ID G9N8Q0_HYPVG Unreviewed; 496 AA.
AC G9N8Q0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171};
GN ORFNames=TRIVIDRAFT_75875 {ECO:0000313|EMBL:EHK17355.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK17355.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK17355.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00024149};
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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:EHK17355.1}.
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DR EMBL; ABDF02000089; EHK17355.1; -; Genomic_DNA.
DR RefSeq; XP_013951548.1; XM_014096073.1.
DR AlphaFoldDB; G9N8Q0; -.
DR STRING; 413071.G9N8Q0; -.
DR EnsemblFungi; EHK17355; EHK17355; TRIVIDRAFT_75875.
DR GeneID; 25797792; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_75875; -.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_1_1; -.
DR InParanoid; G9N8Q0; -.
DR OMA; FGIFWNQ; -.
DR OrthoDB; 216092at2759; -.
DR Proteomes; UP000007115; Unassembled WGS sequence.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
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 PANTHER; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000007115}.
FT DOMAIN 27..488
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 263
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 496 AA; 53711 MW; 33FE22C408FA62B9 CRC64;
MTAAFKISLP NGLNYDQPTG LFIDNEYVPA NGEKFTVYNP TTDEEIITLQ GASEEDVDKA
VAAARRAFDG EWSELEAVER GALLYKLAEL IDRDRKLLAS IDSFDNGKSF SDAYGGDLLE
SYNVFRYYAG AADKITGKTI ETSHKKLAYV LQEPLGVCGQ IIPWNYPFMM LAWKVAPALA
CGNTIVLKPA EQTPLSALYF GKLIVEAGFP PGVVNIIPGL GYISGKALAG HMDVDKIAFT
GSTATGRSIM KSAASNLKNI TLECGGKSPS IVFEDADLDQ AVKWCHSGIM DNMGQVCTST
SRIYVQDTIY DEFLAKFTEK TKEAATKIGD PFHEDTYQGP QVSKAQFDKV LSYIDEGKKS
GARVLHGGAK HGDKGYFIQP TVFADTTEDM KIVKEEIFGP VVAISKFSTE AEVIAKANDT
SYGLAAAVFT QKVTKAHKVA RKIQAGMVFI NSSGDSHFGI PFGGYKSSGI GRELGQYALD
AYTQSKAVHV NLGTEL
//
