ID A0A263CXW6_9PSEU Unreviewed; 586 AA.
AC A0A263CXW6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:OZM70994.1};
GN ORFNames=CFN78_22895 {ECO:0000313|EMBL:OZM70994.1};
OS Amycolatopsis antarctica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1854586 {ECO:0000313|EMBL:OZM70994.1, ECO:0000313|Proteomes:UP000242444};
RN [1] {ECO:0000313|EMBL:OZM70994.1, ECO:0000313|Proteomes:UP000242444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU-G6 {ECO:0000313|EMBL:OZM70994.1,
RC ECO:0000313|Proteomes:UP000242444};
RA Wang J., Leiva S., Huang J., Huang Y.;
RT "Amycolatopsis antarcticus sp. nov., isolated from the surface of an
RT Antarcticus brown macroalga.";
RL Submitted (JUL-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:OZM70994.1}.
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DR EMBL; NKYE01000016; OZM70994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A263CXW6; -.
DR InParanoid; A0A263CXW6; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000242444; 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:UP000242444};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..114
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 201..334
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 399..519
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 356..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 61345 MW; C2C9752705874A8E CRC64;
MRLADALVAT LRDWDTRYVF GVSGANIEHV HDAIHRLGAG RLESVLARRE DGAAFMADAR
ARVHRTLGVC CSTSGGGMMN LAVGLAESYA ESVPVLALIG QPPSSMDGRG AFQDSSGIGR
TVDAAGMLAA FTKYVARPGV ATFWDDLRAA VHAALTGRPG PVALLLPRDV QDSDIGPAPD
GFPSSLTDFL DRPAVPEDEV RALFDVVRSA RRPVLLVGHG VRRGGDPGAV TRFAQAAGVP
TATTMSARAE FPNEDPLFLG VAGLPGHPSA HEAIRDADLV VVAGAGLNAM TRGPLGELPG
GQVAVVNIDP GEAQRSVAPR LVVRADAGAV FERLLEMTRA EPFAVPENAA RPRRRFVPRL
AEPVPGRENP GNDGDDLRQS EAVEVLRDYL PAGGHLVLDA GNCASAAIHL SDVPPGASST
IALGMGGMGY SLPAAVGAQL GSDPGTRTVV LCGDGAFLMN GLELHTAVEL GLPVLFVVFN
NAMHGMCVTR QQVLFDSRLE AVKYAPVDVT GVARGLGTPD RLWVGGAGTL TELRERLADY
HQRHLAGPGV LELRLAIEEV PPFTTLLPAD EPTAVVERVA VHGACR
//
