ID A0A0G3AGC0_9ACTN Unreviewed; 562 AA.
AC A0A0G3AGC0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:AKJ13026.1};
GN ORFNames=ABB07_24215 {ECO:0000313|EMBL:AKJ13026.1};
OS Streptomyces incarnatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ13026.1, ECO:0000313|Proteomes:UP000035366};
RN [1] {ECO:0000313|EMBL:AKJ13026.1, ECO:0000313|Proteomes:UP000035366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366};
RX PubMed=26159526;
RA Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K.,
RA Tamura T.;
RT "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces
RT the Nucleoside Antibiotic Sinefungin.";
RL Genome Announc. 3:e00715-e00715(2015).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP011497; AKJ13026.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3AGC0; -.
DR STRING; 665007.ABB07_24215; -.
DR PATRIC; fig|665007.5.peg.5146; -.
DR Proteomes; UP000035366; 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; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 27..145
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 220..348
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 407..547
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 562 AA; 58772 MW; F6906A7FB336171A CRC64;
MTHDHDLVLR PTETQISAAL NPPPGRNGGD LVVETLAGLG ATTVFGLPGQ HALGMFDALR
RSALRYVGLR VENNAGFAAD AYGRITGEAA PLLLSTGPGA LTSLAALQEA AAASAPVLAI
SSQVPTAGLG GGRHGYLHEL PDQAASFRGV VKSVHTVRTQ SQIPSAIAAA WKSALTAPHG
PVWVEIPQDV LLAETALPVV TAPDATPEDL APRPELTAVA AHLLSRAARP AIIAGGGVVR
SDASGKLRAL AEKLNAPVVT TFGGKGAFPW EHPLSLQSWL EDRHTTDFLE DADVLLVVGS
GLGELSSNYH TFKPRGRVVQ IEADLGKLES NHPALGIHAD ARLALQALLE TVEERADDSA
PERVRELLEK VASRIAAQEL TLEQQVLGAV RRALPDASPS FWDMTILAYW AWSAFDPRGT
NLMHSAQGAG GLGYGFPAAL GAAAADPARP VLAVSGDGGA LYSIAELATA RQYGLPVTWL
IVDDGGYGIL REYMTDAFGQ ATATELTRPD YVALAESFGV PGVRTTPETL EEDLAKALAL
PGPSVVVLPA VLRMFAPTHR TA
//
