ID A0A0D5AEL8_9NOCA Unreviewed; 599 AA.
AC A0A0D5AEL8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN ORFNames=NY08_3494 {ECO:0000313|EMBL:AJW41504.1};
OS Rhodococcus sp. B7740.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1564114 {ECO:0000313|EMBL:AJW41504.1, ECO:0000313|Proteomes:UP000032410};
RN [1] {ECO:0000313|EMBL:AJW41504.1, ECO:0000313|Proteomes:UP000032410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7740 {ECO:0000313|EMBL:AJW41504.1};
RX PubMed=25931596;
RA Zhang D., Li L., Zhu S., Zhang N., Yang J., Ma X., Chen J.;
RT "Complete Genome Sequence of Rhodococcus sp. B7740, a Carotenoid-Producing
RT Bacterium Isolated from the Arctic Sea.";
RL Genome Announc. 3:0-0(2015).
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; CP010797; AJW41504.1; -; Genomic_DNA.
DR RefSeq; WP_045197582.1; NZ_CP010797.1.
DR AlphaFoldDB; A0A0D5AEL8; -.
DR STRING; 1564114.NY08_3494; -.
DR KEGG; rhb:NY08_3494; -.
DR PATRIC; fig|1564114.4.peg.3448; -.
DR HOGENOM; CLU_013748_3_1_11; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000032410; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0009028; F:tartronate-semialdehyde synthase activity; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0009436; P:glyoxylate catabolic process; 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; 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; IPR006397; Glyox_carbo_lig.
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 NCBIfam; TIGR01504; glyox_carbo_lig; 1.
DR PANTHER; PTHR18968:SF14; GLYOXYLATE CARBOLIGASE; 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 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 Ligase {ECO:0000313|EMBL:AJW41504.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 393..561
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 599 AA; 64550 MW; 974223DC862DD5DE CRC64;
MPRMRAADAA VKILELENAT TAFGLPGAAI NPFYAAMRDH GGIRHVLARH VEGASHMAEG
FTRAAPGNIG ICIGTSGPAG TDMITGLYSA MADSIPILAI TGQAPVARLH KEDFQAVDIA
AIAAPVTKMA MTVLEPAQVP GAFAQAFHLM RSGRPGPVLI DLPIDVQLAE IDFDPETYQS
LPVHKPVASR AQAEKAIDML LAAERPLIVA GGGIINADAS DLLVQLAEIL DVPVIPTLMG
WGTIPDDHRL AAGMVGLQTA HRYGNATLLA SDFVLGIGNR WANRHTGGLD TYRKGRKFVH
VDIEPTQIGR VFAPDYGIIS DAKAALEQFV AVAEERRAAG TVRDLSGWVE DCATRKRTMH
RRTHFDNVPI KPQRVYEEMN KVFDRDTRYV STIGLSQIAG GQFLHVYSPR NWINCGQAGP
LGWTIPAALG AVAADPKANV VALSGDYDFQ FMIEELAVGA QFNLPYVHVV VNNSYLGLIR
QAQRAFDMDF CVQLGFDNIN TQESQDTQPG IPKGYGVDHV RVAEGLGCKA LRVTDPDLIG
ETLVRARTLA NEHKVPVVVE IILERVTNIS MGTEIDNVGE FEELATTSSD APTALLLLD
//
