ID W2TT68_NECAM Unreviewed; 278 AA.
AC W2TT68;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=NECAME_06663 {ECO:0000313|EMBL:ETN84859.1};
OS Necator americanus (Human hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Ancylostomatoidea; Ancylostomatidae; Bunostominae; Necator.
OX NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN84859.1, ECO:0000313|Proteomes:UP000053676};
RN [1] {ECO:0000313|Proteomes:UP000053676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24441737; DOI=10.1038/ng.2875;
RA Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT "Genome of the human hookworm Necator americanus.";
RL Nat. Genet. 46:261-269(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; KI657850; ETN84859.1; -; Genomic_DNA.
DR RefSeq; XP_013307086.1; XM_013451632.1.
DR AlphaFoldDB; W2TT68; -.
DR STRING; 51031.W2TT68; -.
DR EnsemblMetazoa; NECAME_06663; NECAME_06663; NECAME_06663.
DR GeneID; 25346695; -.
DR KEGG; nai:NECAME_06663; -.
DR CTD; 25346695; -.
DR OMA; RYSGPDY; -.
DR OrthoDB; 1330179at2759; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000053676; 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 GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
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 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:UP000053676};
KW Schiff base {ECO:0000256|PIRSR:PIRSR001357-50}.
FT ACT_SITE 214
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000256|PIRSR:PIRSR001357-50"
FT ACT_SITE 231
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001357-50"
SQ SEQUENCE 278 AA; 29661 MW; 5066A58AFB28386A CRC64;
MGAFSQAEFD KEVSRDFNTQ EISSAIARYE KEAAALLKDK AQVRKVISYI DLTTLSGDDT
KGRVVALVDR ALNPIPDDSS VTCAAVCVYP QRVADVTKHL TAKQKTLNVA SVAAGFPSGQ
YHLQSKLLEV QLTVADGATE IDIVISRAAA LEGDWKNGEV LKFGLAVHDE VAALKGVCGN
AHMKTILATG ELKTLTNIYK GSWASILAGS DFIKTSTGKE CTNATLEVGF KPAGGIKTPE
EALAYIVLVK DVLGESWLSP ELFRIGASSL LDNCLKAI
//