ID A0A1V4A1B8_9ACTN Unreviewed; 561 AA.
AC A0A1V4A1B8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:OON72535.1};
GN ORFNames=B1H18_29555 {ECO:0000313|EMBL:OON72535.1};
OS Streptomyces tsukubensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=83656 {ECO:0000313|EMBL:OON72535.1, ECO:0000313|Proteomes:UP000190539};
RN [1] {ECO:0000313|EMBL:OON72535.1, ECO:0000313|Proteomes:UP000190539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F601 {ECO:0000313|EMBL:OON72535.1,
RC ECO:0000313|Proteomes:UP000190539};
RA Zong G., Zhong C., Fu J., Qin R., Cao G.;
RT "Draft Genome Sequence of Streptomyces tsukubaensis F601, a Producer of the
RT immunosuppressant tacrolimus FK506.";
RL Submitted (FEB-2017) 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:OON72535.1}.
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DR EMBL; MVFC01000037; OON72535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4A1B8; -.
DR STRING; 83656.B1H18_29555; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000190539; 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:UP000190539};
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"
SQ SEQUENCE 561 AA; 58900 MW; 22A460408EC3476F CRC64;
MTHDHDLELR PTAAQTAEAL SPPPGRTGGD LVVETLRGLG STTVFGLPGQ HALGMFDALR
RSDLTYVGLR VENNAGFAAD AYGRITGEAA PLLLSTGPGA LTSLAALQEA AAGSSPVLAI
GSQVPAAGLG GGRHGYLHEL RDQEASFRGV VKSTHPVRTA SQIPSAIAAA WESALTAPHG
PVWVEIPEDV LLAETVLPVV TAMDADPHDL VPRPELTAVA AHLLAEAERP AVIAGGGVVR
ADAAGKLRAL AERLDLPVVT TFGGKGAFPW EHPLSLQSWI EDRHTTDFLE DADVLLVVGS
GLGELSSNYH TFAPRGRIIQ IEADAGKLES NHPALGIHAD ARLALTALLE TVPEREDPKA
PERVRRVLDL VRERVDSQHL NLEQELLASV RAALPDTAPS FWDMTILAYW AWSAFDARRP
GTMHSAQGAG GLGYAFPAAL GAAVADPTGP VLAVSGDGGA MYSLAELATA AQYGLPVTWL
IVDDGGYGIL REYMKDTFGE ATGTELTRPD FVALAESFGV TAIRSTPESL KDDLTKALAE
PGPSVVVLPA HLRMFAPTHL G
//
