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Database: UniProt
Entry: A0A022MP65_9ACTN
LinkDB: A0A022MP65_9ACTN
Original site: A0A022MP65_9ACTN 
ID   A0A022MP65_9ACTN        Unreviewed;       340 AA.
AC   A0A022MP65;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:EYT82580.1};
DE   Flags: Fragment;
GN   ORFNames=CF54_12510 {ECO:0000313|EMBL:EYT82580.1};
OS   Streptomyces sp. Tu 6176.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1470557 {ECO:0000313|EMBL:EYT82580.1, ECO:0000313|Proteomes:UP000020060};
RN   [1] {ECO:0000313|EMBL:EYT82580.1, ECO:0000313|Proteomes:UP000020060}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tu 6176 {ECO:0000313|EMBL:EYT82580.1,
RC   ECO:0000313|Proteomes:UP000020060};
RA   Olano C., Cano-Prieto C., Mendez C., Salas J.A.;
RT   "Draft genome sequence of Streptomyces sp. Tu 6176, producer of the
RT   cytotoxic benzoxazol nataxazol.";
RL   Submitted (MAR-2014) 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:EYT82580.1}.
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DR   EMBL; JFJQ01000379; EYT82580.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A022MP65; -.
DR   HOGENOM; CLU_817667_0_0_11; -.
DR   Proteomes; UP000020060; 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;
FT   DOMAIN          9..119
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          191..325
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   NON_TER         340
FT                   /evidence="ECO:0000313|EMBL:EYT82580.1"
SQ   SEQUENCE   340 AA;  35875 MW;  AB1A7667CD06D09A CRC64;
     MVSRPARVAI LEQLRADGVR HMFGNPGTVE QGFLDELRNF PDIEYILALQ ESSVVGLADG
     YARATRTPAV MQLHTGVGVG NAVGMLYQAA RGHAPLVAVA GEAGLRYDAM EAQMAVDLVA
     MAEPVTKWAT RVVDPESVLR VLRRAFKVAA TPPYGPVLVV LPADVMDRDT SEPAVPTSYV
     DFAATPDAEV LDRAAGLLAG AERPLVIAGD GVHFAGAQEE LGRLARVWGA EVWGADWAEV
     NLSVEHPAYG GQLGHMFGES SRKVTAAADA VLITGTYALP EVYPALDGVF ADGAPVVHID
     LDTGAIAKNF PVDLGIAADP RRALGGLARA LERRMSPAAR
//
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