ID A0A166HA27_9MICO Unreviewed; 241 AA.
AC A0A166HA27;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=deoC2 {ECO:0000313|EMBL:KZX20225.1};
GN Synonyms=deoC {ECO:0000256|HAMAP-Rule:MF_00114};
GN ORFNames=ACH61_02654 {ECO:0000313|EMBL:KZX20225.1}, EV639_106152
GN {ECO:0000313|EMBL:TCO36749.1};
OS Rathayibacter tanaceti.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=1671680 {ECO:0000313|EMBL:KZX20225.1, ECO:0000313|Proteomes:UP000076717};
RN [1] {ECO:0000313|EMBL:TCO36749.1, ECO:0000313|Proteomes:UP000295366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2596 {ECO:0000313|EMBL:TCO36749.1,
RC ECO:0000313|Proteomes:UP000295366};
RX PubMed=26203337; DOI=.1186/s40793-015-0017-x;
RA Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA Kyrpides N.C.;
RT "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT the genomes of soil and plant-associated and newly described type
RT strains.";
RL Stand. Genomic Sci. 10:26-26(2015).
RN [2] {ECO:0000313|EMBL:KZX20225.1, ECO:0000313|Proteomes:UP000076717}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2596 {ECO:0000313|EMBL:KZX20225.1,
RC ECO:0000313|Proteomes:UP000076717};
RA Vasilenko O.V., Starodumova I.P., Tarlachkov S.V., Dorofeeva L.V.,
RA Evtushenko L.I.;
RT "Draft Genome Sequence of Rathayibacter sp. Strain VKM Ac-2596 Isolated
RT from Leaf Gall Induced by Plant-Parasitic Nematodes.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:TCO36749.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VKM Ac-2596 {ECO:0000313|EMBL:TCO36749.1};
RA Whitman W., Huntemann M., Clum A., Pillay M., Palaniappan K., Varghese N.,
RA Mikhailova N., Stamatis D., Reddy T., Daum C., Shapiro N., Ivanova N.,
RA Kyrpides N., Woyke T.;
RL Submitted (MAR-2019) 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}.
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:KZX20225.1}.
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DR EMBL; LIIN01000120; KZX20225.1; -; Genomic_DNA.
DR EMBL; SLWP01000006; TCO36749.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166HA27; -.
DR PATRIC; fig|1671680.3.peg.2850; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000076717; Unassembled WGS sequence.
DR Proteomes; UP000295366; Unassembled WGS sequence.
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:KZX20225.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076717};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00114}.
FT ACT_SITE 98
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT ACT_SITE 160
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT ACT_SITE 189
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
SQ SEQUENCE 241 AA; 24874 MW; FFFEAAEF38EE5501 CRC64;
MTESSLPSVA EVAALIDHAI LKPEFTRAEV DAQLDEARAA GVFSVCVRPS DIAHSVARLE
GSGVLVGTVI GFPHGTTSTP AKVAEARQAL ADGASELDMV VNIGRLRSGL LEDVEDDIRA
VVEAAEGRIV KVILETGLLD DEQIVEGSRA SERAGADFVK TATGFAGSGA NEHDLRLMRG
AVSDAVQVKA SGGVRDLDTL LAYRALGVTR FGTSGSATIL GDLSARLAGD SSAARVDSAS
Y
//
