ID E0XPB3_9BACT Unreviewed; 196 AA.
AC E0XPB3;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Thiamine pyrophosphate enzyme N-terminal TPP-binding domain-containing protein {ECO:0000259|Pfam:PF02776};
DE Flags: Fragment;
OS uncultured bacterium HF0010_16H03.
OC Bacteria; environmental samples.
OX NCBI_TaxID=710811 {ECO:0000313|EMBL:ADI16254.1};
RN [1] {ECO:0000313|EMBL:ADI16254.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20695878; DOI=10.1111/j.1462-2920.2010.02314.x;
RA Rich V.I., Pham V.D., Eppley J., Shi Y., DeLong E.F.;
RT "Time-series analyses of Monterey Bay coastal microbial picoplankton using
RT a 'genome proxy' microarray.";
RL Environ. Microbiol. 13:116-134(2011).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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DR EMBL; GU474833; ADI16254.1; -; Genomic_DNA.
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 InterPro; IPR029061; THDP-binding.
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; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 3: Inferred from homology;
FT DOMAIN 4..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT REGION 167..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 196
FT /evidence="ECO:0000313|EMBL:ADI16254.1"
SQ SEQUENCE 196 AA; 20965 MW; 2F2A38C49B7B7872 CRC64;
MKLSGADMLM HALHDEGVEL IFGYPGGAAL HIYDAIFRQD KIDHILVRHE QGATHAADGY
SRATGKPGVV LVTSGPGATN AITGIATAFM DSIPMVVISG QVASHLIGTD AFQETDMIGV
SRPVVKHSYT IFDAKDIPTV IKEAFHVATT GRPGPVVIDI PKDMTAPENI SDYSYPEKAG
IRSYXPPTDP DKDQVQ
//