ID A0A0N1NNB9_9ACTN Unreviewed; 517 AA.
AC A0A0N1NNB9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KPI19073.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:KPI19073.1};
GN ORFNames=OK074_1537 {ECO:0000313|EMBL:KPI19073.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI19073.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI19073.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI19073.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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:KPI19073.1}.
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DR EMBL; LJCV01000055; KPI19073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1NNB9; -.
DR PATRIC; fig|1592327.3.peg.1753; -.
DR OrthoDB; 2443624at2; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02002; TPP_BFDC; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF86; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVX-RELATED; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000037991};
KW Transferase {ECO:0000313|EMBL:KPI19073.1}.
FT DOMAIN 1..103
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 376..510
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 517 AA; 52110 MW; C4BF461C5393EDDB CRC64;
MNGAHAVAST LLDSGVEVCF ANPGTSELHF VAALDDVPTL RAVPCLFEGV ATGAADGYGR
MAGRPAATLL HLGPGLGNGL ANLHNPRRAA TPVVNLVGDH ATFHKKYDAP LESDVDALAR
TVSGWVRRCE DPATVGGDVA AAVAAASGAP GQVATVILPA DVSWSDGARP APPVAFRAPA
AVSGQTVATV AAALRTGEPA ALLLGGAATR EPALRAAARI AAATGARLLC ETFPARLERG
AGLPVVERLG YLAEGAMAQL DGVRHLVLVG ARTPVAFFAH PGLPGPLAPD DCRIHTLATA
ADDIPAALGE LADTVAADTP AVLRAAGRPT PPTGALTAES AAAAVGALLP EGAIVVDEAN
TSGLWLPGAT AGAPRHDWLA LTGGAIGQGL PLAAGAALAC PDRPVLCLEA DGSAMYTVSA
LWTHAREGLD ITTVIFANGS YAVLTMESQR LGSPAAGPAR HDLLDLTRPG LDFVALARGM
GVPASRATTA EEFTAQLRRA FDEPGPHLVE AVVPALF
//
