1};
OS Rhodococcus sp. PBTS 1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1653478 {ECO:0000313|EMBL:AMY20064.1, ECO:0000313|Proteomes:UP000076180};
RN [1] {ECO:0000313|EMBL:AMY20064.1, ECO:0000313|Proteomes:UP000076180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBTS 1 {ECO:0000313|EMBL:AMY20064.1,
RC ECO:0000313|Proteomes:UP000076180};
RX PubMed=27284129;
RA Stamler R.A., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.J.;
RT "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT Draft Sequences for Rhodococcus Isolates PBTS 1 and PBTS 2.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000076180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBTS 1 {ECO:0000313|Proteomes:UP000076180};
RA Stamer R., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.;
RT "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT Draft Sequences for Rhodococcus spp. Isolates PBTS 1 and PBTS 2.";
RL Submitted (APR-2016) 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, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP015219; AMY20064.1; -; Genomic_DNA.
DR RefSeq; WP_068102840.1; NZ_CP015219.1.
DR AlphaFoldDB; A0A143QB24; -.
DR STRING; 1653478.A3Q40_02697; -.
DR KEGG; rhu:A3Q40_02697; -.
DR PATRIC; fig|1653478.3.peg.2731; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000076180; Chromosome.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:RHEA.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050487; F:sulfoacetaldehyde acetyltransferase activity; IEA:UniProtKB-EC.
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; 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:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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 Acyltransferase {ECO:0000313|EMBL:AMY20064.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000076180};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:AMY20064.1}.
FT DOMAIN 20..123
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 204..332
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 397..547
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 566 AA; 58551 MW; B1E5E77DB1EEEECF CRC64;
MSTATTPATS AVKPAVSTAT VADVVAEVLT ELGVGHAFGV VGSGNFAVTN ALIARGVPFT
AARHEGGAAS MADGYSRFAA HPGVLTLHQG CGLTNAVTGI GEAAKSRTPM IVLTADVAAS
SRLSNFRIDQ DALALSVGAV PERVHSAETA VADVTRAWQT AVHGRRTVVV SLPLDVQAAP
APASTTVRRP VAPAPMRPAE SAVREFARLI AESERPVFVA GRGGRNAGAE IAALADHVGA
LVATSAVANG LFRGHEFDLG ISGGFSAPLT AELISNADLI VGWGCALNMW TMRHGSLIGA
DTAVVQIDDT AEALGAHRPV TLGIHGDCRT TAVDVLSAVG DTAQRYRTSD VSARLTESRW
WNDTPTEDLS TADTIDPRVF SAELDRLLPA ERLVAIDSGN FMGYPSTYLR VPDHHSFCFT
QAFQSIGLGL ASGLGAALTR PDRLPVIGTG DGGFLMGIAE LETAVRLGTP LVIAVYDDAA
YGAEVHHFAG PEHADDDVDL STVTFPDVDL AAVARGYGAT GVTVRTTADL AAVAAWLQSP
KGVLVIDAKI APDGGAWWLA EAFRGH
//
