(data stored in ACNUC7421 zone)

HOGENOM: ACTP2_1_PE1001

ID   ACTP2_1_PE1001                       STANDARD;      PRT;   258 AA.
AC   ACTP2_1_PE1001; A3N123;
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=Deoxyribose-phosphate aldolase; Short=DERA; EC=4.1.2
DE   4;AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase;AltName:
DE   Full=Phosphodeoxyriboaldolase; Short=Deoxyriboaldolase; (ACTP2_1.PE1001).
GN   Name=deoC; OrderedLocusNames=APL_1015;
OS   ACTINOBACILLUS PLEUROPNEUMONIAE SEROVAR 5B STR. L20.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACTP2_1.PE1001.
CC       Actinobacillus pleuropneumoniae L20, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:DEOC_ACTP2
CC   -!- FUNCTION: Catalyzes a reversible aldol reaction between
CC       acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-
CC       D-ribose 5-phosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2-deoxy-D-ribose 5-phosphate = D-
CC       glyceraldehyde 3-phosphate + acetaldehyde.
CC   -!- PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate
CC       degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-
CC       deoxy-alpha-D-ribose 1-phosphate: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 2
CC       subfamily.
CC   -!- GENE_FAMILY: HOG000241644 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A3N123; -.
DR   EMBL; CP000569; ABN74109.1; -; Genomic_DNA.
DR   RefSeq; YP_001053714.1; NC_009053.1.
DR   ProteinModelPortal; A3N123; -.
DR   SMR; A3N123; 3-235.
DR   STRING; A3N123; -.
DR   GeneID; 4849634; -.
DR   GenomeReviews; CP000569_GR; APL_1015.
DR   KEGG; apl:APL_1015; -.
DR   eggNOG; COG0274; -.
DR   OMA; ELVQQCK; -.
DR   PhylomeDB; A3N123; -.
DR   ProtClustDB; PRK05283; -.
DR   BioCyc; APLE416269:APL_1015-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:EC.
DR   GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR   HAMAP; MF_00592; DeoC_type2; 1; -.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011343; DeoC.
DR   InterPro; IPR002915; DeoC/AroFGH_arch.
DR   InterPro; IPR023649; DeoC_bac.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   PANTHER; PTHR10889; DeoC; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF001357; DeoC; 1.
DR   TIGRFAMs; TIGR00126; DeoC; 1.
DR   HOGENOMDNA; ACTP2_1.PE1001; -.
KW   Complete proteome; Cytoplasm; Lyase; Schiff base.
SQ   SEQUENCE   258 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSLKDSAKIA LSLMDLTTLN DNDTDEKVIT LCQQGKTEFG TPAAVCVYPR FVPIARKALK
     AQGTEQVKIA TVTNFPHGNN DIDIAVAETK AAVAYGADEV DVVFPYKALM AGNEQIGFEL
     VQQCKAVCQA SNVLLKVIIE TGELKTAELI RKASEISIKA GADFIKTSTG KVPVNATLEY
     ARIMLETIRD LNVADRVGFK AAGGVKTAEE AAQYLALAQE ILGHDWVNSD HFRFGASSLL
     TNLLAALNGQ ANQKVSGY
//

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