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Database: UniProt
Entry: A0A221RA72_9MICC
LinkDB: A0A221RA72_9MICC
Original site: A0A221RA72_9MICC 
ID   A0A221RA72_9MICC        Unreviewed;       563 AA.
AC   A0A221RA72;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:ASN53866.1};
GN   ORFNames=CGQ25_03340 {ECO:0000313|EMBL:ASN53866.1};
OS   Sinomonas sp. R1AF57.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Sinomonas.
OX   NCBI_TaxID=2020377 {ECO:0000313|EMBL:ASN53866.1, ECO:0000313|Proteomes:UP000199767};
RN   [1] {ECO:0000313|EMBL:ASN53866.1, ECO:0000313|Proteomes:UP000199767}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R1AF57 {ECO:0000313|EMBL:ASN53866.1,
RC   ECO:0000313|Proteomes:UP000199767};
RA   Sastre D.E., Santos L., Kagohara E., Andrade L.H.;
RT   "Draft Genome Sequence of Sinomonas sp., Isolated from Brazilian Amazon
RT   Soils with Potential for Applications in Biocatalysis.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP022463; ASN53866.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A221RA72; -.
DR   Proteomes; UP000199767; Chromosome.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000199767};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          11..129
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          201..332
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          405..549
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   563 AA;  59829 MW;  7D5F3AE2E4FFB4D7 CRC64;
     MRQVGDRSVR NGGDLVVETL EALGAKTVFG IPGQHALGLF DAMGRGNLKF VSSRVENNSA
     FAADGYSRAT GEVGVLFLST GPGALTSLAG LQEAYATGVP MVVIASQIPL EGLGARRKGM
     LHQLDDQKAS AANVTKSQRL IQHASGIPSA IQDAWTDAIS SPQGPVWVEI PQNVLLEPIM
     VPPVEDALAV AADNPPRVEL VREAVRWLRE ARRPAVIAGG GTRRGHAEKA LLSFAERLRA
     PVICTPGGNG AFPWEHPLSL QSWIEDRHMT DLLEDADVLV VIGSSLGEVT SNYFTFEPRG
     RIIQIDAEPR VLESNRPGLG IRADAGQALD ALNAALDAAL PGALDGERPA PDWHGRSPEE
     VVADSLEAVR ARLASQDLGK ELRFMADIRA AVPDDMQTFW DMTISAYWAW SCWDARQGQF
     HSAQGAGGLG FGFPAAIGGA VGLATIGKPA RVLAVSGDGS AMYSISELAT ARQHNVPVTW
     LIVDDGGYGI LREYMVGAFG KATATELARP DFVALAESFG VPAKRVPVDR VREALEEGFA
     ADGPNVVVVE TLLKMFAPTH LEA
//
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