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Database: UniProt
Entry: A0A0P9E737_9ARCH
LinkDB: A0A0P9E737_9ARCH
Original site: A0A0P9E737_9ARCH 
ID   A0A0P9E737_9ARCH        Unreviewed;       287 AA.
AC   A0A0P9E737;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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:KPV62616.1};
GN   ORFNames=AOA65_1743 {ECO:0000313|EMBL:KPV62616.1};
OS   Candidatus Bathyarchaeota archaeon BA1.
OC   Archaea; Candidatus Bathyarchaeota.
OX   NCBI_TaxID=1700835 {ECO:0000313|EMBL:KPV62616.1, ECO:0000313|Proteomes:UP000050312};
RN   [1] {ECO:0000313|EMBL:KPV62616.1, ECO:0000313|Proteomes:UP000050312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BA1 {ECO:0000313|EMBL:KPV62616.1};
RX   PubMed=26494757; DOI=10.1126/science.aac7745;
RA   Evans P.N., Parks D.H., Chadwick G.L., Robbins S.J., Orphan V.J.,
RA   Golding S.D., Tyson G.W.;
RT   "Methane metabolism in the archaeal phylum Bathyarchaeota revealed by
RT   genome-centric metagenomics.";
RL   Science 350:434-438(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}.
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:KPV62616.1}.
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DR   EMBL; LIHJ01000073; KPV62616.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P9E737; -.
DR   STRING; 1700835.AOA65_1743; -.
DR   KEGG; barc:AOA65_1743; -.
DR   PATRIC; fig|1700835.3.peg.2529; -.
DR   UniPathway; UPA00002; UER00468.
DR   Proteomes; UP000050312; 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:SF1; 2-DEOXY-D-RIBOSE 5-PHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR10889; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR   Pfam; PF01791; 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        107
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT   ACT_SITE        169
FT                   /note="Schiff-base intermediate with acetaldehyde"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT   ACT_SITE        198
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
SQ   SEQUENCE   287 AA;  31476 MW;  F38F2CF4A5E7B07D CRC64;
     MNRYGCVGEM KVDTTITKEK LAKMIDHTLL EPSATYEKIE RLCEEAMAYG FASVCVNPFH
     VSRAAKLLCG SGVKVCCVVG FPLGASTPEV KALETRNAIE NGAQEVDMVI NIGALRSRDY
     DLVKKDIEAV VEAAHGSTVK VIIETGFLTD EEKVKACELA RGAGAHFVKT STGFGPMGAL
     PSDVRLMRKT VGDGMGVKAA GGITDFRSAL RLIEAGANRL GTSASTPIIE GLEWMKFSRS
     WFIEEIPCKI CPSRHASLAK QPKEVFLYYK DRCKTCPDRE YNRFYEK
//
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