SPM_000580


  Uniprot: A0A037UL06
Description: deoxyribose-phosphate aldolase
EC number: 4.1.2.4
Annotation score: 3 out of 5
Miscellaneous [CC]: 
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. {ECO:0000256|HAMAP-Rule:MF_00114, ECO:0000256|SAAS:SAAS00559183}.
Cofactor: 
Enzyme regulation: 
Function [CC]: FUNCTION: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate. {ECO:0000256|HAMAP-Rule:MF_00114, ECO:0000256|SAAS:SAAS00559186}.
Pathway: PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00114, ECO:0000256|SAAS:SAAS00535480}.
Active site: ACT_SITE 151 151 Schiff-base intermediate with acetaldehyde. {ECO:0000256|HAMAP-Rule:MF_00114}.; ACT_SITE 180 180 {ECO:0000256|HAMAP-Rule:MF_00114}.
Binding site: 
Calcium binding: 
DNA binding: 
Metal binding: 
Nucleotide binding: 
Site: 
Gene names (primary): deoC
Gene names (synonym): 
Mass: 23,418
Subunit structure [CC]: 
Gene ontology (GO): cytoplasm [GO:0005737]; deoxyribose-phosphate aldolase activity [GO:0004139]; carbohydrate catabolic process [GO:0016052]; deoxyribonucleotide catabolic process [GO:0009264]; deoxyribose phosphate catabolic process [GO:0046386]
Gene ontology IDs: GO:0004139; GO:0005737; GO:0009264; GO:0016052; GO:0046386
Chain: 
Signal peptide: 
Domain [CC]: 
Sequence similarities: SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00114, ECO:0000256|SAAS:SAAS00535487}.
Protein families: DeoC/FbaB aldolase family, DeoC type 1 subfamily
Coiled coil: 
Domain [FT]: 
Motif: 
Region: 
EMBL: AGBZ02000001
ProteinModelPortal: 
MEROPS: 
EnsemblBacteria KO: KAI92604
UniPathway: 
CDD: 
Gene3D: cd00959
HAMAP: 3.20.20.70
InterPro: MF_00114
PANTHER: IPR013785;IPR011343;IPR002915;IPR028581
PIRSF: PTHR10889
PRINTS: PIRSF001357
PROSITE: 
Pfam: 
ProDom: PF01791
SMART: 
SUPFAM: SM01133
TIGRFAMs: 
123988-124651(-)

>nucleotide sequence
TTAATAACCTGTTCGATGTGGTTTATTTTCCATAATATTAACCCCACCACTTGTTCCAAT
CCGCGTTGCCCCTGCTGTAATCATTGCTAAAACATCAGCTTTAGTACGAACTCCCCCAGC
TGCCTTAACTTGCATATCCTTACCAACTGTTGTTTTCATTAGTTTAACATTGGCAATAGT
TGCACCTGCTTTACTAAAACCTGTTGAAGTTTTAACAAAATCAAGGCCTGCTGCTTTTGC
TAACTGACACGCTTTAATAATTTCTGTTTCAGATAATAAGCATGTTTCTAAAATTACTTT
TACAATATTCTGTCCAGCTGCTTTTTTACATGCTGCCATATCTGCACGCACTAAATCATA
ATTATTTGATTTAAATTGACTAATATTCATTACCATATCAATTTCTGTTGCCCCATCAGC
TAATGCTGTTGTAATTTCTGTCACTTTTGTTATAGTAGCATTTGCACCTAATGGAAAACC
AACCACCACACAAACATTAACTGTACTATCTTGTAATAAATTATGAGCTAATTGAACATA
AGTTGGATTAATACAAACCGATGCAAAATCATATTCTTTTGCTTCAGCACATAATTTTTT
AATCTCTATTATAGTTGCATCTGGTTTCAATAAAGTATGATCAATATATTTATTTAATTT
CAT


>protein sequence
MKLNKYIDHTLLKPDATIIEIKKLCAEAKEYDFASVCINPTYVQLAHNLLQDSTVNVCVV
VGFPLGANATITKVTEITTALADGATEIDMVMNISQFKSNNYDLVRADMAACKKAAGQNI
VKVILETCLLSETEIIKACQLAKAAGLDFVKTSTGFSKAGATIANVKLMKTTVGKDMQVK
AAGGVRTKADVLAMITAGATRIGTSGGVNIMENKPHRTGY






















© Fisunov Lab of Proteomics, 2016.