ID M0EUJ1_9EURY Unreviewed; 580 AA.
AC M0EUJ1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Thiamine pyrophosphate protein domain protein TPP-binding {ECO:0000313|EMBL:ELZ50089.1};
GN ORFNames=C464_03150 {ECO:0000313|EMBL:ELZ50089.1};
OS Halorubrum coriense DSM 10284.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1227466 {ECO:0000313|EMBL:ELZ50089.1, ECO:0000313|Proteomes:UP000011509};
RN [1] {ECO:0000313|EMBL:ELZ50089.1, ECO:0000313|Proteomes:UP000011509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10284 {ECO:0000313|EMBL:ELZ50089.1,
RC ECO:0000313|Proteomes:UP000011509};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ50089.1}.
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DR EMBL; AOJL01000016; ELZ50089.1; -; Genomic_DNA.
DR RefSeq; WP_006112052.1; NZ_AOJL01000016.1.
DR AlphaFoldDB; M0EUJ1; -.
DR STRING; 1227466.C464_03150; -.
DR PATRIC; fig|1227466.3.peg.633; -.
DR OrthoDB; 6837at2157; -.
DR Proteomes; UP000011509; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 17..127
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 203..337
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 411..560
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 166..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 59929 MW; E89C94229E194BC5 CRC64;
MDADEPSPAA DRDDSPTVAE AVVDAMLDRG VDTVFGIPGK QTLPLNRALA DRDARFVVAR
HETAVPHQAW GYAETSEPGA MAATCVVPGP GDTNAMNGLK NALNDCVPLL HLAVETERSV
RGGDGIHETP PETYDTVVKE NVLVDSPAGA VPAVVEAIRT AREHPQGPVR VGIPKDFLAG
RTPQPAVGER EPSPPPTPPA AAVREAADLL GDAAAPVVLA GGGVRRAAAS DALRSVAEGF
DAPVVTTYKG KGTLPETHPL SAGVLCGGAS AELRSLLADA DVGLVVGSDL DAVATASWSV
SMPETLIHVT LDGDDVGFGY DADLGVVADA DRFLRALADR LDGERTGTRG DDGVDRAESV
RAADRERFAA LSESTGDGPG GASGDDRPLR SVEVLSAVRD AAPEDAVVAA DAGGFRLWTL
VSFPAAGPQS YVNPGSWATM GTGLPSALGA KLANPDRDVV ALTGDGGLMM CVHELHTLAS
EGIDITVVAL NNDDYAIISE EASRSYDFPD QSYGWAETGL DLVAVASGMG LPAERVRDRD
AVGDAVERAR DRDGPALVEV VTDPAEPQAS EWMTGPHPSE
//
