ID A0A0G3ITS1_9MYCO Unreviewed; 656 AA.
AC A0A0G3ITS1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-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=AB431_20415 {ECO:0000313|EMBL:AKK28646.1};
OS Mycobacterium sp. EPa45.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1545728 {ECO:0000313|EMBL:AKK28646.1, ECO:0000313|Proteomes:UP000035237};
RN [1] {ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|Proteomes:UP000035237};
RA Kato H., Ogawa N., Ohtsubo Y., Ohshima K., Toyoda A., Yamazoe A., Mori H.,
RA Maruyama F., Nagata Y., Hattori M., Fujiyama A., Kurokawa K., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45, Isolated from a Phenanthrene-Degrading Consortium.";
RL Genome Announc.0:0-0(2015).
RN [2] {ECO:0000313|EMBL:AKK28646.1, ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|EMBL:AKK28646.1,
RC ECO:0000313|Proteomes:UP000035237};
RX PubMed=26184940;
RA Kato H., Ogawa N., Ohtsubo Y., Oshima K., Toyoda A., Mori H., Nagata Y.,
RA Kurokawa K., Hattori M., Fujiyama A., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45 (NBRC 110737), Isolated from a Phenanthrene-Degrading
RT Consortium.";
RL Genome Announc. 3:e00782-15(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; CP011773; AKK28646.1; -; Genomic_DNA.
DR RefSeq; WP_047331465.1; NZ_CP011773.1.
DR AlphaFoldDB; A0A0G3ITS1; -.
DR STRING; 1545728.AB431_20415; -.
DR KEGG; mye:AB431_20415; -.
DR PATRIC; fig|1545728.4.peg.4157; -.
DR OrthoDB; 3194735at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000035237; Chromosome.
DR GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0019310; P:inositol 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; cd02003; TPP_IolD; 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; IPR030817; Myo_inos_IolD.
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; TIGR04377; myo_inos_iolD; 1.
DR PANTHER; PTHR18968:SF9; 3D-(3,5_4)-TRIHYDROXYCYCLOHEXANE-1,2-DIONE HYDROLASE; 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 Hydrolase {ECO:0000313|EMBL:AKK28646.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 22..158
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 245..379
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 443..601
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 656 AA; 70150 MW; 69BA20C2B4F22CEC CRC64;
MVSTAPKSTG KLADTEGTVR LTVAQATIRF LSNQYVERDG VRRKFFAGCF GIFGHGNVAG
LGQALLQDEI ESAESKPRRQ PGLKYVLGRN EQAMVHTAVA YARQKDRLEA WAVTASVGPG
STNMLTGAAL ATINRLPVLL LPADTFATRV SSPVLQELEL PSSGDVTVND AFKPLSRYFD
RVWRPEQLPA ALLGAMRVLT DPVETGAATV SIPQDVQAQA HDWPESLFAE RIWHVARPLP
ERSVITRAAE IIAGASNPLI IAGGGVHYSE AEHALAAFCE QTGIPVAESQ AGKGSLRFDH
PQSVGAVGST GTTAANELAA EADVVIGIGT RYSDFTSASR TAFNNPDVRF VNINVASLDS
VKQGGISVVS DAREAIEALG PALEGHTVSD EYRSRVAELA AEWDDTVSSV YATSDDDAAL
NQNQVIGLVN TLSDPRDVVV CAAGSMPGDL HKLWRTRDRK GYHVEYGYSC MGYEIAGGIG
VRMADDDRDV FIMVGDGSYL MMATELVTAV QEGVKVIAVL VQNHGFASIG GLSESLGSQR
FGTAYRYRSD DGRLDGDKLP VDLAANAASL GAGVIKVSTA AEFADAVKVA KASEHTTVIH
VETDPLIHAP DSQSWWDVPV SEVSTLESTQ TAYQRYADWK KVQRPLVKPS VNPSER
//
