ID W0HN04_9GAMM Unreviewed; 259 AA.
AC W0HN04;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
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:AHF73565.1};
GN ORFNames=SOPEG_1287 {ECO:0000313|EMBL:AHF73565.1};
OS Candidatus Sodalis pierantonius str. SOPE.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=2342 {ECO:0000313|EMBL:AHF73565.1, ECO:0000313|Proteomes:UP000019025};
RN [1] {ECO:0000313|EMBL:AHF73565.1, ECO:0000313|Proteomes:UP000019025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=none {ECO:0000313|Proteomes:UP000019025};
RX PubMed=24407854; DOI=10.1093/gbe/evt210;
RA Oakeson K.F., Gil R., Clayton A.L., Dunn D.M., von Niederhausern A.C.,
RA Hamil C., Aoyagi A., Duval B., Baca A., Silva F.J., Vallier A.,
RA Jackson D.G., Latorre A., Weiss R.B., Heddi A., Moya A., Dale C.;
RT "Genome degeneration and adaptation in a nascent stage of symbiosis.";
RL Genome Biol. Evol. 6:76-93(2014).
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; CP006568; AHF73565.1; -; Genomic_DNA.
DR RefSeq; WP_025244784.1; NZ_CP006568.1.
DR AlphaFoldDB; W0HN04; -.
DR STRING; 2342.SOPEG_1287; -.
DR KEGG; pes:SOPEG_1287; -.
DR PATRIC; fig|2342.5.peg.1347; -.
DR eggNOG; COG0274; Bacteria.
DR HOGENOM; CLU_053595_3_1_6; -.
DR Proteomes; UP000019025; 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 Lyase {ECO:0000313|EMBL:AHF73565.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019025}.
SQ SEQUENCE 259 AA; 27680 MW; 8EE4DFA6C17E2F29 CRC64;
MNQLTLAAQR ALSLMDLTTL NDDDTDEKVI ALCRQAHTSV GETAAVCLYP RFIPLAWQTL
NAQGSTAVRI ATVTNFPHGN DCLDITLAET RAAIAYGADE VDIVFPYRAL IAGNEQIGLE
MVKQASELCH ASQVLLKVII ESGELRRADL IRRASQIAIA GDADFIKTST GKVPVNATLE
NAGIMLNVIA EEGVGDRVGF KAAGGVRTAE EAAAYLALAD EIMGEGWVNP RHFRFGASSL
LGSLLTVLRQ EAPPAKNGY
//
