ID A4FNV7_SACEN Unreviewed; 328 AA.
AC A4FNV7;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=deoxyribose-phosphate aldolase {ECO:0000256|ARBA:ARBA00012515};
DE EC=4.1.2.4 {ECO:0000256|ARBA:ARBA00012515};
DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000256|ARBA:ARBA00032755};
DE AltName: Full=Phosphodeoxyriboaldolase {ECO:0000256|ARBA:ARBA00031814};
GN Name=deoC {ECO:0000313|EMBL:CAM05732.1};
GN OrderedLocusNames=SACE_6564 {ECO:0000313|EMBL:CAM05732.1};
GN ORFNames=A8924_6914 {ECO:0000313|EMBL:PFG99372.1};
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM05732.1, ECO:0000313|Proteomes:UP000006728};
RN [1] {ECO:0000313|EMBL:CAM05732.1, ECO:0000313|Proteomes:UP000006728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC {ECO:0000313|EMBL:CAM05732.1};
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
RN [2] {ECO:0000313|EMBL:PFG99372.1, ECO:0000313|Proteomes:UP000225825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG99372.1,
RC ECO:0000313|Proteomes:UP000225825};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde
CC 3-phosphate; Xref=Rhea:RHEA:12821, ChEBI:CHEBI:15343,
CC ChEBI:CHEBI:59776, ChEBI:CHEBI:62877; EC=4.1.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000764};
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 {ECO:0000256|ARBA:ARBA00004816}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00009473}.
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DR EMBL; AM420293; CAM05732.1; -; Genomic_DNA.
DR EMBL; PDBV01000001; PFG99372.1; -; Genomic_DNA.
DR RefSeq; WP_011875084.1; NZ_PDBV01000001.1.
DR AlphaFoldDB; A4FNV7; -.
DR STRING; 405948.SACE_6564; -.
DR KEGG; sen:SACE_6564; -.
DR eggNOG; COG0274; Bacteria.
DR HOGENOM; CLU_053595_3_0_11; -.
DR Proteomes; UP000006728; Chromosome.
DR Proteomes; UP000225825; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR CDD; cd00959; DeoC; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011343; DeoC.
DR InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR NCBIfam; TIGR00126; deoC; 1.
DR PANTHER; PTHR10889; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR10889:SF3; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR Pfam; PF01791; DeoC; 1.
DR SMART; SM01133; DeoC; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:CAM05732.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006728}.
SQ SEQUENCE 328 AA; 34784 MW; 639A41C6C3CCA9EB CRC64;
MAYPPPTTPS VTSSPGLPAE LAEATKDDST LRRFLHGLPG VDQVGLEQRA AGLATRSIKK
AAKLWAIDTA IGMVDLTTLE GADTEGKVRA LCAKGRNPDP DRPGTPRVAA ICVYPDLAAV
AVEALRGSGV GVASVATAFP SGRSSREVKL ADVELAVSAG ATEVDMVIDR GAFLSGRYGQ
VFDEIRAVKA ACGDTHLKVI LETGELATYD NVRRASWLAL LAGGDFIKTS TGKVSPAATL
PVTHLMLQAV RDWRDRTGEL RGVKPAGGIR NTKDAIRYLV AVHEVAGPEW LTPELFRFGA
SSLLNDLLMQ RRTQLDGHYS GPDYVAVD
//
