ID F3NEP9_9ACTN Unreviewed; 623 AA.
AC F3NEP9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:EGG48033.1};
GN ORFNames=SGM_1613 {ECO:0000313|EMBL:EGG48033.1};
OS Streptomyces griseoaurantiacus M045.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=996637 {ECO:0000313|EMBL:EGG48033.1, ECO:0000313|Proteomes:UP000003022};
RN [1] {ECO:0000313|EMBL:EGG48033.1, ECO:0000313|Proteomes:UP000003022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M045 {ECO:0000313|EMBL:EGG48033.1,
RC ECO:0000313|Proteomes:UP000003022};
RX PubMed=21551298; DOI=10.1128/JB.05053-11;
RA Li F., Jiang P., Zheng H., Wang S., Zhao G., Qin S., Liu Z.;
RT "Draft genome sequence of the marine bacterium Streptomyces
RT griseoaurantiacus M045, which produces novel manumycin-type antibiotics
RT with a pABA core component.";
RL J. Bacteriol. 193:3417-3418(2011).
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:EGG48033.1}.
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DR EMBL; AEYX01000027; EGG48033.1; -; Genomic_DNA.
DR RefSeq; WP_006139218.1; NZ_AEYX01000027.1.
DR AlphaFoldDB; F3NEP9; -.
DR STRING; 996637.SGM_1613; -.
DR eggNOG; COG3962; Bacteria.
DR Proteomes; UP000003022; Unassembled WGS sequence.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000003022};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 10..126
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 223..356
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 419..576
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 623 AA; 66616 MW; 831BEB9DCA4F302F CRC64;
MSPSPRVRLT VAQALVRFLS AQYTERDGAR HRLIAGTWGV FGHGNVAGVG QALLEYADAM
PYHQGRNEQA MVHAAVGYAR QLNRLSAQAV TTSIGPGATN LVTGAALATI NRLPVLLLPG
DHFATRPADP LLQQLEHPSG ADITVNDALR PVSRFFDRIT RPEALLASAL QAMRVLTDPA
ETGAVTLALP QDVQAEAYDW PEEFFAERVW HVRRPEPDPA ELAEAVRLLR GARRPLLVAG
GGVHHSEAEE ALKALVDVTG IPVASTQAGK GSLRHDHPAD LGGIGHTGTA VADALAREAD
LVLGVGTRYS DFTTASGTLF QHPDVRFVNL NITAFDAHKL AARPLLADAR SGLTALTAAL
ADHRVDAAYE AEYRAGKERW ERVVAAAFDA EDDAVPTQTQ VLGALDAVVG DTDVVINAAG
SLPGDLHKLW RARSPRQYHL EYGYSCMGYE IPAAVGVQQA APEVVVWSLV GDGTYLMMPT
EIVTAVQEGL PVNLVLLQNH GYASIGGLSE ETGGERFGTA YRYRAADGSF TGDPLPVDLA
ANAASLGMDV LRAKTVRELR EALTAARASD RPTCVYVETD PAATAPPAEA WWDVPVAAVS
GREAALAARE RYDRRVTARR HHL
//