ID A0A2S8ZSL6_9MICO Unreviewed; 532 AA.
AC A0A2S8ZSL6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:PRB04232.1};
GN ORFNames=CQ047_16860 {ECO:0000313|EMBL:PRB04232.1};
OS Microbacterium sp. MYb72.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1848693 {ECO:0000313|EMBL:PRB04232.1, ECO:0000313|Proteomes:UP000238041};
RN [1] {ECO:0000313|EMBL:PRB04232.1, ECO:0000313|Proteomes:UP000238041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MYb72 {ECO:0000313|EMBL:PRB04232.1,
RC ECO:0000313|Proteomes:UP000238041};
RA Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA Kaleta C., Schulenburg H.;
RT "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL Submitted (SEP-2017) 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:PRB04232.1}.
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DR EMBL; PCOT01000039; PRB04232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8ZSL6; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000238041; 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 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; 2-KETOARGININE DECARBOXYLASE ARUI-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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 8..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 387..527
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 532 AA; 55082 MW; 29A819E297A93295 CRC64;
MTDQYADTAG RAVLETIRGY GVTAVFGIPG THNLELYRPL ADLGIRAVTN RHEQGSGYGA
DGWAQQTGLP GVVITTSGPG LQNAMSAIGT AFCESRPLLV LSPGVPLGSE FADVGTLHET
KDATAMVGAI AEWSRRVTTA AEAVDAVHDA FALFRTGRPR PVHIEIPLDV LEAPAGVPEA
HRLPRPAPSP HSGDPAGVAE AARLLADART PVIVAGGGST DAAAGVTALA ERLGAPVLTT
LNGKGVVDER HPLSLGSNLR LAAARAVAED ADVLLVVGSK LGEAELWAPR LEARGAVVRI
DISVAQLDKN LAATVGIAGD AAAVVDALLA HLPSGDRPPR DLAVERAAID TEMRDTAPET
VALAEIIAEA LPDDAIVAGD SSQIVYMALG SVLRSQHPHS LLYTPTYATL GYGLPAAIGA
RVADDSRPAV TVIGDGALMF CVNELVTAVE QRVDVTVVCV DNGGYAEIRQ NELDRGMTPI
GVDLVQPDWA ALATAFGATG RRVERREDIA ASIRDAIADG GVQLVHIPQN AL
//
