ID A0A151BN12_9ARCH Unreviewed; 559 AA.
AC A0A151BN12;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KYH41052.1};
GN ORFNames=AYL31_005260 {ECO:0000313|EMBL:KYH41052.1};
OS Candidatus Bathyarchaeota archaeon B26-1.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1779370 {ECO:0000313|EMBL:KYH41052.1, ECO:0000313|Proteomes:UP000075365};
RN [1] {ECO:0000313|EMBL:KYH41052.1, ECO:0000313|Proteomes:UP000075365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B26-1 {ECO:0000313|EMBL:KYH41052.1};
RA He Y., Li M., Perumal V., Feng X., Fang J., Xie J., Sievert S., Wang F.;
RT "Evidence for homoacetogenesis among multiple lineages of the archaeal
RT phylum Bathyarchaeota widespread in marine sediments.";
RL Submitted (FEB-2016) 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:KYH41052.1}.
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DR EMBL; LUCD01000036; KYH41052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151BN12; -.
DR STRING; 1779370.AYL31_005260; -.
DR Proteomes; UP000075365; 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; 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:SF129; ACETOLACTATE SYNTHASE; 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 7..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 391..538
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 559 AA; 62387 MW; 3C564A5AF9FFCC67 CRC64;
MGIRLPNGAE VLIECILNEG INLISGVPGE QVLGVLNAIY DVQYDLEFIL MKDERNASFF
ADAHYRLTGR PGVCLSTLGP GATNLLTGLA NAYLDRSAVI ALTGQASTEE MVKESHQKIP
VSKIFAPVTK WSFTVGRADL IPEAVRKAFK TSKSGRPGPV HLELPSDVMA ELCDVEPLNP
LLYEPKYPPG GNLEVIKKAL NYIMEAEFPV VLVGNGVIRD EASENLRMFI EKFHLPVVST
FMAKGAVPED HPLHLGILGA FSWDVARRAV GRADVVVAVG YDFAELPAEY WNRDCKRLVV
HIDRIAAEID KYYPVRYEVV GNINRTLQFM LNFRVDEPEA KRLRRLREIE EFKRDFLDQL
YPTEETRPLK PSDIVKVLNE AVSDETVVTV DVGDHKVWMS RCLVRRKPRK YLVSNGLSAM
GFSLPAAISA KTIFRDSPVL CTVGDGGFAM SFGELETMRR LKLAIPIIIF DNDVLGQVYT
RQRIAYGDRI IGVSFSNPDF VKISEAFGMD GFKVETLGEL REAVELGFKN DRATIIDVKV
DVEETLRMIK RLGPLRSVP
//
