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Database: UniProt
Entry: A0A068Y814_ECHMU
LinkDB: A0A068Y814_ECHMU
Original site: A0A068Y814_ECHMU 
ID   A0A068Y814_ECHMU        Unreviewed;       336 AA.
AC   A0A068Y814;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Aldehyde dehydrogenase family 3 member B1 {ECO:0000313|EMBL:CUT98793.1};
OS   Echinococcus multilocularis (Fox tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX   NCBI_TaxID=6211 {ECO:0000313|EMBL:CUT98793.1};
RN   [1] {ECO:0000313|EMBL:CUT98793.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23485966; DOI=10.1038/nature12031;
RA   Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA   Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA   Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA   De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA   Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA   Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA   Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA   Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA   Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA   Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA   Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA   Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA   Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT   "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL   Nature 496:57-63(2013).
RN   [2] {ECO:0000313|EMBL:CUT98793.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986}.
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DR   EMBL; LN902845; CUT98793.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068Y814; -.
DR   STRING; 6211.A0A068Y814; -.
DR   eggNOG; KOG2456; Eukaryota.
DR   OMA; MQFYGSD; -.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
PE   3: Inferred from homology;
FT   DOMAIN          4..306
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   336 AA;  37612 MW;  7FBD893B14F8F533 CRC64;
     MIPLAGAIAA GNCVIIKPAE LATATNQLFV EQIPKYFGRS VCQVLTGTLE DTKDFLREYS
     CDFIYFTGAS NDGIYIAREA AKTLTPVFFN LYGKCPVYVD SSADITLAAM RVMWGKIFNC
     GQMSAAPDYV LCHADVQPKF LKECRNALDY FFGGLPKIDT KNYGRIISME HTERLKEMIF
     KTEGKLVLGG YVHVPAKFVQ PTVFCDVPEY DILMQFEIFG PILPVITVNS PEEALEYVSN
     QKKPQAVYVF SSKKDVFRTW KKHTESDGII QNDVVMMKGT KMTFGGVEAS GLGRYRGKSS
     IELFSHRRGV ILRSIKDDTD CKMRYPPSHS ASPIQT
//
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