ID   A0A365T5V1_9EURY        Unreviewed;       579 AA.
AC   A0A365T5V1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:RBI59279.1};
GN   ORFNames=DMJ13_23570 {ECO:0000313|EMBL:RBI59279.1};
OS   halophilic archaeon.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales.
OX   NCBI_TaxID=29295 {ECO:0000313|EMBL:RBI59279.1, ECO:0000313|Proteomes:UP000252983};
RN   [1] {ECO:0000313|EMBL:RBI59279.1, ECO:0000313|Proteomes:UP000252983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H22 {ECO:0000313|EMBL:RBI59279.1,
RC   ECO:0000313|Proteomes:UP000252983};
RA   Chen S.;
RT   "Draft genome sequence of Haloarchaeon sp. H22 isolated from a salt mine.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:RBI59279.1}.
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DR   EMBL; QNGA01000010; RBI59279.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A365T5V1; -.
DR   Proteomes; UP000252983; 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; cd00568; TPP_enzymes; 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:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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   Reference proteome {ECO:0000313|Proteomes:UP000252983};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          5..116
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          198..336
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          404..554
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   579 AA;  62601 MW;  D72A2B09BFC81AA7 CRC64;
     MAERNGGEII AEYLEKEGVE YLVGIPGHGS TNLLDAFNDS DVEVIQPRHE QGAAHLADGY
     ARASGKPLAV FTSIGPGATN TVTGVATAFV DSIPMVVFTG GPQTHEYGEG ILQEIERKKP
     GDFPSVMEPI TKQSFVVDDV ERLPRVLRRA FQEALTGRPG PVHVEVPMDV QGAVADVEIP
     NPERSRVQSR PGGDPESVAA AADLLVNADR PVIVPGGGCQ LSEAWDEVRA LAEYLQAPVS
     PTFQGKGVIP EDHDLFVGYA GWIGSTAANE LASSADVILA IGVRFSDLHT SSFEPGVSFE
     IPPSELVHVD IDPHEIGKNY PVEVGIQGDA KVVTNQIHDA VADRTEPVDS EGNEYYDEIQ
     ELWDEWEEMV KARRADDDVP MSISRVLAAL RESMDRDGIV VSSAGQPQET TNPEFPVYEP
     RTNVSCGGFS TMGFGVSAAI GAKLARPGRQ VVAVEGDGSF LQTNQEVACA VQHDVDLVYL
     VLNNHGWKSI RNLQVEKYGW DRVLDTEFDP ETDVDYLKLA DAFNVEFAER VVKPEALGDV
     LDDAFEHDGP AVVEAMVRPD DPDSGAIITG EWDLADLEN
//