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Database: UniProt
Entry: A0A101S3L3_9ACTN
LinkDB: A0A101S3L3_9ACTN
Original site: A0A101S3L3_9ACTN 
ID   A0A101S3L3_9ACTN        Unreviewed;       598 AA.
AC   A0A101S3L3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KUN66623.1};
GN   ORFNames=AQJ54_15450 {ECO:0000313|EMBL:KUN66623.1};
OS   Streptomyces griseorubiginosus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67304 {ECO:0000313|EMBL:KUN66623.1, ECO:0000313|Proteomes:UP000054375};
RN   [1] {ECO:0000313|EMBL:KUN66623.1, ECO:0000313|Proteomes:UP000054375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40469 {ECO:0000313|EMBL:KUN66623.1,
RC   ECO:0000313|Proteomes:UP000054375};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces griseorubiginosus DSM 40469, type
RT   strain for the species Streptomyces griseorubiginosus.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KUN66623.1}.
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DR   EMBL; LMWV01000014; KUN66623.1; -; Genomic_DNA.
DR   RefSeq; WP_062237845.1; NZ_KQ948736.1.
DR   AlphaFoldDB; A0A101S3L3; -.
DR   Proteomes; UP000054375; 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; cd02014; TPP_POX; 1.
DR   CDD; cd07039; TPP_PYR_POX; 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; IPR047211; POXB-like.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   InterPro; IPR047212; TPP_POXB-like.
DR   InterPro; IPR047210; TPP_PYR_POXB-like.
DR   PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR   PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 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.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054375};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          4..118
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          198..328
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          389..544
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   598 AA;  65424 MW;  7E1856A6B99AD6EC CRC64;
     MSTKVSDHIL ERLREWGVDH VFGYPGDGIN GLLAAWGRAD NQPRFVQSRH EEMSAFEAVG
     YAKFSGRIGV CAATSGPGAI HLLNGLYDAK LDHVPVLAIV GQTHRTAMGG SYQQEVDLHT
     LFKDVASEFV ETVTVPEQLP NVLDRAIRTA YARRCPTAII IPGDVQELDY APPTHEFKML
     PSSLGRSNWT TVPSEESLQR AAEILNSGEK PAILIGQGAA GARAEVERVA EMLGAGVAKA
     LLGKDVLSDE LPYVTGSIGL LGTRPSYELM RDCDTLLTIG SSFPYTQFMP EFGKARAVQI
     DIDPHMIGMR YPYEVNLVGD AKATLQRLIP MLDAERGERK WYETVCDNVK RWRDVMDRRA
     QQSADPINPE YVARALDPLL PDDVIVTSDS GSTANWYARH LTMRPGMRSS LSGTLATMGP
     GVPYAIGAKF AHPDRPAIAL VGDGAMQMNG MAELITAAKY RELWEDPRLI IAVWNNHDLN
     QVTWEMRAME GAPSFLPSQQ LPDVQYAAFA RSLGLTGIRV EKPEDVEAAW RAGLAADGPA
     VLEFLTDPAV PPIPPHATWE QMEATAAAIL KGDADRGSMV KQGFKAKVQE FLPGREKK
//
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