ID A0A175ACI8_CLOIN Unreviewed; 239 AA.
AC A0A175ACI8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
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 ECO:0000313|EMBL:MZH60762.1};
GN ORFNames=ADH65_01840 {ECO:0000313|EMBL:ASU17329.1}, GT649_12380
GN {ECO:0000313|EMBL:MZH60762.1}, I5Q87_18905
GN {ECO:0000313|EMBL:QQR25883.1};
OS Clostridium innocuum.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=1522 {ECO:0000313|EMBL:MZH60762.1, ECO:0000313|Proteomes:UP000478871};
RN [1] {ECO:0000313|EMBL:ASU17329.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I46 {ECO:0000313|EMBL:ASU17329.1};
RX PubMed=29051233;
RA Garzetti D., Brugiroux S., Bunk B., Pukall R., McCoy K.D., Macpherson A.J.,
RA Stecher B.;
RT "High-Quality Whole-Genome Sequences of the Oligo-Mouse-Microbiota
RT Bacterial Community.";
RL Genome Announc. 5:e00758-17(2017).
RN [2] {ECO:0000313|Proteomes:UP000214713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I46 {ECO:0000313|Proteomes:UP000214713};
RA Garzetti D.;
RT "High-quality whole genome sequences of the Oligo-Mouse-Microbiota.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:MZH60762.1, ECO:0000313|Proteomes:UP000478871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A13 {ECO:0000313|EMBL:MZH60762.1,
RC ECO:0000313|Proteomes:UP000478871};
RX PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
RN [4] {ECO:0000313|EMBL:QQR25883.1, ECO:0000313|Proteomes:UP000595712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I46 {ECO:0000313|EMBL:QQR25883.1,
RC ECO:0000313|Proteomes:UP000595712};
RA Marbouty M., Lamy-Besnier Q., Debarbieux L., Koszul R.;
RT "Closed and high quality bacterial genomes of the OMM12 community.";
RL Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases.
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; CP022722; ASU17329.1; -; Genomic_DNA.
DR EMBL; WWTM01000024; MZH60762.1; -; Genomic_DNA.
DR EMBL; CP065320; QQR25883.1; -; Genomic_DNA.
DR RefSeq; WP_008817578.1; NZ_WWTY01000056.1.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000214713; Chromosome.
DR Proteomes; UP000478871; Unassembled WGS sequence.
DR Proteomes; UP000595712; 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; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR10889:SF1; 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, ECO:0000313|EMBL:MZH60762.1};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00114}.
FT ACT_SITE 95
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT ACT_SITE 159
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT ACT_SITE 188
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
SQ SEQUENCE 239 AA; 26351 MW; 404C9C291BEC8DBA CRC64;
MKRWTVEELA RMIDHTYVKA DATRKQMEKL CKEAREYHFA MAAINSSQTA LCAEYLRDSD
IHVGAAIGFP LGQTTIAAKV FEAEDAIQNG ADEIDYMINL TEVKAGNWEY VKEEMQQIVT
VCRNNGKLCK VILETCYLTK DEIKQMCKIA VAVKPDFVKT STGFGSAGAT AEDVALMRRC
VGTAVKVKAS GGIRDARTFK KMVSSGALRI GTSAGVSIVR ELQTEAFKHS GYIAIPEEY
//
