(data stored in ACNUC7421 zone)

SWISSPROT: A5FTR0_ACICJ

ID   A5FTR0_ACICJ            Unreviewed;       571 AA.
AC   A5FTR0;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   07-JUN-2017, entry version 69.
DE   SubName: Full=Pyruvate dehydrogenase (Cytochrome) {ECO:0000313|EMBL:ABQ28992.1};
GN   OrderedLocusNames=Acry_3383 {ECO:0000313|EMBL:ABQ28992.1};
OS   Acidiphilium cryptum (strain JF-5).
OG   Plasmid pACRY02 {ECO:0000313|EMBL:ABQ28992.1,
OG   ECO:0000313|Proteomes:UP000000245}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=349163 {ECO:0000313|EMBL:ABQ28992.1, ECO:0000313|Proteomes:UP000000245};
RN   [1] {ECO:0000313|EMBL:ABQ28992.1, ECO:0000313|Proteomes:UP000000245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JF-5 {ECO:0000313|Proteomes:UP000000245};
RC   PLASMID=Plasmid pACRY02 {ECO:0000313|Proteomes:UP000000245};
RG   US DOE Joint Genome Institute;
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., Sims D., Brettin T., Bruce D., Han C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Magnuson T.,
RA   Richardson P.;
RT   "Complete sequence of plasmid2 pACRY02 of Acidiphilium cryptum JF-5.";
RL   Submitted (MAY-2007) 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; CP000690; ABQ28992.1; -; Genomic_DNA.
DR   RefSeq; WP_011930662.1; NC_009468.1.
DR   ProteinModelPortal; A5FTR0; -.
DR   EnsemblBacteria; ABQ28992; ABQ28992; Acry_3383.
DR   KEGG; acr:Acry_3383; -.
DR   HOGENOM; HOG000258444; -.
DR   KO; K00156; -.
DR   OMA; DRNAFQD; -.
DR   OrthoDB; POG091H02KO; -.
DR   Proteomes; UP000000245; Plasmid pACRY02.
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   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; A5FTR0.
DR   SWISS-2DPAGE; A5FTR0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000245};
KW   Plasmid {ECO:0000313|EMBL:ABQ28992.1};
KW   Pyruvate {ECO:0000313|EMBL:ABQ28992.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000245};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN        4    169       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      190    317       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      378    524       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   571 AA;  61727 MW;  C5BD5A8795961BAD CRC64;
     MASTVAEIIV DTLCQAGARR CWGIVGDTIN HFTDAVRKSD LRWVHVRHEE AGALAAGGEG
     YLTGELAVCA GTCGPGSLHF VNGIFESHRN GAPVVLIASD VARAEAGLRF PQEVDQRKIY
     EQASVFCEYV SHPDQARRIT TLAAQAALTR GGVAVVIVNG DMFTETTDDR LEWRVHRPSS
     VLRPSDDELD ALARDLDSAA RVTIYAGIGA RGAAARVVQL AGLLKAPIVH TSRAKEFIEP
     NNPFNIGMTG ILGNRAGVEA IDAADIMLCL GTDFAWTQFY PDARYVIQID SDPTHLGRRA
     PIRTGLVGDV GATIEALLPR LKTRSDSAHL DRSLKRWAAD REGYAKLACA HDDALIHPQT
     VAQTLDTLAA DDAIFTADGG SPMVWLLRHV TANGRRSFLT SLLHGTMANA YPQAMGMAAA
     FPGRQVIAMC GDGGMTMLMG DLLTLVQEKL PIKLLVFNNG SLGFVEMEQR VEGLIDSFTE
     LKNPDFAKLA EVCGISGWRV DTGPELEPAM RRWLAAEGPA LLDVHVNRVE LVMPPKVEIG
     QVASTALFGV RAVLDGRSRE VVQLLRDNFL R
//

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