ID W4M855_9BACT Unreviewed; 229 AA.
AC W4M855;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Thiamine pyrophosphate enzyme N-terminal TPP-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=ETSY2_17635 {ECO:0000313|EMBL:ETX06353.1};
OS Candidatus Entotheonella gemina.
OC Bacteria; Nitrospinae/Tectomicrobia group; Candidatus Tectomicrobia;
OC Entotheonella.
OX NCBI_TaxID=1429439 {ECO:0000313|EMBL:ETX06353.1, ECO:0000313|Proteomes:UP000019140};
RN [1] {ECO:0000313|EMBL:ETX06353.1, ECO:0000313|Proteomes:UP000019140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSY2 {ECO:0000313|Proteomes:UP000019140};
RX PubMed=24476823; DOI=10.1038/nature12959;
RA Wilson M.C., Mori T., Ruckert C., Uria A.R., Helf M.J., Takada K.,
RA Gernert C., Steffens U.A., Heycke N., Schmitt S., Rinke C., Helfrich E.J.,
RA Brachmann A.O., Gurgui C., Wakimoto T., Kracht M., Crusemann M.,
RA Hentschel U., Abe I., Matsunaga S., Kalinowski J., Takeyama H., Piel J.;
RT "An environmental bacterial taxon with a large and distinct metabolic
RT repertoire.";
RL Nature 506:58-62(2014).
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:ETX06353.1}.
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DR EMBL; AZHX01000721; ETX06353.1; -; Genomic_DNA.
DR AlphaFoldDB; W4M855; -.
DR HOGENOM; CLU_1216935_0_0_7; -.
DR Proteomes; UP000019140; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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:UP000019140}.
FT DOMAIN 1..104
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 185..229
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT NON_TER 229
FT /evidence="ECO:0000313|EMBL:ETX06353.1"
SQ SEQUENCE 229 AA; 24709 MW; F3F31DD17C7A2498 CRC64;
MDTNQAVARV LKSEGVEWVA CFPSNNLIEA VAKEGIRPIM FRQERGALMA ADGFSRLSNR
KAFGVVITQG GPGSENSMGG LAQAFGDNVP MLYLPGGPAL AQHDVRPNFS PVRTYQTVST
YGEVIWKPEM TASVMRRAFH KLRNGRPGPV IVEIPADVST QEVPESSFNY LPPKRLIQAP
SPSDVKEAVQ ILLGAKKPVI WSGMGTLLGE ASEELKALAE LTGVPVYCT
//
