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Database: UniProt
Entry: W0JXB9_9EURY
LinkDB: W0JXB9_9EURY
Original site: W0JXB9_9EURY 
ID   W0JXB9_9EURY            Unreviewed;       580 AA.
AC   W0JXB9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Thiamine pyrophosphate protein central region {ECO:0000313|EMBL:AHG01855.1};
GN   ORFNames=HALLA_00760 {ECO:0000313|EMBL:AHG01855.1};
OS   Halostagnicola larsenii XH-48.
OG   Plasmid unnamed {ECO:0000313|EMBL:AHG01855.1}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Halostagnicola.
OX   NCBI_TaxID=797299 {ECO:0000313|EMBL:AHG01855.1, ECO:0000313|Proteomes:UP000019024};
RN   [1] {ECO:0000313|EMBL:AHG01855.1, ECO:0000313|Proteomes:UP000019024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XH-48 {ECO:0000313|EMBL:AHG01855.1,
RC   ECO:0000313|Proteomes:UP000019024};
RC   PLASMID=2 {ECO:0000313|Proteomes:UP000019024};
RG   DOE Joint Genome Institute;
RA   Anderson I., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP007057; AHG01855.1; -; Genomic_DNA.
DR   RefSeq; WP_049954709.1; NZ_CP007057.1.
DR   AlphaFoldDB; W0JXB9; -.
DR   GeneID; 25147224; -.
DR   KEGG; hlr:HALLA_00760; -.
DR   PATRIC; fig|797299.3.peg.3570; -.
DR   eggNOG; arCOG01998; Archaea.
DR   HOGENOM; CLU_013748_3_1_2; -.
DR   OrthoDB; 6837at2157; -.
DR   Proteomes; UP000019024; Plasmid 2.
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:SF169; 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   Plasmid {ECO:0000313|EMBL:AHG01855.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019024};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          5..118
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          198..337
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          403..553
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          176..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   580 AA;  62790 MW;  34CAF488E854EA10 CRC64;
     MPTLTGGEIV AKYLEKEGVE YLVGIPGHGS TNLLDAFNDS DVEVIQPRHE QGATHLADGY
     ARASGDPLAV FTSIGPGATN TVTGAATAYV DSIPMVIFTG APQTHEYGQG ILQELDRQKP
     GDFPSVMEPV TKRSFVVRDV EQLPRTLRRA FQVAVTGRPG PVHVDIPMDV QGSAADVEIP
     DPEETRTHSR PGGDPESIEE AANLLADADR PVIVPGGGCM LGEAWDEVQA LAEHLKAPVI
     PTFQAKGIIP EDHELFVGYA GWIGSSAGNE LASNADVVLG IGCRFSDLHT SSFEQGVSFE
     IPPSKLIHVD IDNTEIGKNY PVEVGILGDA KVVTDQLHDA VFERVDEVST EDNEYYDEIQ
     RLWADWQEQV EQRHTDDVPM SIARALASLR EALPREGMIV SSAGQPQEIT NPEFPVYDPR
     TNISCGGFST MGFGVSAAIG AKLAEPDRPV VDIEGDGSFL MCNQEVACAV EHDIDVTWVV
     VNNNGWKSIR NLQVDKYGWD RVLNTEFDND SDVDFVKMAD AFSIDFAERV VKPENLTETI
     TDAIEHDGPA FVEAVVEPDS ADSGAIITGE WDLADLEADD
//
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