ID K0V9M2_MYCVA Unreviewed; 518 AA.
AC K0V9M2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN ORFNames=MVAC_05902 {ECO:0000313|EMBL:EJZ11553.1};
OS Mycolicibacterium vaccae ATCC 25954.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1194972 {ECO:0000313|EMBL:EJZ11553.1, ECO:0000313|Proteomes:UP000006072};
RN [1] {ECO:0000313|EMBL:EJZ11553.1, ECO:0000313|Proteomes:UP000006072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25954 {ECO:0000313|EMBL:EJZ11553.1,
RC ECO:0000313|Proteomes:UP000006072};
RX PubMed=23105074; DOI=10.1128/JB.01462-12;
RA Ho Y.S., Adroub S.A., Abadi M., Al Alwan B., Alkhateeb R., Gao G.,
RA Ragab A., Ali S., van Soolingen D., Bitter W., Pain A., Abdallah A.M.;
RT "Complete Genome Sequence of Mycobacterium vaccae Type Strain ATCC 25954.";
RL J. Bacteriol. 194:6339-6340(2012).
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}.
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:EJZ11553.1}.
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DR EMBL; ALQA01000008; EJZ11553.1; -; Genomic_DNA.
DR AlphaFoldDB; K0V9M2; -.
DR PATRIC; fig|1194972.3.peg.1196; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_11; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000006072; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; 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: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:SF167; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVB2-RELATED; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 2..105
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 180..311
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 371..507
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 518 AA; 53650 MW; 1A4C1D6DBAF944F9 CRC64;
MLGVSHVFGI PGQNALALFD AIRRSDLTFV SSRVENNSAF GADGYARATG EVGVLFLSTG
PGALTALGAL QEAYATGVPL LVIVSQVPRA GMGLRRGMLH QLDDQRRSAV NVTKSTAIAR
HPSQIPSLLA DAWSLAQSAP AGPVWVEIPQ DLLQEPVDVP PVTSVATSVT RRRPRVELVS
AAGALLDSAE RPVILAGGGV RRSAGGPAAL VSIAERLDAP VVSTVGGKGA IPFGHPLSAA
SWIEDRHTTA LLEDADVLLA VGTAMGEVTS NYFTLAPKGR VIHIDAEARV LEANHPALGI
HADAAAALTA LAGQVTPRTG DGPAVAAMLR TAVQDRLAGQ DVAAELTLMS DLRAAVPVAA
QTFWDMTIAG YWAWSAWDPR DGEFHSAQGA GGLGFAFPAA VAAAIGTGQR TFAVTGDGGA
MYGIAELATA RQHDADVTWL IVDDGGYGIL REYMTDTFGQ ATATELDRPD FVALAQSFGV
PAQRVSLEGV GEAIADTFTT RGPAVVVLPA LLRMFAPT
//