(data stored in ACNUC7421 zone)

HOGENOM: THICR_1_PE1001

ID   THICR_1_PE1001                       STANDARD;      PRT;   886 AA.
AC   THICR_1_PE1001; Q31GX7;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Pyruvate dehydrogenase E1 component; EC=1.2.4 1;
DE   (THICR_1.PE1001).
GN   OrderedLocusNames=Tcr_1001;
OS   THIOMICROSPIRA CRUNOGENA XCL-2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Thiomicrospira.
OX   NCBI_TaxID=317025;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS THICR_1.PE1001.
CC       Thiomicrospira crunogena XCL-2, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:Q31GX7_THICR
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains
CC       multiple copies of three enzymatic components: pyruvate
CC       dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
CC       lipoamide dehydrogenase (E3) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC       acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate (By similarity).
CC   -!- GENE_FAMILY: HOG000115215 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q31GX7; -.
DR   EMBL; CP000109; ABB41596.1; -; Genomic_DNA.
DR   RefSeq; YP_391270.1; NC_007520.2.
DR   ProteinModelPortal; Q31GX7; -.
DR   SMR; Q31GX7; 56-886.
DR   STRING; Q31GX7; -.
DR   GeneID; 3760487; -.
DR   GenomeReviews; CP000109_GR; Tcr_1001.
DR   KEGG; tcx:Tcr_1001; -.
DR   NMPDR; fig|317025.3.peg.787; -.
DR   eggNOG; COG2609; -.
DR   OMA; YYYVTLM; -.
DR   PhylomeDB; Q31GX7; -.
DR   ProtClustDB; PRK09405; -.
DR   BioCyc; TCRU317025:TCR_1001-MONOMER; -.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:EC.
DR   InterPro; IPR004660; 2-oxoA_DH_E1.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR   InterPro; IPR015941; Transketolase-like_C.
DR   InterPro; IPR005474; Transketolase_N.
DR   Gene3D; G3DSA:3.40.50.920; Transketo_C_like; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR   SUPFAM; SSF52922; Transketo_C_like; 1.
DR   TIGRFAMs; TIGR00759; AceE; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   HOGENOMDNA; THICR_1.PE1001; -.
KW   pyruvate dehydrogenase subunit E1;
KW   Complete proteome; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
SQ   SEQUENCE   886 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNDKFVDQDP QETQEWIDAL EAVVSFEGSD KAQHIIGTLI EKARVHGIDI PYSANTPYIN
     TIAPEEQENY PGDVGIERKM RALLRWNAMA MVSRANKYTS VGGHIASYAS SCTLYEVGMN
     HFFKGPKHKQ GADMIFFQGH TAPGMYARSY MEGRLEADQL RNYRQEVDGN GLSSYPHPWL
     MSDYWQFPTV SMGLGPLMAI YQARFMKYMQ ARGLAETEGR KVWAFLGDGE MDEPESRGAL
     QLAKRENLDN LIFVINCNLQ RLDGPVRGND KIIQELEGVF RGAGWNVIKV IWGSGWDRLL
     SKDVTGKLIE RMGEVVDGEY QAYKAKDGAF VREHFFGKYP ETAELVKDMT DDEIFRLTRG
     GHSPRKIYNA YKRATETQGQ PTVILAKTVK GYGMGQYGEA ANTAHQQKKL DIEGMKYFRD
     RFSVPISNEE LEKDIPFHRP DEDSDVLKYM KERREALGGD LPSRQDTAEP LPVPDLSVFK
     MLTEGTEDRE MSTTMAFVRI ISILLRDKKI GPRCVPIIPD EARTFGMEGL FRQVGIYDPA
     GQLYEPMDSD QLMWYKESAN GQVFQEGINE AGAMSNWIAA ATAYANYGVS MVPFYIYYSM
     FGYQRIGDLA WAAGDSRARG FLMGGTAGRT TLEGEGLQHQ DGHNLIQFDH VPNCLSYDPT
     FAYEMAVIIR DGIKRMFNEK EDVYYYITCM NENYSHPAMP AGSEEGILKG LYSFKKSEAK
     HKNKVQLMGS GTIFREVIAA AEMLENEWDV AADIWAAPSF NLLRRDGVET TRWNTMHPTE
     KPKVSYCEAT LSGAKGPFIA ATDYIRDYPN RIREYVPGEF YVLGTDGFGR SDTREQLRKF
     FEVNRYYVVV ESLKALADAG SIKPEVVQKA IEKYGIDSEK TYPVHA
//

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