ID DEOC_CORGL Reviewed; 222 AA. AC Q8NTC4; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 46. DE RecName: Full=Deoxyribose-phosphate aldolase; DE EC=4.1.2.4; DE AltName: Full=Phosphodeoxyriboaldolase; DE Short=Deoxyriboaldolase; DE Short=DERA; GN Name=deoC; OrderedLocusNames=Cgl0383, cg0458; OS Corynebacterium glutamicum (Brevibacterium flavum). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=1718; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RA Nakagawa S.; RT "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; RX MEDLINE=22830012; PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8; RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., RA Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., RA Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., RA McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A., RA Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., RA Tauch A.; RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence RT and its impact on the production of L-aspartate-derived amino acids RT and vitamins."; RL J. Biotechnol. 104:5-25(2003). 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-D-ribose 1-phosphate: step 2/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the deoC/fbaB aldolase family. DeoC type 1 CC subfamily. 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; BA000036; BAB97776.1; -; Genomic_DNA. DR EMBL; BX927149; CAF19098.1; -; Genomic_DNA. DR RefSeq; NP_599631.1; -. DR RefSeq; YP_224684.1; -. DR HSSP; O66540; 1MZH. DR GeneID; 1021418; -. DR GeneID; 3344707; -. DR GenomeReviews; BA000036_GR; Cgl0383. DR GenomeReviews; BX927147_GR; cg0458. DR KEGG; cgb:cg0458; -. DR KEGG; cgl:NCgl0372; -. DR HOGENOM; Q8NTC4; -. DR OMA; Q8NTC4; EEKIAMC. DR BioCyc; CGLU196627-1:CG0458-MON; -. DR BRENDA; 4.1.2.4; 812. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:HAMAP. DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:HAMAP. DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro. DR HAMAP; MF_00114; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011343; DeoC. DR InterPro; IPR002915; DeoC/AroFGH_arch. 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. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Lyase; Schiff base. FT CHAIN 1 222 Deoxyribose-phosphate aldolase. FT /FTId=PRO_0000057230. FT ACT_SITE 156 156 Schiff-base intermediate with FT acetaldehyde (By similarity). FT ACT_SITE 186 186 By similarity. SQ SEQUENCE 222 AA; 22520 MW; 563C3D6B6805DD08 CRC64; MTISRSTMAQ ILDYTLLGPE VTNSELAAFI DSAIELGVGT ICVPNSMVNL TAKAQEAGIR VATVAGFPHG KTPALVKAAE ARLAVQSGAS EVDVVLDIAV VKEGDANRLL QEIVAIREAV PSPVVLKFIL ETAVVSDEAI VTAVNALIAA GADFAKTSTG FHPAGGATVE AVRVMASASR GRVGIKAAGG VKTWEDAVAF VEAGATRIGT SNAGAILEGA PE //