ID A0A0X3S2D5_9ACTN Unreviewed; 606 AA.
AC A0A0X3S2D5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KUJ37990.1};
GN ORFNames=ADL25_26040 {ECO:0000313|EMBL:KUJ37990.1};
OS Streptomyces sp. NRRL F-5122.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609098 {ECO:0000313|EMBL:KUJ37990.1, ECO:0000313|Proteomes:UP000054048};
RN [1] {ECO:0000313|Proteomes:UP000054048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-5122 {ECO:0000313|Proteomes:UP000054048};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
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:KUJ37990.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMWH01000240; KUJ37990.1; -; Genomic_DNA.
DR RefSeq; WP_059130259.1; NZ_LMWH01000240.1.
DR AlphaFoldDB; A0A0X3S2D5; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000054048; 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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054048};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..120
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 388..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 606 AA; 66131 MW; CF05762E18F4ACC1 CRC64;
MSMKVSDHVL ERLRDWGVEH VFAYPGDGIN GLLAAWGRAD DKPRFIQARH EEMAAFEAVG
YAKFSGRVGV CAATSGPGAI HLLNGLYDAK LDHVPVVAIV GQTNRSAMGG SYQQEVDLLS
LYKDVASDFC EMVTVPEQLP NVLDRAMRTA MARRSVTAVI IPADVQELDY SPPEHAFKMV
PSSLGMPHYA PVPSDEDVTR AADVLNAGDK VAILIGQGAR GARQEVMAVA DRLGAGVAKA
LLGKDALDDD LPYVTGSIGL LGTRPSYEMM QGCDTLLVIG SSFPYTQFLP EFGQARAVQI
DIDPHMIGLR YPFEVNLVGD ARETLDRLLP LLDTAKDQGW RRKIEKNTAR WWEVMERRAA
VAAYPINPEY VAHALNDLLP DNVVLASDSG SAANWYARHL KLRGAMRGSL SGTLATMGPG
VPYVIGAKFA HGDRPAIALV GDGAMQMNGM AELITVAKYY REWEDPRLIV AILNNHDLNQ
VTWEMRAMEG APQFLPSQSI PDVAYADFAR LIGLEGLRVE KPVDVRGAWE TALATDRPCV
LDFVTDPAVP PIPPHATLDQ IEAAAASVIK GDSDRAAMVR QGFKAKVQEF LPGHRHRNER
PSRTER
//
