ID A0A0N1NIK0_9ACTN Unreviewed; 627 AA.
AC A0A0N1NIK0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KPI11825.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:KPI11825.1};
GN ORFNames=OK006_4146 {ECO:0000313|EMBL:KPI11825.1};
OS Actinobacteria bacterium OK006.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPI11825.1, ECO:0000313|Proteomes:UP000037912};
RN [1] {ECO:0000313|EMBL:KPI11825.1, ECO:0000313|Proteomes:UP000037912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK006 {ECO:0000313|EMBL:KPI11825.1,
RC ECO:0000313|Proteomes:UP000037912};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four Actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KPI11825.1}.
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DR EMBL; LJCU01000154; KPI11825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1NIK0; -.
DR PATRIC; fig|1592326.3.peg.5119; -.
DR Proteomes; UP000037912; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
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 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:KPI11825.1}.
FT DOMAIN 8..126
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 221..354
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 420..577
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 627 AA; 67796 MW; AFF0334ED7C798C9 CRC64;
MTSTTRLTVA QALVRFLAAQ YTERDGERRR LIGATWGIFG HGNVAGLGQA LIEYADEMPY
HQGRNEQSMV HAAVGFARQS NRLSAHAVTT SIGPGATNLV TGAALATINH LPVLLLPGDI
FATRPADPVL QQLEVPYAGD VSVNDCLRPV SKYFDRVTRP EALIPAALQA MRVLTDPVET
GAVTLALPQD VQAEAYDWPE EFFQERIWTV RRPAADASEL AAAVTAIREA RRPLIVAGGG
VHHSRAEDVL AELAATTRIP VASTQAGKGS LKWDHPQDVG GVGHTGTATA NELARTADLV
IGVGTRYTDF TTASGTLFTA SNVRFLNLNI APYDGHKLSG IPLIADARAG LEALTEALLL
HGHRVEPAYA TEYTDDKERW EYRVDAAYEA EDIDIRPTQP QVLGVLDELV TEDDILINAA
GSLPGDLHKL WRARSRDQYH VEYGYSCMGY EIPAAIGVRM AAPDRPVWAL VGDGTYLMMP
TEIVTAVQEG VAIKVLILQN HGYASIGGLS ESVGAERYGT AYRYRSEDRT YTGAPLPVDL
AANAASLGMR VLRAKTVRDL RAALAEARAA DTPTCVYVET ETADTVSGAP PAQAWWDVPV
AETATRSSAV KAREEYDRHV AARRRHL
//
