DEOC_AERPE
ID DEOC_AERPE Reviewed; 235 AA.
AC Q9Y948;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-2002, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00114};
DE Short=DERA {ECO:0000255|HAMAP-Rule:MF_00114};
DE EC=4.1.2.4 {ECO:0000255|HAMAP-Rule:MF_00114};
DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00114};
DE AltName: Full=Phosphodeoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00114};
DE Short=Deoxyriboaldolase {ECO:0000255|HAMAP-Rule:MF_00114};
GN Name=deoC {ECO:0000255|HAMAP-Rule:MF_00114}; OrderedLocusNames=APE_2437.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), PROTEIN SEQUENCE OF 2-13, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP BIOTECHNOLOGY.
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=12529358; DOI=10.1074/jbc.m212449200;
RA Sakuraba H., Tsuge H., Shimoya I., Kawakami R., Goda S., Kawarabayasi Y.,
RA Katunuma N., Ago H., Miyano M., Ohshima T.;
RT "The first crystal structure of archaeal aldolase. Unique tetrameric
RT structure of 2-deoxy-D-ribose-5-phosphate aldolase from the
RT hyperthermophilic archaea Aeropyrum pernix.";
RL J. Biol. Chem. 278:10799-10806(2003).
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:0000255|HAMAP-Rule:MF_00114,
CC ECO:0000269|PubMed:12529358}.
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:0000255|HAMAP-Rule:MF_00114,
CC ECO:0000269|PubMed:12529358};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.057 mM for 2-deoxy-D-ribose 5-phosphate
CC {ECO:0000269|PubMed:12529358};
CC pH dependence:
CC Optimum pH is 6.5. Is extremely stable over a wide pH range: upon
CC heating at 50 degrees Celsius for 60 minutes, the enzyme does not
CC lose activity at pH 4.5-11.0. {ECO:0000269|PubMed:12529358};
CC Temperature dependence:
CC Extremely thermostable. Retains full activity upon heating at 100
CC degrees Celsius for 10 minutes and at 80 degrees Celsius for 60
CC minutes. {ECO:0000269|PubMed:12529358};
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:0000255|HAMAP-
CC Rule:MF_00114}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12529358}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00114}.
CC -!- BIOTECHNOLOGY: Its high stability makes the enzyme a potential
CC candidate to be used as a synthetic catalyst in practical application.
CC {ECO:0000269|PubMed:12529358}.
CC -!- MISCELLANEOUS: The enzyme is also highly resistant to organic solvents
CC such as ethanol, methanol, N,N-dimethylformamide, and Me(2)SO at 50
CC degrees Celsius. Loss of activity is not observed in the presence of
CC these reagents even at a concentration as high as 40%.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00114, ECO:0000305}.
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DR EMBL; BA000002; BAA81452.2; -; Genomic_DNA.
DR PIR; D72474; D72474.
DR PDB; 1N7K; X-ray; 2.00 A; A/B=2-235.
DR PDBsum; 1N7K; -.
DR AlphaFoldDB; Q9Y948; -.
DR SMR; Q9Y948; -.
DR STRING; 272557.APE_2437.1; -.
DR EnsemblBacteria; BAA81452; BAA81452; APE_2437.1.
DR KEGG; ape:APE_2437.1; -.
DR PATRIC; fig|272557.25.peg.1618; -.
DR eggNOG; arCOG04320; Archaea.
DR OMA; KQYLDST; -.
DR BRENDA; 4.1.2.4; 171.
DR UniPathway; UPA00002; UER00468.
DR EvolutionaryTrace; Q9Y948; -.
DR Proteomes; UP000002518; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IDA:UniProtKB.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
DR CDD; cd00959; DeoC; 1.
DR Gene3D; 3.20.20.70; -; 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 PANTHER; PTHR10889; PTHR10889; 1.
DR PANTHER; PTHR10889:SF1; PTHR10889:SF1; 1.
DR Pfam; PF01791; DeoC; 1.
DR PIRSF; PIRSF001357; DeoC; 1.
DR SMART; SM01133; DeoC; 1.
DR TIGRFAMs; TIGR00126; deoC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Lyase;
KW Reference proteome; Schiff base.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12529358"
FT CHAIN 2..235
FT /note="Deoxyribose-phosphate aldolase"
FT /id="PRO_0000057286"
FT ACT_SITE 107
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 167
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT ACT_SITE 197
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00114"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:1N7K"
FT HELIX 18..22
FT /evidence="ECO:0007829|PDB:1N7K"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1N7K"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:1N7K"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1N7K"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:1N7K"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:1N7K"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1N7K"
FT HELIX 88..101
FT /evidence="ECO:0007829|PDB:1N7K"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1N7K"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1N7K"
FT HELIX 116..132
FT /evidence="ECO:0007829|PDB:1N7K"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1N7K"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1N7K"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:1N7K"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:1N7K"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1N7K"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:1N7K"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1N7K"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:1N7K"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:1N7K"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:1N7K"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:1N7K"
SQ SEQUENCE 235 AA; 24529 MW; 64CE582A38DCFD38 CRC64;
MPSARDILQQ GLDRLGSPED LASRIDSTLL SPRATEEDVR NLVREASDYG FRCAVLTPVY
TVKISGLAEK LGVKLCSVIG FPLGQAPLEV KLVEAQTVLE AGATELDVVP HLSLGPEAVY
REVSGIVKLA KSYGAVVKVI LEAPLWDDKT LSLLVDSSRR AGADIVKTST GVYTKGGDPV
TVFRLASLAK PLGMGVKASG GIRSGIDAVL AVGAGADIIG TSSAVKVLES FKSLV
