ID A0A0J7ZL99_STRVR Unreviewed; 600 AA.
AC A0A0J7ZL99;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:KMS76801.1};
GN ORFNames=ACM01_02870 {ECO:0000313|EMBL:KMS76801.1};
OS Streptomyces viridochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938 {ECO:0000313|EMBL:KMS76801.1, ECO:0000313|Proteomes:UP000037432};
RN [1] {ECO:0000313|EMBL:KMS76801.1, ECO:0000313|Proteomes:UP000037432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3414 {ECO:0000313|EMBL:KMS76801.1,
RC ECO:0000313|Proteomes:UP000037432};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUN-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:KMS76801.1}.
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DR EMBL; LFNT01000002; KMS76801.1; -; Genomic_DNA.
DR RefSeq; WP_048579402.1; NZ_LGUR01000117.1.
DR AlphaFoldDB; A0A0J7ZL99; -.
DR PATRIC; fig|1938.3.peg.176; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000037432; 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 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 600 AA; 65215 MW; A1F4D6457DB0A727 CRC64;
MSTKVADHVL QRLREWGVEH VFGYPGDGIN GLLAAWGRAE NKPRFIQSRH EEMSAFQAVG
YAKFSGRLGV CAATSGPGAI HLLNGLYDAK LDHVPVLAVV GQTHRTAMGG SYQQEVDLHT
LFKDVASDFV ETVTVPEQLP NVLDRAIRTA YARRAPTAII IPGDVQELDY SPPTHEFKMV
PSSLDRSGWT SIPSDDSIRR AAEILNAGDK VAILVGQGAS GARAEVERIA ELLGAGVAKA
LLGKDALSDE LPYVTGSIGL LGTRPSYELM RDCDTLLTIG SSFPYTQFLP DFGEARGVQI
DIDPHMVGMR YPYEVNLVGD AKATLERLIP LIRSEERGRE WYDTVCDNVA RWSEVMERRA
NQSADPINPE YVARTLAPLL PDNAIVSSDS GSAANWYARH LTMRPGMRGS LSGTLATMGC
GVPYAIGAKF AHPDRPAIAL VGDGAMQMNG LAELITAAKY KDLWEDPRLV VAVLNNHDLN
QVTWEMRAME GAPSFLPSQE LPDVQYAAFA RSLGLTGIRV EKPEDVEAGW RAGLEADGPA
VIEFLTDPAV PPIPPHATWE QMEATASSIL KGDADRGSMI RQGFKAKVQE FLPGREKKGH
//
