ID   A0A0P7GBP6_9EURY        Unreviewed;       435 AA.
AC   A0A0P7GBP6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Thiamine pyrophosphate protein {ECO:0000313|EMBL:KPN31196.1};
GN   ORFNames=SY89_01939 {ECO:0000313|EMBL:KPN31196.1};
OS   Halolamina pelagica.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae.
OX   NCBI_TaxID=699431 {ECO:0000313|EMBL:KPN31196.1, ECO:0000313|Proteomes:UP000050535};
RN   [1] {ECO:0000313|Proteomes:UP000050535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDK2 {ECO:0000313|Proteomes:UP000050535};
RA   Hoang H.T., Killian M.L., Madson D.M., Arruda P.H.E., Sun D.,
RA   Schwartz K.J., Yoon K.;
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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:KPN31196.1}.
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DR   EMBL; LGUC01000001; KPN31196.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7GBP6; -.
DR   STRING; 699431.SY89_01939; -.
DR   PATRIC; fig|699431.3.peg.1990; -.
DR   Proteomes; UP000050535; 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; -; 1.
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:SF167; 2-KETOARGININE DECARBOXYLASE ARUI-RELATED; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000050535}.
FT   DOMAIN          1..111
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          187..321
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   REGION          396..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   435 AA;  45396 MW;  276C22153B70742E CRC64;
     MTLAASVIDR LVANGIDTVF GIPGKQTLPL NEAIDGRDDV RFVMARHETA VSQQAWGYAE
     TSGRPAATVV VPGPGDMNAM NGLKNAYNDN TPLVHIAVET DPEVRGRDGI HETPPETYDT
     VTKANRVVKN PEGVLAAVER AVETATTAPK GPVRLGIPKS YLPAATPNGG VGDAGSDEPV
     RPPADTVADA AKTLADADAP AIVAGGGVRS ANASEELREF AERYDAPVLT TYKGKGVLPE
     THPLSAGVLC GATTPEIHEY VAEADAVLAV GTDFDELVTR GRSLEIPGEL IHVTLSPDDL
     GTNYDPAVGI VADAKPTLAA LNGKLPVSDH DAAAVADRLR ESVARRVDDL VDGDLPLSSP
     GALRAVRAAT PDDAIVAADA GGFRIWALAT FPAMGRDPTS TPARGRRWGA ASRRRWEHRP
     PTPTATWSRS PATAG
//