ID A0A135VC11_9ARCH Unreviewed; 405 AA.
AC A0A135VC11;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:KXH70207.1};
DE Flags: Fragment;
GN ORFNames=AM324_10050 {ECO:0000313|EMBL:KXH70207.1};
OS Candidatus Thorarchaeota archaeon SMTZ1-83.
OC Archaea; Asgard group; Candidatus Thorarchaeota.
OX NCBI_TaxID=1706445 {ECO:0000313|EMBL:KXH70207.1, ECO:0000313|Proteomes:UP000070043};
RN [1] {ECO:0000313|EMBL:KXH70207.1, ECO:0000313|Proteomes:UP000070043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMTZ1-83 {ECO:0000313|EMBL:KXH70207.1};
RX PubMed=26824177;
RA Seitz K.W., Lazar C.S., Hinrichs K.U., Teske A.P., Baker B.J.;
RT "Genomic reconstruction of a novel, deeply branched sediment archaeal
RT phylum with pathways for acetogenesis and sulfur reduction.";
RL ISME J. 0:0-0(2016).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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:KXH70207.1}.
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DR EMBL; LRSK01000255; KXH70207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135VC11; -.
DR Proteomes; UP000070043; Unassembled WGS sequence.
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 PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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); 1.
PE 3: Inferred from homology;
FT DOMAIN 4..123
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 200..334
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT NON_TER 405
FT /evidence="ECO:0000313|EMBL:KXH70207.1"
SQ SEQUENCE 405 AA; 43817 MW; 7A5133AFC9B2E6D8 CRC64;
MSMMTGGEVL ARCLIQEGVK YVFGIPGDQL YPLLDSIHTS EEIEFVTFRH EQAAAHAADA
WARTTGQPGV CLGTVGPGAA DLVPGVYTAF ADSIPMIVLC AQNQSWRIHP DHGSSQGLDQ
LEMFKPITKW GATVSHWQRI PHLVHWAVRE ALSGKPGPVF LDLPSDVLYM KCDESTLEDG
IVPAEKYRMT RPPVGDPELI SKAADMLVNA AFPLVHAGGG VLASDSAKEL VEIAEHLQAP
VTTSVGARGA IPEDHPLSLV PASFGAIGAQ CQSDLVLLVG GRFGDLDFWG RAPGWGDCAE
QRLIQIDIAP EMIAHNRVVD LAIVGDAKST LTELLRIVKS KPKAKPRTEM ADCREAQDSW
LTDFVSQGKS DQVPIHPLRM VQEVRDFFPR DAISIVDGGN IAVWS
//
