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Database: UniProt
Entry: D6YAT0_THEBD
LinkDB: D6YAT0_THEBD
Original site: D6YAT0_THEBD 
ID   D6YAT0_THEBD            Unreviewed;       536 AA.
AC   D6YAT0;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   28-MAR-2018, entry version 43.
DE   SubName: Full=Thiamine pyrophosphate protein TPP binding domain protein {ECO:0000313|EMBL:ADG88297.1};
GN   OrderedLocusNames=Tbis_1583 {ECO:0000313|EMBL:ADG88297.1};
OS   Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 /
OS   JCM 10125 / NBRC 14880 / R51).
OC   Bacteria; Actinobacteria; Actinobacteria incertae sedis;
OC   Thermobispora.
OX   NCBI_TaxID=469371 {ECO:0000313|EMBL:ADG88297.1, ECO:0000313|Proteomes:UP000006640};
RN   [1] {ECO:0000313|EMBL:ADG88297.1, ECO:0000313|Proteomes:UP000006640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / NBRC 14880 /
RC   R51 {ECO:0000313|Proteomes:UP000006640};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Jando M., Schneider S., Klenk H.-P.,
RA   Eisen J.A.;
RT   "The complete genome of Thermobispora bispora DSM 43833.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP001874; ADG88297.1; -; Genomic_DNA.
DR   RefSeq; WP_013131830.1; NC_014165.1.
DR   STRING; 469371.Tbis_1583; -.
DR   EnsemblBacteria; ADG88297; ADG88297; Tbis_1583.
DR   KEGG; tbi:Tbis_1583; -.
DR   eggNOG; ENOG4105C7K; Bacteria.
DR   eggNOG; COG0028; LUCA.
DR   HOGENOM; HOG000258446; -.
DR   KO; K01652; -.
DR   OMA; AWQEVDY; -.
DR   OrthoDB; POG091H02KO; -.
DR   BioCyc; TBIS469371:G1GL8-1586-MONOMER; -.
DR   Proteomes; UP000006640; Chromosome.
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   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
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-bd_C.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006640};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006640};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN       10    178       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      197    326       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      388    528       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   536 AA;  54779 MW;  39C11B9C6FA8430B CRC64;
     MSDPAKTTVT GGEALVAALA AHGVDVVFGI PGTHNLPIYA HLRGHGIRHF SPRHEQGAGY
     AADGYARVSG RPGVCLTTTG PGALNAITAA AQAYSDSVPV LFIAPGMPLA HPGHGNGFLH
     EVKDQTAAMA AVVAHAHRVT GVPEIPAAVA QAFAAMRSGR PRPAYLEIPL DLLDQRAEVT
     PVAPLPVPAA PPGPERLDRA ARVLAGAARP GVIAGGGCRG AAGELRRLAE ALGAPVITTA
     NGKGTLPEDH PLSLGAGIHH PSVRDFIAEC DAVVAVGTEL APSDLWNGPL RFTGPLVRID
     IDPHQAVVNA LPDVSVIGDA AAALAGLLDR HGGSPAPDAA ARAARWRARI REDARREGGP
     WLPILEAMAA ALGRDGVVAG DSTMAAYYGA LSNLPAYGPA AFLYPTGLGT LGYGLPAAIG
     AKLARPGVRV VALHGDGGVM FTVAELAAAA QAGLALPVVV VDNGGYGEIR REMLERGDTP
     LAVDLGHPDF PGLARSLGCH GVTIEDPERL TAELEEAFRA DRPTLLHVRE PEGGAG
//
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