ID A0A0N0TDR2_9ACTN Unreviewed; 555 AA.
AC A0A0N0TDR2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KOV94428.1};
GN ORFNames=ADL04_25025 {ECO:0000313|EMBL:KOV94428.1};
OS Streptomyces sp. NRRL B-3648.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519493 {ECO:0000313|EMBL:KOV94428.1, ECO:0000313|Proteomes:UP000037702};
RN [1] {ECO:0000313|EMBL:KOV94428.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-3648 {ECO:0000313|EMBL:KOV94428.1};
RA Noorani M.;
RL Submitted (JUL-2015) 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:KOV94428.1}.
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DR EMBL; LGDZ01000197; KOV94428.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0TDR2; -.
DR PATRIC; fig|1519493.3.peg.5304; -.
DR Proteomes; UP000037702; 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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000037702};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 21..139
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 214..342
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 401..541
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 555 AA; 57779 MW; FEAF6EBDF471027F CRC64;
MVLRPTTAQI TAALNPPPGR NGGDLVVETL AGLGATTVFG LPGQHALGMF DALRRSALRY
VGLRVENNAG FAADAYGRIT GEAAPLLLST GPGALTSLAA LQEAAAASAP VLAISSQVPT
AGLGGGRHGY LHELPDQAAS FRGVVKSVHT VRTPSQIPSA IAAAWKSALT APHGPVWVEI
PQDVLLAQTS LPVVTAMDAT PDELLPRPEL TAVAADLLSR AARPAIIAGG GVVRADASGK
LLRLAERLQA PVVTTFGGKG AFPWNHPLSM QSWLEDRHTT DFLEDADVLL VVGSGLGELS
SNYHTFRPRG RVVQIEADLG KLESNHPALG IHADARPALQ ALLETVEERT DASAPERVRE
LLAKVADRIA GQELTLEQDV LASVRRALPA GSPSFWDMTI LAYWAWSAFD AQGPNTMHSA
QGAGGLGYGF PAALGAAAAD PTRPVLAVSG DGGALYSIAE LATARQYGLP VTWLIVDDGG
YGILREYMTD AFGQATATEL TRPDYVSLAE SFGVPAVRTT PETLAEDLAK ALSAPGPSVV
VLPAVLRMFA PTHLG
//
