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Database: UniProt
Entry: A0A242K1Y5_9ENTE
LinkDB: A0A242K1Y5_9ENTE
Original site: A0A242K1Y5_9ENTE 
ID   A0A242K1Y5_9ENTE        Unreviewed;       568 AA.
AC   A0A242K1Y5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Thiamine pyrophosphate enzyme TPP-binding domain-containing protein {ECO:0000259|Pfam:PF02775};
GN   ORFNames=A5888_003770 {ECO:0000313|EMBL:OTP11671.1};
OS   Enterococcus sp. 9E7_DIV0242.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1834193 {ECO:0000313|EMBL:OTP11671.1, ECO:0000313|Proteomes:UP000195141};
RN   [1] {ECO:0000313|EMBL:OTP11671.1, ECO:0000313|Proteomes:UP000195141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9E7_DIV0242 {ECO:0000313|EMBL:OTP11671.1,
RC   ECO:0000313|Proteomes:UP000195141};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genomic Center for Infectious Diseases;
RA   Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA   Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Enterococcus sp. 9E7_DIV0242.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:OTP11671.1}.
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DR   EMBL; NGMM01000007; OTP11671.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A242K1Y5; -.
DR   OrthoDB; 2254214at2; -.
DR   Proteomes; UP000195141; 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   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; IPR000399; TPP-bd_CS.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF9; 3D-(3,5_4)-TRIHYDROXYCYCLOHEXANE-1,2-DIONE HYDROLASE; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 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   Reference proteome {ECO:0000313|Proteomes:UP000195141}.
FT   DOMAIN          418..548
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   568 AA;  62920 MW;  C76BD3ED28491DA6 CRC64;
     MKSPKTDGFK ALSDFLSSLK INLYSGVTGG GVIHFLKYLG PYKGSENSDS PAFFTLSEYA
     AGFTPLGYYL ATGQVSAAVA TTGAATKLLA CGLSDGKLHD IPSVYLFPVS NISHAEDEAL
     QDTSIYGSNI VQQLRAEFPE QVFLLDNVFN FKEQLKNAEQ VLMSRKPVVF LLDNETMMLP
     NYEAVQTTTF EEPDDIEEIK VFLKQFKEKT DGKRVILLVG EEGIHDVGIR KLTTAVCKEL
     KAAAVWSMNG GNCVEADNPY GYGYISFGGN DRALDLWSSI SEEDVVLCVG ASPDEYTTDL
     KKIKANDVFF INNIPNAYGQ IRGSFQHGVA HNVYQISAPI TEVLQSLINE GHYATVACPK
     APENLNDRDI LPPRKGFADM EKVYKRLYDW WQPDSLIISD VCLVYKDYQY VTQRPNENIT
     YFSFYRGSAM GGAYGVAVGA KLGAPDKRVY LFSGDGCFRL YGGSLEEAKN LGIVLFLINN
     QNYSIVSQGL PKILPDVKPE RYHDDLNGLD YCKVAEASGW LSYSVATDLS NFDEILSEIE
     KNETRSILVN IPVDPEQILG QNPRVRNL
//
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