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Database: UniProt
Entry: I3TTS6_TISMK
LinkDB: I3TTS6_TISMK
Original site: I3TTS6_TISMK 
ID   I3TTS6_TISMK            Unreviewed;       593 AA.
AC   I3TTS6;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Thiamine pyrophosphate protein domain protein TPP-binding protein {ECO:0000313|EMBL:AFK56164.1};
GN   Name=ydaP {ECO:0000313|EMBL:AFK56164.1};
GN   OrderedLocusNames=TMO_b0156 {ECO:0000313|EMBL:AFK56164.1};
OS   Tistrella mobilis (strain KA081020-065).
OG   Plasmid pTM2 {ECO:0000313|EMBL:AFK56164.1,
OG   ECO:0000313|Proteomes:UP000005258}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Geminicoccaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK56164.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK56164.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|Proteomes:UP000005258};
RC   PLASMID=Plasmid pTM2 {ECO:0000313|Proteomes:UP000005258};
RX   PubMed=22458477; DOI=10.1021/ja301735a;
RA   Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA   Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT   "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT   agents.";
RL   J. Am. Chem. Soc. 134:8625-8632(2012).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP003238; AFK56164.1; -; Genomic_DNA.
DR   RefSeq; WP_014752917.1; NC_017966.1.
DR   AlphaFoldDB; I3TTS6; -.
DR   KEGG; tmo:TMO_b0156; -.
DR   PATRIC; fig|1110502.3.peg.4413; -.
DR   HOGENOM; CLU_013748_3_0_5; -.
DR   OMA; ANWYARH; -.
DR   Proteomes; UP000005258; Plasmid pTM2.
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   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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   Plasmid {ECO:0000313|EMBL:AFK56164.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          9..124
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          205..332
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          394..540
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          172..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   593 AA;  63375 MW;  97AEB3A7CA987BE9 CRC64;
     MTAPSPALTA ADILVETLIA WEVDTVFGLP GDGINGVMEA LRTRQDRIRF IQTRHEESAA
     FMASAHAKFT GKLGVCLATS GPGGTHLITG LCDAALDQAP VLAITGLQAH DLIDSFTQQD
     IDLSRMIGNI AVFDTKVASA AHMETVAGLA CRAALTRRGV AHLSIPADMQ VQRLEDSPRS
     SRNRPGHVPN RRFYGRSLPD PDQVELAASI LNRAERVMIL AGQGAAGAVS ELEKTADLLA
     APVAKALLGK AILPEDHPHS TGGIGMLGTL PSEEAMEGCD ALLIVGSTFP YIEYYPDPGQ
     ARAVQIDRDG ERIGLRYPVE AGLVGDAAES LHLLNEKLER KQDRSFLERA QSGMARWREM
     MRAAERQDDV PMKPQVVVGA LGRRLPPEAI LTSDSGQNTE LAARHVPLGP GQDYAVSGTL
     ASMACGLPYA IAAGLAHPDR PVFAIVGDGG FAMQLGEFST AVRHGLNLKL LVIRNGMLNQ
     IAWEQMMFLG NPQFACELQP IDFAKAAEAM GGRGFTVSEP GQVDAVLDQA LATPGPVVID
     AIVDPYEPMM PPRLPETHAR NLREALPETP GREKIEAALA AEPLRTMIEA GRK
//
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