ID A0A1B1MKW0_STRLN Unreviewed; 560 AA.
AC A0A1B1MKW0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:QMV10818.1};
DE SubName: Full=TPP-requiring enzyme {ECO:0000313|EMBL:ANS69236.1};
GN ORFNames=GJU35_37505 {ECO:0000313|EMBL:QMV10818.1}, SLCG_7000
GN {ECO:0000313|EMBL:AXG58155.1}, SLINC_7012
GN {ECO:0000313|EMBL:ANS69236.1};
OS Streptomyces lincolnensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1915 {ECO:0000313|EMBL:ANS69236.1, ECO:0000313|Proteomes:UP000092598};
RN [1] {ECO:0000313|EMBL:ANS69236.1, ECO:0000313|Proteomes:UP000092598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2936 {ECO:0000313|EMBL:ANS69236.1,
RC ECO:0000313|Proteomes:UP000092598};
RA Meng S.C.;
RT "Enhancement of antibiotic productionsby engineered nitrateutilization in
RT actinobacteria.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AXG58155.1, ECO:0000313|Proteomes:UP000253884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC-G {ECO:0000313|EMBL:AXG58155.1,
RC ECO:0000313|Proteomes:UP000253884};
RX PubMed=29574602; DOI=10.1007/s10295-018-2029-1;
RA Xu Y., Tan G., Ke M., Li J., Tang Y., Meng S., Niu J., Wang Y., Liu R.,
RA Wu H., Bai L., Zhang L., Zhang B.;
RT "Enhanced lincomycin production by co-overexpression of metK1 and metK2 in
RT Streptomyces lincolnensis.";
RL J. Ind. Microbiol. Biotechnol. 45:345-355(2018).
RN [3] {ECO:0000313|EMBL:QMV10818.1, ECO:0000313|Proteomes:UP000515335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B48 {ECO:0000313|EMBL:QMV10818.1,
RC ECO:0000313|Proteomes:UP000515335};
RX PubMed=32322696;
RA Wang R., Kong F., Wu H., Hou B., Kang Y., Cao Y., Duan S., Ye J., Zhang H.;
RT "Complete genome sequence of high-yield strain S. lincolnensis B48 and
RT identification of crucial mutations contributing to lincomycin
RT overproduction.";
RL Synth Syst Biotechnol 5:37-48(2020).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP016438; ANS69236.1; -; Genomic_DNA.
DR EMBL; CP022744; AXG58155.1; -; Genomic_DNA.
DR EMBL; CP046024; QMV10818.1; -; Genomic_DNA.
DR RefSeq; WP_067442797.1; NZ_CP046024.1.
DR AlphaFoldDB; A0A1B1MKW0; -.
DR STRING; 1915.SLINC_7012; -.
DR KEGG; sls:SLINC_7012; -.
DR PATRIC; fig|1915.4.peg.7724; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000092598; Chromosome.
DR Proteomes; UP000253884; Chromosome.
DR Proteomes; UP000515335; 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; cd02004; TPP_BZL_OCoD_HPCL; 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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF166; 2-HYDROXYACYL-COA LYASE 2; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000092598};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 10..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 200..325
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 393..542
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 560 AA; 60077 MW; 513ECA414BD1F9A7 CRC64;
MPDDTQDVIS GGHLVAKALK AEGVDRIYTL CGGHIIDIYD GCVDEGIEVV DVRHEQVAAH
AADGYARITG KPGCAVVTAG PGTTDAVTGV ANAFRAESPM LLIGGQGALT QHKMGSLQDL
PHVDMMTPIT KFAAAVPDTA RAADMVSMAF RECYHGAPGP SFLEIPRDVL DAKVPVAKAR
VPEPGAYRAS TRSAGDPEAI EKLADLLVHA EKPAILLGSQ VWTTRGTESA IDLVRTLNIP
AYMNGAGRGT LPPGDPHHFQ LSRRYAFSNA DVIVIVGTPF DFRMGYGKRL SPDATVVQID
LDYRTVGKNR DIDLGIVGDA GLVLKSVTEA ASGRVNGGAS RRKEWLDELR AAEQTAIEKR
LPSLKSDASP IHPYRLVSEI NEFLTEDSIY IGDGGDIVTF SGQVVQPKSP GHWMDPGPLG
TLGVGVPFVL AAKQARPDKE VVALFGDGAF SLTGWDFETL VRYDLPFVGI VGNNSSMNQI
RYGQKAKYGE ERERVGNTLG DVHYDKFAQM LGGYGEEVRD PADIGPALRR ARESGKPSLI
NVWVDPDAYA PGTMNQTMYK
//
