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Database: UniProt
Entry: G1WCC3_9BACT
LinkDB: G1WCC3_9BACT
Original site: G1WCC3_9BACT 
ID   G1WCC3_9BACT            Unreviewed;       309 AA.
AC   G1WCC3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
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=HMPREF9431_01474 {ECO:0000313|EMBL:EGV30693.1};
OS   Segatella oulorum F0390.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Segatella.
OX   NCBI_TaxID=702438 {ECO:0000313|EMBL:EGV30693.1, ECO:0000313|Proteomes:UP000005141};
RN   [1] {ECO:0000313|EMBL:EGV30693.1, ECO:0000313|Proteomes:UP000005141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0390 {ECO:0000313|EMBL:EGV30693.1,
RC   ECO:0000313|Proteomes:UP000005141};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA   Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella oulorum F0390.";
RL   Submitted (JUL-2011) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGV30693.1}.
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DR   EMBL; ADGI01000050; EGV30693.1; -; Genomic_DNA.
DR   RefSeq; WP_004380517.1; NZ_JH114216.1.
DR   AlphaFoldDB; G1WCC3; -.
DR   PATRIC; fig|702438.4.peg.1527; -.
DR   eggNOG; COG0274; Bacteria.
DR   HOGENOM; CLU_053595_3_0_10; -.
DR   OrthoDB; 9778711at2; -.
DR   Proteomes; UP000005141; 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   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:UP000005141}.
SQ   SEQUENCE   309 AA;  34067 MW;  F2243C2B3FD90302 CRC64;
     MKTILPISES TRSDDTQSKY EEMLKLYDTQ VNDADVQAAV AQIVAEKVPQ NNTHEVKKFL
     LGSIELTTLS TTDTEEKVLQ MVEKVNQFDR DYPDLPHVAA ICVYPVFTEL VSNSLEVDGV
     AITNVSGNFP SSQARMEVKV AETQLAIADG ATEIDIVMPV GKFLSEDYEG VCDDINELKQ
     ACGDVPMKVI LETGDLENDS NIMKAALLSM YAGADYIKTS TGKEKVSATP EAAYVMCQAI
     KAYYDKTGIQ IGFKPAGGIN SVMDAITYYT IVKEVLGEKW LTNQWFRMGT SRLTNLLLSE
     ILGTETKFF
//
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