ID A0A249LEF3_9ACTN Unreviewed; 314 AA.
AC A0A249LEF3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 ORFNames=PHILAsVB114_01620 {ECO:0000313|EMBL:ASY27377.1};
OS Candidatus Planktophila limnetica.
OC Bacteria; Actinomycetota; Actinomycetes; Candidatus Nanopelagicales;
OC Candidatus Nanopelagicaceae; Planktophila.
OX NCBI_TaxID=573600 {ECO:0000313|EMBL:ASY27377.1, ECO:0000313|Proteomes:UP000217221};
RN [1] {ECO:0000313|EMBL:ASY27377.1, ECO:0000313|Proteomes:UP000217221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-VB-114 {ECO:0000313|EMBL:ASY27377.1};
RA Neuenschwander S.M., Salcher M., Ghai R., Pernthaler J.;
RT "High microdiversification within the ubiquitous acI lineage of
RT Actinobacteria.";
RL Submitted (JUL-2016) 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; CP016782; ASY27377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A249LEF3; -.
DR KEGG; plim:PHILAsVB114_01620; -.
DR OrthoDB; 6579831at2; -.
DR Proteomes; UP000217221; Chromosome.
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 PIRSF; PIRSF001357; DeoC; 1.
DR SMART; SM01133; DeoC; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000217221}.
SQ SEQUENCE 314 AA; 33586 MW; E21E228B6FC27DD7 CRC64;
MYYGLTDGTD TSLRKFLTDL PGVDAVGADS RAAMLATRSI KTTSKRWAID TAISMVDLTT
LEGADTQGKV QALCAKAVRP DPTDLSVPSV GAVCVYNDMV SIARTHLDLI GGTHVPVAAV
STAFPSGRAS MEVKIQDTKD AIAAGAAEID MVIDRGAFLS GKYIEVFNEI VAIKEICGDK
AHLKVIFETG ELVTYDNVRK ASYLAMLAGA DFIKTSTGKI APAATPPVVL VMLEAVRDFY
EMAGVRIGVK PAGGIRNTKD AIKQLVLVNE TAGPEWLTPK LFRIGASALL NDLLMQRMKM
DDGYYASPQY VTID
//
