ID A0A1P8UUF2_9RHOB Unreviewed; 331 AA.
AC A0A1P8UUF2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=deoxyribose-phosphate aldolase {ECO:0000256|ARBA:ARBA00012515};
DE EC=4.1.2.4 {ECO:0000256|ARBA:ARBA00012515};
DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000256|ARBA:ARBA00032755};
DE AltName: Full=Phosphodeoxyriboaldolase {ECO:0000256|ARBA:ARBA00031814};
GN ORFNames=Ga0080574_TMP2690 {ECO:0000313|EMBL:APZ53024.1};
OS Salipiger abyssi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1250539 {ECO:0000313|EMBL:APZ53024.1, ECO:0000313|Proteomes:UP000187059};
RN [1] {ECO:0000313|EMBL:APZ53024.1, ECO:0000313|Proteomes:UP000187059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT2014 {ECO:0000313|EMBL:APZ53024.1,
RC ECO:0000313|Proteomes:UP000187059};
RA Tang K.;
RT "Deep-sea bacteria in the southern Pacific.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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};
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.
CC {ECO:0000256|ARBA:ARBA00004816}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00009473}.
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DR EMBL; CP015093; APZ53024.1; -; Genomic_DNA.
DR RefSeq; WP_076700088.1; NZ_CP015093.1.
DR AlphaFoldDB; A0A1P8UUF2; -.
DR STRING; 1250539.Ga0080574_TMP2690; -.
DR KEGG; paby:Ga0080574_TMP2690; -.
DR OrthoDB; 6579831at2; -.
DR Proteomes; UP000187059; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR CDD; cd00959; DeoC; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011343; DeoC.
DR InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR NCBIfam; TIGR00126; deoC; 1.
DR PANTHER; PTHR10889; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR10889:SF3; 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 Lyase {ECO:0000313|EMBL:APZ53024.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000187059}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 331 AA; 35686 MW; 1FB9E26A99E4AB0B CRC64;
MAETTEAPRS VTHLPQAMEP RNPGMALDMD WVLRARANRS AIERRAATLP GRRSVKKDFQ
AAWLARAISC IDLTTLSGDD TPGRVARLCA KAKRPVRADL LDALGLPDLT VGAVCVYHDM
IAPAVAALDG SGIPVAAVST GFPAGLSPFP LRLAEIGESV KAGAREIDIV ISRRLVLTGD
WQGLYDEMRQ FRAACGEAHV KAILATGELG TLQNVARASL VCMMAGADFI KTSTGKESVN
ATLPVSLVMI RAIRDYYEAT GYRVGYKPAG GISKAKDSLN YLALIKEELG DRWLRPDLFR
FGASSLLGDI ERQLEHRVTG AYSASWRHAL G
//
