ID A0A1C6NR80_9ACTN Unreviewed; 551 AA.
AC A0A1C6NR80;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SCK33596.1};
GN ORFNames=H180DRAFT_02726 {ECO:0000313|EMBL:SCK33596.1};
OS Streptomyces sp. WMMB 322.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1286821 {ECO:0000313|EMBL:SCK33596.1, ECO:0000313|Proteomes:UP000182082};
RN [1] {ECO:0000313|EMBL:SCK33596.1, ECO:0000313|Proteomes:UP000182082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMMB 322 {ECO:0000313|EMBL:SCK33596.1,
RC ECO:0000313|Proteomes:UP000182082};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; FMHI01000007; SCK33596.1; -; Genomic_DNA.
DR RefSeq; WP_055486323.1; NZ_FMHI01000007.1.
DR AlphaFoldDB; A0A1C6NR80; -.
DR STRING; 1286821.GCA_001418285_02714; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000182082; 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 9..127
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 205..335
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 396..534
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 551 AA; 56894 MW; E85AEB4A7923C784 CRC64;
MASAPAVRTG SDLVTESLTA LGAHTVFGLP GQHALGAFDA VRRSGLPYVG LRVENNAGFA
ADAYARITGT VTPLLISTGP GALMSLAALQ ESAAASAPVL GISSQVPTAG LGGGRKGYLH
ELRDQKASFR DIVKSVHTVR AASQIPTVLA SAWAEAAEAP CGPTWVEIPQ DVLVAPTDVP
PPESLAAPGG PAHPRPLPAR PELTARAAAL LDAAERPAVL AGGGVVRAGA RAQLLGLAER
LDAPVATTFG GKGAFPCEHR LSLGSWLEDR HTTDFLAAAD VLLVVGSGLG ELSSNYHTFA
PRGRVIHIEA DVGKLEANHP ALGIHADARA ALEALTAAVA PRPAGRAERE VAALLDRVRD
RIAAQGLDLE QQVLGAVREA LPDTSPSFWD MTILAYWAWS AFDPREGAMH SAQGAGGLGY
GFPAALGAAA ADPERRTPVL AVSGDGGAMY SIAELATARQ YGLPVTWLIV DDGGYGILRS
YMTEAFGEAT GTELARPDFV ALAESFGVPA VRSSPERLRE DLSAALASPG PSVVLLPAEL
RMFAPTHLDA H
//
