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Database: UniProt
Entry: A0A0A7I4T1_9BIFI
LinkDB: A0A0A7I4T1_9BIFI
Original site: A0A0A7I4T1_9BIFI 
ID   A0A0A7I4T1_9BIFI        Unreviewed;       224 AA.
AC   A0A0A7I4T1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00114};
DE            Short=DERA {ECO:0000256|HAMAP-Rule:MF_00114};
DE            EC=4.1.2.4 {ECO:0000256|HAMAP-Rule:MF_00114};
DE   AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00114};
DE   AltName: Full=Phosphodeoxyriboaldolase {ECO:0000256|HAMAP-Rule:MF_00114};
DE            Short=Deoxyriboaldolase {ECO:0000256|HAMAP-Rule:MF_00114};
GN   Name=deoC {ECO:0000256|HAMAP-Rule:MF_00114};
GN   ORFNames=AH68_02910 {ECO:0000313|EMBL:AIZ14170.1};
OS   Bifidobacterium catenulatum PV20-2.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1447716 {ECO:0000313|EMBL:AIZ14170.1, ECO:0000313|Proteomes:UP000030625};
RN   [1] {ECO:0000313|EMBL:AIZ14170.1, ECO:0000313|Proteomes:UP000030625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PV20-2 {ECO:0000313|EMBL:AIZ14170.1,
RC   ECO:0000313|Proteomes:UP000030625};
RX   PubMed=25614572;
RA   Vazquez-Gutierrez P., Lacroix C., Chassard C., Klumpp J., Jans C.,
RA   Stevens M.J.;
RT   "Complete and Assembled Genome Sequence of Bifidobacterium kashiwanohense
RT   PV20-2, Isolated from the Feces of an Anemic Kenyan Infant.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- FUNCTION: Catalyzes a reversible aldol reaction between acetaldehyde
CC       and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_00114}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_00114};
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. {ECO:0000256|HAMAP-
CC       Rule:MF_00114}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00114}.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 1
CC       subfamily. {ECO:0000256|ARBA:ARBA00010936, ECO:0000256|HAMAP-
CC       Rule:MF_00114}.
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DR   EMBL; CP007456; AIZ14170.1; -; Genomic_DNA.
DR   RefSeq; WP_039197473.1; NZ_CP007456.1.
DR   AlphaFoldDB; A0A0A7I4T1; -.
DR   STRING; 1447716.AH68_02910; -.
DR   KEGG; bka:AH68_02910; -.
DR   HOGENOM; CLU_053595_0_1_11; -.
DR   OrthoDB; 6579831at2; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000030625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProtKB-UniRule.
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   HAMAP; MF_00114; DeoC_type1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011343; DeoC.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR028581; DeoC_typeI.
DR   NCBIfam; TIGR00126; deoC; 1.
DR   PANTHER; PTHR10889:SF1; 2-DEOXY-D-RIBOSE 5-PHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR10889; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00114};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00114};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_00114}.
FT   ACT_SITE        94
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT   ACT_SITE        158
FT                   /note="Schiff-base intermediate with acetaldehyde"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT   ACT_SITE        187
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
SQ   SEQUENCE   224 AA;  23228 MW;  67BA1C5D227713E0 CRC64;
     MNLTQAQLAK YMDHTLLKAS ATADQIDAVV AEAIEYGTAS VCVNPYWVPR VSKALAGSGV
     ATCTVIGFPL GASTTETKVF ETRDAIAKGA DEIDMVINIG ELKAGNDDVV RNDIRAVADA
     THEGGKLLKV IIETALLTDE EKTRASKLTV EGNADYVKTS TGFSTAGATA PDVALMRKAV
     GPDFGVKAAG GIHTLADAYA MIEAGATRLG VSASVAILEE AARQ
//
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