ID A0A176KVP0_9ACTN Unreviewed; 586 AA.
AC A0A176KVP0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:OAA96139.1};
GN ORFNames=A6P39_34945 {ECO:0000313|EMBL:OAA96139.1};
OS Streptomyces sp. FXJ1.172.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=710705 {ECO:0000313|EMBL:OAA96139.1};
RN [1] {ECO:0000313|EMBL:OAA96139.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAA96139.1};
RA Liu M., Liu N., Shang F., Huang Y.;
RT "Activation and identification of NC-1, a novel cryptic cyclodepsipeptide
RT from red soil-derived Streptomyces sp. FXJ1.172.";
RL Submitted (APR-2016) 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:OAA96139.1}.
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DR EMBL; LWRP01000175; OAA96139.1; -; Genomic_DNA.
DR RefSeq; WP_067054638.1; NZ_CP119133.1.
DR AlphaFoldDB; A0A176KVP0; -.
DR STRING; 710705.A6P39_34945; -.
DR OrthoDB; 4959782at2; -.
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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 189..318
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 401..547
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 586 AA; 62279 MW; 8B528F41B5FBE4A8 CRC64;
MTRTVARVIV DALSELGVRQ VFGVVGDALN PLTDAIRTTE GLEWVGCRHE EAAAFAASAQ
SQLTGTLGVC MGTVGPGSVH LLNGLYDAAK SHAPVLAIAG QVPLAELGSD SFQEVDNDAL
FRDVAVFRAT ITSPDQLPQM LETAVRHALG RRGVAVLTVP GDLGERELAD RPARFALSAP
VSRPDGSAVH RAAELLDRSE RVTLLVGEGA RAAREEVLTL ADRLAAPMVL TLKAKAGFEG
DDNPFQVGQT GLIGNPAAAA ALQDADTLLL LGTDFPYRDW YPAGRTVIQV DTEATHIGRR
VPVDVGLVGD TGATVRDLLD DLAAAPAGFE GARDRSHLEK ARERFDQWRT GQARLADPSH
DKGVVGRIRS ALDNRAHDIR PEALAAAVDR IAADDAVFTS DTGMATVWLS RFVEMRGERR
LIGSYNLGSM ANAMPQALGA QCLDRERQVV AFCGDGGLSM LLGDLMTLKT YRLPVKLVVF
DNRRLGMVKL EQEQAGLPEF GTVLDNPDFA AVAEAMGITG IRVTDPADVE GAVRRALGSP
GPVLLDVLTN PDEIAVPAKP TVEQGWGFAV AKVKEIVRSH GESGEN
//
