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
//