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
//