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Database: UniProt
Entry: A0A024TGJ4_9STRA
LinkDB: A0A024TGJ4_9STRA
Original site: A0A024TGJ4_9STRA 
ID   A0A024TGJ4_9STRA        Unreviewed;       510 AA.
AC   A0A024TGJ4;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   ORFNames=H310_13140 {ECO:0000313|EMBL:ETV92711.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV92711.1};
RN   [1] {ECO:0000313|EMBL:ETV92711.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETV92711.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
CC       ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; KI913998; ETV92711.1; -; Genomic_DNA.
DR   RefSeq; XP_008878747.1; XM_008880525.1.
DR   AlphaFoldDB; A0A024TGJ4; -.
DR   STRING; 157072.A0A024TGJ4; -.
DR   EnsemblFungi; H310_13140-t26_1; H310_13140-t26_1-p1; H310_13140.
DR   EnsemblProtists; ETV92711; ETV92711; H310_13140.
DR   GeneID; 20090190; -.
DR   VEuPathDB; FungiDB:H310_13140; -.
DR   eggNOG; KOG2456; Eukaryota.
DR   OrthoDB; 606537at2759; -.
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   CDD; cd07087; ALDH_F3-13-14_CALDH-like; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
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   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR036492,
KW   ECO:0000256|RuleBase:RU003345}.
FT   DOMAIN          9..444
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        219
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        253
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ   SEQUENCE   510 AA;  55631 MW;  E355768C965AC429 CRC64;
     MASNETAVAA ISKDVAALRA SFGADRTRPL KFRKRQLQFL RQMLVDHEAT LSNSLQTDMR
     KDPHDVYLFE IGPILYEIQL HMDYLDDWAA SRSVAVNAPC LPGQSWVVPE PLGVVLIFGT
     WNYPLNVTLL PLVGAISAGN CVFIRLPAEG STDATNALLA RLLAVYMDPD VVRFASGGLD
     VSKETLAQRY DLIFCTGSER IGKIIARAAA ETLTPVVLEL GGKSPTIVDA TVNLELAAKR
     IAWGAFSNAG QTCVRPDHVF VESSIGDAFV AALKVETAAL YGANAKDSRE YARLGNALHF
     DKIKRIVDQD AAFVVHGGST DATDRYIAPT IVNFKSNTAA FDASAAMADE IFGPVLPVVY
     YDSLSTVVAR IKRSPKPLAL YLFTTNKSVM DSVVQRTSSG GVCINDTMLQ IGNFNLPFGG
     VGASGMGRYH GKYSFDTFSH EKAVMRKSFW LDLPQRYPPF TSSAVKFVRL VMTPVPRSLL
     RLSWWVAVVL VLLWTAQQPK AQRALAALMS
//
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