ID A0A0W1R6V2_9EURY Unreviewed; 563 AA.
AC A0A0W1R6V2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KTG09128.1};
GN ORFNames=AUR64_15130 {ECO:0000313|EMBL:KTG09128.1};
OS Haloprofundus marisrubri.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloprofundus.
OX NCBI_TaxID=1514971 {ECO:0000313|EMBL:KTG09128.1, ECO:0000313|Proteomes:UP000054387};
RN [1] {ECO:0000313|EMBL:KTG09128.1, ECO:0000313|Proteomes:UP000054387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB9 {ECO:0000313|EMBL:KTG09128.1,
RC ECO:0000313|Proteomes:UP000054387};
RA Zhang G., Stingl U., Rashid M.;
RT "Haloprofundus marisrubri gen. nov., sp. nov., an extremely halophilic
RT archaeon isolated from the Discovery deep brine-seawater interface in the
RT Red Sea.";
RL Submitted (DEC-2015) 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:KTG09128.1}.
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DR EMBL; LOPU01000029; KTG09128.1; -; Genomic_DNA.
DR RefSeq; WP_058582281.1; NZ_LOPU01000029.1.
DR AlphaFoldDB; A0A0W1R6V2; -.
DR STRING; 1514971.AUR64_15130; -.
DR OrthoDB; 6837at2157; -.
DR Proteomes; UP000054387; 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 GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR CDD; cd02002; TPP_BFDC; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 202..338
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 410..559
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 563 AA; 60410 MW; FC54544C20D561A0 CRC64;
MADSYTGADL FVDALEQYGI THLFGNPGTT ELPVMQALEG SDLDYVLGLH EDVAVGAAAG
YASTRRYHSH HDSSILPVGV VNLHVTPGLA HGLGNLYGAS VAGAPLVVTA GNHSTDFRHE
EPILSGDLRE LADQFCKWSD EVLDVAALPT MLRRAFRVAL TPPTGPVFLA LPLDVMMTET
DAEPERLGPI PDAGRGDPTQ LDRTAELLAE ADNPVLVVGD EVARAGTDAI DAVVEFAEAT
GARVHGEILS CEVNFPGDHP QWVSYVPPDE GLASTLMSTD TLIFAGISTH TTLTRHENPL
VPADATCIHL GPDAWELGKN HPADATVLGD LGHIAAELAE RVREGVSDGE REARLERVEM
MKQMAEERMR SLGEGEETDD PRASKAELVD AIRAAAPDAY IVDEGVTSKY AMLTRWPLAP
EQYISNKGGG LGYGLPASVG AALAESQRDD PRTVLGFVGD GSYLYYPQTL YTAARYDLDL
TVVVSDNRNY RILKDNTLGL FGGDEDDYEF VGMDFDPAVD IPKNAESHGA RGRLVDSPDD
IEAAVREAIS REGPDVLDVL VHD
//
