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Database: UniProt
Entry: A0A135VEP5_9ARCH
LinkDB: A0A135VEP5_9ARCH
Original site: A0A135VEP5_9ARCH 
ID   A0A135VEP5_9ARCH        Unreviewed;       574 AA.
AC   A0A135VEP5;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:KXH71118.1};
GN   ORFNames=AM325_15125 {ECO:0000313|EMBL:KXH71118.1};
OS   Candidatus Thorarchaeota archaeon SMTZ1-45.
OC   Archaea; Asgard group; Candidatus Thorarchaeota.
OX   NCBI_TaxID=1706444 {ECO:0000313|EMBL:KXH71118.1, ECO:0000313|Proteomes:UP000070149};
RN   [1] {ECO:0000313|EMBL:KXH71118.1, ECO:0000313|Proteomes:UP000070149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMTZ1-45 {ECO:0000313|EMBL:KXH71118.1};
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   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KXH71118.1}.
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DR   EMBL; LRSL01000100; KXH71118.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135VEP5; -.
DR   STRING; 1706444.AM325_15125; -.
DR   Proteomes; UP000070149; 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; cd02004; TPP_BZL_OCoD_HPCL; 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:SF166; 2-HYDROXYACYL-COA LYASE 2; 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   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          4..122
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   DOMAIN          397..544
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   574 AA;  62606 MW;  17B3662C8D8461FF CRC64;
     MTKMTGGEVL TKCLRQENVR YVFGIPGDQL YPFLDSINST DGIDFVTFRH EQAAAHAADA
     WARTTGNPGV CLGTVGPGAA DLVPGVYAAF ADSIPMIVLC AQNQSWRINP DHGSTQGLDQ
     LNLFKPITKW GATVTHWQRI PHLVHWAFRE ALSGRPGPVF LDIPADVLYL RCEEETLEDG
     IVASDRYRMT KPPVGNPDLI AKAAEMLSKA KFPLIHAGNG VLMSNASREL IAIAEHLQAP
     VTTSVAARGS IPEDHPLTLT PGSFGAIGAQ CESDLVLLVG GRLGDYDFWG RAPGWGDCAD
     QRLIQIDIAP EMIAHNRVVD LAIVGDAKST LTELLKQIKS KPKAKPRPAM TDCRKAQENW
     LVDFIEQGKS TKVPIHPLRM IQEIRNFFPR DAISILDGGN IVVWAIYLNK IYEPRTFLWP
     CDSGHLGVGT GYAIGSKLAH PNKEVYVISG DGAFMFNVQE LETAKRMGTA FTIAIANDRA
     YGMIKAGQKG LYDGRYVGVD FVDVRYDKIA EAMGCFGIRV KKPEDIAPAL QKAKDSGLPA
     VLDIVIDPNI NLVPPDFESV ASVWLEGCQL PGEE
//
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