ID A0A0V1NQJ7_9BILA Unreviewed; 904 AA.
AC A0A0V1NQJ7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 Name=F09E5.3 {ECO:0000313|EMBL:KRZ86067.1};
GN ORFNames=T08_6525 {ECO:0000313|EMBL:KRZ86067.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ86067.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ86067.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ86067.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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}.
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:KRZ86067.1}.
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DR EMBL; JYDM01000127; KRZ86067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1NQJ7; -.
DR STRING; 92180.A0A0V1NQJ7; -.
DR UniPathway; UPA00002; UER00468.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011343; DeoC.
DR InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10889; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR10889:SF3; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR Pfam; PF01791; DeoC; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SMART; SM01133; DeoC; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054924}.
FT DOMAIN 768..862
FT /note="Methyltransferase type 11"
FT /evidence="ECO:0000259|Pfam:PF08241"
FT REGION 91..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 904 AA; 101585 MW; E1A49F5391A77F8E CRC64;
MGSPCDYLSA SLASFQRPIC QKKFKNIPPE HDKRVNSRCL RTRHAPSSGS SSEVTSMLNI
GSENEKMQHH RRRAAKVYQN SQLRCQNLVS NRNHNGASSA TTSTNKHKTA PQNCKNSKVS
SKIDFRTKQS PLNRSTSVVD NCSSNDGRSR TATMGSPTSR NLTVSRPANR IPNSTKNHLR
PNGHNDCAIF KSQSLTSLTG QRNLPQTVPS TSIVELESAK QISQSEQHLA IDNSTVDDEH
LKPDKSKLSL LTNHAEVEEF KRDPTTSKNV EEPVVEIFKQ FNVEDRTNEE SVDKNSRSDE
DNTSVSVSAT TKSNSIATSD SQDKSTVATN DTKIEVDSYL IPWLLDNVSM VVKYRLNTIL
LRDAICGTTS FVKESGDLSN ITYGSEVLYN LGYYMKSIAE EAERINTEEK IDIIKKLISF
TDLTSLNATD SLETVKKLID RATQPLALSL LNDSETCCAS VCIYPYYVKD AVAFRNFACA
LGRSFVSIVT VAGAFPSGMY KLITKVHECR EAKEDGADEI DVVINRGLVA TRNWRELYKE
LVAMRKEIAS PILMKTILST GDIASPNDIY AAATVAMMAG MKFIHQIFHW QREAQFYSTR
EFSDLFGNSV VGFKAAGGIK TAQEAIVYYV LVKQILGERW LSREYFRIGA SELLDDLVRT
LEKLQFGKES SSYLHDAREM QHYRPTFSNI HIRKKMKKQQ QSCSNESVGN FNCFLDPNYK
DTNEVIKYYS AMATNYDTII DNGYYRGPKI VANSVNDIIE DKNALLIDIC GGTGSTALEL
RKYGFQNIDC IDACEGMLEI AKQKSAYSNC ICELLLPGKQ STLNAEKYDC VFCVGSFAPG
HLQPEVVDEF IRILKNEGYC VIGMREEWLY TADDYRDKLE PYMFKLKKWR LIKRESDSQK
IRSP
//
