GenomeNet

Database: UniProt/TrEMBL
Entry: D1A2M8_THECD
LinkDB: D1A2M8_THECD
Original site: D1A2M8_THECD 
ID   D1A2M8_THECD            Unreviewed;       534 AA.
AC   D1A2M8;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   11-JUN-2014, entry version 30.
DE   SubName: Full=Thiamine pyrophosphate protein domain protein TPP-binding protein;
GN   OrderedLocusNames=Tcur_0450;
OS   Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 /
OS   NCIMB 10081).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptosporangineae; Thermomonosporaceae; Thermomonospora.
OX   NCBI_TaxID=471852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / NCIMB 10081;
RX   DOI=10.4056/sigs.1453580;
RA   Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Djao O., Land M., Hauser L.,
RA   Chang Y., Jeffries C., Brettin T., Han C., Detter J., Rohde M.,
RA   Goker M., Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Klenk H., Kyrpides N.;
RT   "Complete genome sequence of Thermomonospora curvata type strain
RT   (B9).";
RL   Stand. Genomic Sci. 1:13-22(2011).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001738; ACY96048.1; -; Genomic_DNA.
DR   RefSeq; YP_003298086.1; NC_013510.1.
DR   ProteinModelPortal; D1A2M8; -.
DR   EnsemblBacteria; ACY96048; ACY96048; Tcur_0450.
DR   GeneID; 8601747; -.
DR   KEGG; tcu:Tcur_0450; -.
DR   PATRIC; 32510409; VBITheCur33965_0451.
DR   HOGENOM; HOG000258446; -.
DR   KO; K01652; -.
DR   OMA; ADSAMAC; -.
DR   OrthoDB; EOG6SR96S; -.
DR   BioCyc; TCUR471852:GHHD-457-MONOMER; -.
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   Gene3D; 3.40.50.1220; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
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; Thiamine pyrophosphate.
SQ   SEQUENCE   534 AA;  54637 MW;  ED085A7D16252D07 CRC64;
     MATMTGGEAL IAALAAHGVD TIFGIPGTHN LSAYAAMKRH GIRHISPRHE QGAGYAADGY
     ARSSGRPGVC LTTTGPAILN AASAALQAYS DSVPVLFVSP GMPLRHPGRG NGLLHEVKDQ
     SGAMAAILGR SHRVTSVAEI PLAVAQAWTD LTGGRPRPVH LEIPLDLLEE RAEVTVVDPV
     PATTCTPAPE SVTAGAAACA GARRPVLVVG GGARRAGAEV IALAEAVGAP ILATSNGKGI
     VPEDHPLFVG AGLQHRCVLD LMDDSDLVIA VGTEFAPSDW WIGLPDLSGK VLRIDVDPAG
     IVTNVVPAVP VVGDAAVALR ALRAELDRPA PAGAAQRAAQ WRDRHRQAAR AEGEPWLPIV
     SAIAEALPRD AIVAADSAMA CYYGALSNLP LHRPGAFLYP TGAGTLGFGL PAGIGAKIAD
     PDAAVLVLQG DGGTMFTVAE LAAAAELGIA LPVVVVDNGG YGEIRNEMAD RGEPVHAVAL
     GRPDFPALAR SLGCHGVRAA DPAELTGAVK AALEADRPTL IHVREESRAA RGMA
//
DBGET integrated database retrieval system