ID A0A0G0JEV8_9BACT Unreviewed; 594 AA.
AC A0A0G0JEV8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Thiamine pyrophosphate protein central region {ECO:0000313|EMBL:KKQ26701.1};
GN ORFNames=US40_C0001G0050 {ECO:0000313|EMBL:KKQ26701.1};
OS Candidatus Roizmanbacteria bacterium GW2011_GWC2_37_13.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1618486 {ECO:0000313|EMBL:KKQ26701.1, ECO:0000313|Proteomes:UP000034917};
RN [1] {ECO:0000313|EMBL:KKQ26701.1, ECO:0000313|Proteomes:UP000034917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKQ26701.1}.
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DR EMBL; LBSV01000001; KKQ26701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0JEV8; -.
DR Proteomes; UP000034917; 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 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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF142; ACETOLACTATE SYNTHASE; 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 1..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 203..336
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 398..548
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 594 AA; 66255 MW; 415AF9CF112AF680 CRC64;
MRIADYIIDY IYKNGTDTIF TLAGGGAMFL NDAVACHKKM KYVCNHHEQA SAMAAEAYAK
TNQGIGAVMV TSGPGSTNAI TGLLEAWQNS IPVIFISSQA KKSQMTHFSG LPIRQFGIQE
LDIIPIVRPL TKYADYVEKP EEIRFKIEKA YQEMLSGRPG PVWLDIPPDV ASQSIDPEKL
PGFVDKKTPN SLPKISTREI GLVINLLNRA RKPIIIAGGG IKLAKAVSEF RALVNILKIP
VVVPEMGIDL LENNHPCYAG HGGTKGDRAG NIVIQNSDLI LAIGSRLSVS FTGHEFDKYA
PRSVKIVIDV DEKEHQKKTV KINHLIISDA KYFIEEMIKN KQKLIDNKNV WLKKCQIIKN
KYGLYLPKIK DKNGEISMYH IVDTISKLSR PGDFFITDAG VTAYIAVQTL KFKKNQRMII
PGATLTMGYN LPAILGVWAA NKNARIICIT GDGSLQMNIH ELGTIAYHKI PAKIFVINNH
GYLAIRTTQK NFFQSRLIGE GSGSGVYLPS SQKIAQAYGY KYVRIKNYKE LSKIKQVMKE
KSAVICEVFS PYWQDVLTVS SKKMPDGKMV SLPIDDMYPF LPEEEMKQIR QSLK
//
