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
//