ID C9RGS9_METVM Unreviewed; 511 AA.
AC C9RGS9;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Thiamine pyrophosphate protein TPP binding domain protein {ECO:0000313|EMBL:ACX72781.1};
GN OrderedLocusNames=Metvu_0923 {ECO:0000313|EMBL:ACX72781.1};
OS Methanocaldococcus vulcanius (strain ATCC 700851 / DSM 12094 / M7)
OS (Methanococcus vulcanius).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=579137 {ECO:0000313|EMBL:ACX72781.1, ECO:0000313|Proteomes:UP000002063};
RN [1] {ECO:0000313|EMBL:ACX72781.1, ECO:0000313|Proteomes:UP000002063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700851 / DSM 12094 / M7
RC {ECO:0000313|Proteomes:UP000002063};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Lcollab F.I., Brettin T., Detter J.C.,
RA Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ovchinikova G., Sieprawska-Lupa M., Whitman W.B., Woyke T.;
RT "Complete sequence of chromosome of Methanocaldococcus vulcanius M7.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP001787; ACX72781.1; -; Genomic_DNA.
DR RefSeq; WP_015733001.1; NC_013407.1.
DR AlphaFoldDB; C9RGS9; -.
DR STRING; 579137.Metvu_0923; -.
DR GeneID; 8513260; -.
DR KEGG; mvu:Metvu_0923; -.
DR eggNOG; arCOG02000; Archaea.
DR HOGENOM; CLU_013748_3_1_2; -.
DR Proteomes; UP000002063; Chromosome.
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; 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; 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.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 8..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 208..309
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 362..499
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 511 AA; 57855 MW; DFDF45E5E5134A8B CRC64;
MIVITKFLES IVDFLEKNVK RIFSYPGEQI LPLYNEIEGS SIKNIMVRDE RGAGFMADGY
ARITNHVGVC LVTAGPGATN LTTPIATSYK DSSAVIAITG RCSRDKIGKN YFQEIDMSFL
NFYKGYFVKE PNLKYFEEAF SLSFQNKKPV HLNIPKDVYG EFTIEEEINL NEMKDNNKDN
SKDNDNKGND IVDKTFNWKT LINENEKFKK TLILIGQGIY GTLSYKEMEK ISSVLKKLDI
PIATTFPARG IINEKEENCV GLIGRRGVIK PLLEADRIIN VSSSLSFNTY PESIRKKLLS
KTENIHLTPK NIDEIKEFFE TFGLGEPWET EKWKRISPQG DYSTKINEII ENIPENSIII
TDAGKHTVFT CLLKTCVVPR NIIASHSFGT MGFSVPVSIG AKFGTIDFGI DREVVSISGD
GGFLMNVEEL QVISEHNLKI LMIVMKNNSL AEFCKIKNPN INRLADAFDI DNCYIENVDE
IPQTIREYVK KDKPMLVVVE TRDEKLPRPN I
//