ID   A0A151BMA6_9ARCH        Unreviewed;       554 AA.
AC   A0A151BMA6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Thiamine pyrophosphate-binding protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AYL32_008700 {ECO:0000313|EMBL:KYH40948.1};
OS   Candidatus Bathyarchaeota archaeon B26-2.
OC   Archaea; Candidatus Bathyarchaeota.
OX   NCBI_TaxID=1779371 {ECO:0000313|EMBL:KYH40948.1, ECO:0000313|Proteomes:UP000075437};
RN   [1] {ECO:0000313|EMBL:KYH40948.1, ECO:0000313|Proteomes:UP000075437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B26-2 {ECO:0000313|EMBL:KYH40948.1};
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 (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:KYH40948.1}.
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DR   EMBL; LUCE01000020; KYH40948.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151BMA6; -.
DR   STRING; 1779371.AYL32_008700; -.
DR   Proteomes; UP000075437; 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..119
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          198..332
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          395..543
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   554 AA;  59252 MW;  79DA09EF8FF42483 CRC64;
     MASTGAEILV SVLKDYGVTF VSTLCGNGLN RFYMACRDAG IRLVDTHNEQ AAAYMADTYG
     RLTGKIGVCA VSSGVAHSNA LTGVANAYFD GSPMLLITGA SAGYGANRGV FQEYDQVALA
     APICKFSRCV YRVEDLDFMV EEALRTAMSG RPGPVHLTVP LDVMEAEVDG AASKRARPPS
     TVADLQGSQS RGVDLKLVEE AVKVIRGSER PILVAGSGVF YSGGQEALIR FSEAGAIPIV
     IPIWDRGSVE RPHQNFVGVV GAASGEPRLL EDSDLIIMVG ARVDYRVGFL EPPKVSPEAF
     ILRIDVDAAE LMQGTVPDMA VLASPASALN ALAEALTRLG GPTHKEWMRE ARERWRRFRA
     RWVEKSPPAG KPMTGWHIVN ALQPLLGEDV VFLIDGGNIG QWAHMVLADH YPGRWLTCGA
     SAVVGWGLPG AMAAKLAYPE RPVLLLSGDG AFSFTLAEIE AAVRHGLPFV AVVSNDSAWG
     LVVSTQKSRY GEERVIASRF GGVRFDLVAE AMGARGVRVE NPRELRRAVE EGFSSKVPTI
     IDVPVSVLGP PDVV
//