ID D5U0M9_THEAM Unreviewed; 237 AA.
AC D5U0M9;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
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 OrderedLocusNames=Tagg_0404 {ECO:0000313|EMBL:ADG90679.1};
OS Thermosphaera aggregans (strain DSM 11486 / M11TL).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Thermosphaera.
OX NCBI_TaxID=633148 {ECO:0000313|EMBL:ADG90679.1, ECO:0000313|Proteomes:UP000002376};
RN [1] {ECO:0000313|EMBL:ADG90679.1, ECO:0000313|Proteomes:UP000002376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11486 / M11TL {ECO:0000313|Proteomes:UP000002376};
RX PubMed=21304709;
RA Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A.,
RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA Detter J.C., Tapia R., Han C., Heimerl T., Weikl F., Brambilla E.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Thermosphaera aggregans type strain (M11TL).";
RL Stand. Genomic Sci. 2:245-259(2010).
RN [2] {ECO:0000313|Proteomes:UP000002376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11486 / M11TL {ECO:0000313|Proteomes:UP000002376};
RX DOI=10.4056/sigs.821804;
RA Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A.,
RA Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.C., Brettin T.,
RA Detter J.C., Tapia R., Han C., Heimerl T., Weikl F., Brambilla E.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.-P.;
RT "Complete genome sequence of Thermosphaera aggregans type strain
RT (M11TLT).";
RL Stand. Genomic Sci. 2:245-259(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 11486;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Spring S., Lapidus A., Munk C., Schroeder M., Glavina Del Rio T., Tice H.,
RA Copeland A., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.-J.,
RA Jeffries C.C., Brettin T., Detter J.C., Tapia R., Han C., Chain P.,
RA Heimerl T., Weik F., Goker M., Rachel R., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.;
RT "Complete genome sequence of Thermosphaera aggregans type strain (M11TL).";
RL Submitted (FEB-2010) 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; CP001939; ADG90679.1; -; Genomic_DNA.
DR RefSeq; WP_013129272.1; NC_014160.1.
DR AlphaFoldDB; D5U0M9; -.
DR STRING; 633148.Tagg_0404; -.
DR GeneID; 9165418; -.
DR KEGG; tag:Tagg_0404; -.
DR eggNOG; arCOG04320; Archaea.
DR HOGENOM; CLU_053595_0_2_2; -.
DR OrthoDB; 31145at2157; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000002376; 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:ADG90679.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002376};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00114}.
FT ACT_SITE 102
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT ACT_SITE 167
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT ACT_SITE 196
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
SQ SEQUENCE 237 AA; 25459 MW; A24F5ECCA4C373C6 CRC64;
MKGFYSGRIE SITPTEFASM IDHTLLKPDA DYKILEKYIN DVREHGFKLL MLPLSLLDKA
LEIAGRTIKY GVVVGFPLGN TSTKVKVFEA VEAASSGASE VDMVMNISLF KSREYARVLE
DISTVVAEAK KKGVESVKVI LETTLLDDSE KIKAVELVSS AGADFVKTNT GFLGGGATVH
DVALLYRASQ GRIKVKASGG IRHALDALAL IEAGASRIGT SSGDKLMKEF LELTGEA
//
