ID C7P3G7_HALMD Unreviewed; 215 AA.
AC C7P3G7;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, 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=Hmuk_1524 {ECO:0000313|EMBL:ACV47639.1};
OS Halomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB
OS 13541) (Haloarcula mukohataei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halomicrobium.
OX NCBI_TaxID=485914 {ECO:0000313|EMBL:ACV47639.1, ECO:0000313|Proteomes:UP000001746};
RN [1] {ECO:0000313|EMBL:ACV47639.1, ECO:0000313|Proteomes:UP000001746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541
RC {ECO:0000313|Proteomes:UP000001746};
RX PubMed=21304667; DOI=10.4056/sigs.42644;
RA Tindall B.J., Schneider S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA Goodwin L., Pitluck S., Mikhailova N., Pati A., Ivanova N., Mavrommatis K.,
RA Chen A., Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Han C., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.,
RA Detter J.C.;
RT "Complete genome sequence of Halomicrobium mukohataei type strain (arg-
RT 2).";
RL Stand. Genomic Sci. 1:270-277(2009).
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; CP001688; ACV47639.1; -; Genomic_DNA.
DR RefSeq; WP_015762484.1; NC_013202.1.
DR AlphaFoldDB; C7P3G7; -.
DR STRING; 485914.Hmuk_1524; -.
DR GeneID; 8411045; -.
DR KEGG; hmu:Hmuk_1524; -.
DR eggNOG; arCOG04320; Archaea.
DR HOGENOM; CLU_053595_0_1_2; -.
DR OrthoDB; 31145at2157; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000001746; 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:ACV47639.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001746};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00114}.
FT ACT_SITE 86
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT ACT_SITE 147
FT /note="Schiff-base intermediate with acetaldehyde"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
FT ACT_SITE 172
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00114"
SQ SEQUENCE 215 AA; 22346 MW; B8ECEB316F4C332D CRC64;
MDTVPERIEH TVLGPTTRWA DVQTVLDEAA QHGLRACIPP CYVERADEYA DVPLSTVVNF
PHGQGATDAV AAEATEAWDD GADEIDVVCN VGQLKAGADA AVEETISEVV AAVPIPVKVI
VEAPLLTDGE KHRAGEIVAE AGAEFCKTAT GFSDGGATVA DVELLSQYRP VKASGGVGSW
ERAKAMFDAG AERIGASSGV TIAEEWRAAE GGEDA
//
