(data stored in SCRATCH zone)

SWISSPROT: A1AZQ1_PARDP

ID   A1AZQ1_PARDP            Unreviewed;       553 AA.
AC   A1AZQ1;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 79.
DE   SubName: Full=Thiamine pyrophosphate enzyme TPP binding domain protein {ECO:0000313|EMBL:ABL68745.1};
GN   OrderedLocusNames=Pden_0633 {ECO:0000313|EMBL:ABL68745.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68745.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) 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; CP000489; ABL68745.1; -; Genomic_DNA.
DR   RefSeq; WP_011746978.1; NC_008686.1.
DR   STRING; 318586.Pden_0633; -.
DR   PRIDE; A1AZQ1; -.
DR   EnsemblBacteria; ABL68745; ABL68745; Pden_0633.
DR   KEGG; pde:Pden_0633; -.
DR   eggNOG; ENOG4105C7K; Bacteria.
DR   eggNOG; COG0028; LUCA.
DR   HOGENOM; HOG000258445; -.
DR   KO; K01652; -.
DR   OMA; ATWVHRF; -.
DR   BioCyc; PDEN318586:G1GW1-640-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
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;
DR   PRODOM; A1AZQ1.
DR   SWISS-2DPAGE; A1AZQ1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN        3    169       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      187    325       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      380    525       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   553 AA;  58514 MW;  ACF021E33954603E CRC64;
     MRHGGQILVD ALKTNGVGRV FSVPGESFLA VLDGLYASGI RNVVCRHEGG AAMMAEAHGK
     LTGRPGVGFV TRGPGATNAS AGVHVARQDG TPMILFVGQI ARADRDRDAF QEVDYRAMFG
     PLAKWVAEID QTERIPEYVS RAFHLAMSGR PGPVVLALPE DMISARAEVP DLPPPAAPLA
     AVAAESVEAV AQALAGAERP LVVPGGTLWS QAAADDLARF AESWGLPVAV PFRRQGHIDN
     AHPNYVGDLG VGMNPALGQA LSQADCVLSL GSRLGDTLTR GYELMDPVRP HARVIHVHPS
     PDELGRLWRP DPGLAADPRV VVAALAALPV PRRWDGWTAG LRAAYEAWQQ PRPTPGAVRM
     EAVVRWLSDH LPPDAIITNG AGNYAAFVHR YYRFRRWGTQ LAPTSGSMGY GLPAAIAAKL
     EHPGRSVVCM AGDGCLQMTV NELSTAAQHG AAVIVIVANN GHYGTIRMHQ ERSYPGRVSG
     TALANPDFVA LARAYGGHGE TVTRQEDFAD AFARAQAAGR LAVLELMLDP EALSTGATLA
     ETRAAGAAGL RRA
//

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