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
//