ID V6L0I2_9ACTN Unreviewed; 582 AA.
AC V6L0I2;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=N566_10135 {ECO:0000313|EMBL:EST37945.1};
OS Streptomycetaceae bacterium MP113-05.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae.
OX NCBI_TaxID=1380770 {ECO:0000313|EMBL:EST37945.1, ECO:0000313|Proteomes:UP000017915};
RN [1] {ECO:0000313|EMBL:EST37945.1, ECO:0000313|Proteomes:UP000017915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP113-05 {ECO:0000313|EMBL:EST37945.1,
RC ECO:0000313|Proteomes:UP000017915};
RA Valde M., Degnes K.F., Sletta H., Ruckert C., Kalinowski J., Zotchev S.B.;
RT "Streptomyces bacterium from a marine sponge: physiological
RT characterization and genome-based analysis of secondary metabolite
RT biosynthesis potential.";
RL Submitted (SEP-2013) 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:EST37945.1}.
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DR EMBL; AWQV01000311; EST37945.1; -; Genomic_DNA.
DR AlphaFoldDB; V6L0I2; -.
DR STRING; 1380770.N566_10135; -.
DR PATRIC; fig|1380770.3.peg.1781; -.
DR HOGENOM; CLU_013748_3_1_11; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000017915; 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:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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:UP000017915};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 216..315
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 397..544
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 582 AA; 59664 MW; C67D7397630DE994 CRC64;
MHSGGPRVAD YLVDSLAALG IEHVFGVGGA NIEDLYDAAH HSGRVTPVVA KHEFAAACMA
EGNHRTGGGP GVVMTTSGAG AMNLVPGVSE AYAARVPLIA LVGQPPRALD GRGAFQDSSG
RSGALDAAEL FGSISRFCAR VDNPGDTDEL LAAAVDATRG PRGGPAVLLL PKDVQQAPAE
GLRPLLDLLP ARDTPAAAQR GAAAALLTAE AAGGADIVLI AGDGVAHQGA RGELARLAGL
LDATVAVTPE GKDAFDNHDP RYIGVTGAIG HPTVLRGIEK AAVCVLVGTR LGVMARAGLD
LALADTPLVA FDPEPPFPEP REGGRPALHV DGDLGIELHA LNEELAALPG RSGKPRYASE
GPEYLMLPPA DTTGVRLVDA VRAIETAVPE DATVVSDAGN ASAAAIHYLP TPRRGNYVIA
MGMGGMGHSF GAGIGAAFAT GRRVYVLSGD GGFYAHGMEL HTAVEYGLPV TFVIFDNSAH
GMCVTREQLF YDGSYSYNSF KPADITAGAR AMFPSLTAVE ATTAEQLRDT LLSTNATAGP
ALVGVRCDPD DMPPFTPFLQ LLDSRSTHTS GAPHVHPAAP VG
//
