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Database: UniProt
Entry: A0A2I0SRV8_9ACTN
LinkDB: A0A2I0SRV8_9ACTN
Original site: A0A2I0SRV8_9ACTN 
ID   A0A2I0SRV8_9ACTN        Unreviewed;       573 AA.
AC   A0A2I0SRV8;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:PKT72645.1};
GN   ORFNames=CW362_12790 {ECO:0000313|EMBL:PKT72645.1};
OS   Streptomyces populi.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2058924 {ECO:0000313|EMBL:PKT72645.1, ECO:0000313|Proteomes:UP000236178};
RN   [1] {ECO:0000313|EMBL:PKT72645.1, ECO:0000313|Proteomes:UP000236178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A249 {ECO:0000313|EMBL:PKT72645.1,
RC   ECO:0000313|Proteomes:UP000236178};
RA   Wang Z.;
RT   "Streptomyces populusis sp. nov., a novel endophytic actinobacterium
RT   isolated from stems of Populus adenopoda Maxim.";
RL   Submitted (DEC-2017) 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:PKT72645.1}.
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DR   EMBL; PJOS01000019; PKT72645.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0SRV8; -.
DR   OrthoDB; 2443624at2; -.
DR   Proteomes; UP000236178; 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; cd02002; TPP_BFDC; 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:SF169; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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   Reference proteome {ECO:0000313|Proteomes:UP000236178};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          11..119
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          212..340
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          415..569
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   573 AA;  61316 MW;  A1E5145E32C54A26 CRC64;
     MTDTENTPGA GGEALVSAFD SMGADYVFCS SGSEWAPVWE SLARRHRDGE RAPRYLDLTH
     ETVAVGMATG YGLLARRPQA VLLHAAPGLL QGSMAVHGAL LAGVPMVVAS SESTTYGDGP
     GPDPGGQWYR NLSVVGGPHG IARPFTKWSN EAAGVHTLPA MVTRAAELAR RAPAGPVYLN
     IPLEILLEEW DGREAKPVVP PGSTHSSPEE ADAVAELIRE AANPVIVTET AGREAGGFEA
     LVAFAEAWNI PVVEPDSAVC GNFPRTHPLH AGSDIGPWMD EADLILLVNC RAPFYPPSRR
     PSKARIVVVD EVPQRPHIAY QVLFADRYLE GNVTNTLRQL AERAHTRPPD AEATAAVTAR
     RAEHERRHAD EQASIAAAEA KAARSEGIDP VHVAATLRGL LDGRDAIVVD ETITHSRVVR
     RHVRTAAPDS YFYVQGGLGQ GIAVALGVKL AARERPVVLT IGDGAFTYNP IVPSYDAANA
     YGLPLLIVVF NNRVYKSMNL NHRRFYPEGA AAETGEWLGT DLRRLPRLAA FAEPFGMHTE
     TVDAPDALAP ALERALKAVA EGTTAVVDVL VTR
//
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