ID A0A151GJA6_9HYPO Unreviewed; 488 AA.
AC A0A151GJA6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:KYK57168.1};
GN ORFNames=DCS_04175 {ECO:0000313|EMBL:KYK57168.1};
OS Drechmeria coniospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK57168.1, ECO:0000313|Proteomes:UP000076580};
RN [1] {ECO:0000313|EMBL:KYK57168.1, ECO:0000313|Proteomes:UP000076580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK57168.1,
RC ECO:0000313|Proteomes:UP000076580};
RX PubMed=26975455; DOI=10.1038/srep23122;
RA Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA Molnar I., Lin M.;
RT "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL Sci. Rep. 6:23122-23122(2016).
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:KYK57168.1}.
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DR EMBL; LAYC01000002; KYK57168.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151GJA6; -.
DR STRING; 98403.A0A151GJA6; -.
DR InParanoid; A0A151GJA6; -.
DR OrthoDB; 216092at2759; -.
DR Proteomes; UP000076580; Chromosome 02.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd07106; ALDH_AldA-AAD23400; 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; IPR044086; LUC3-like.
DR PANTHER; PTHR11699:SF263; ALDEHYDE DEHYDROGENASE DOMAIN-CONTAINING PROTEIN-RELATED; 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:UP000076580}.
FT DOMAIN 29..478
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 255
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 488 AA; 54365 MW; 7D1C63B826C23EAD CRC64;
MDITVGPPPP PPPKRPSHLP RQSWQFVASE RTRHSIDPAT GEALYEVPVA TRDDLDLAVQ
HAREAFTAWS KTAFAERSRL LLAFADAIEQ NRHELEQLLT MEQGKPLSLS HQELDMTLAW
LRTFATMEVK EEVVEDVEER TIYATFPPLG VCGAIIPWNW PILLGMGKVG PALMTGNVMI
VKPSPFTPYC DLKLGELGMS IFPPGVFQVL SGHDELGPWM TEHGGIDMIS FTGSIPTGKR
VAASCAKTLK RYVLELGGND AAVVCEDVDV AKCVPKIAMS SFLNSGQICM LTKRIYVHEE
IYDQFRDAMV EFTRAKVKTG AGFEPDVVVG PVQNRIQFDL VKDMYSQIDA CRWRTALRGE
VRSSSKGYFI EPAIIDNPPE DSRIVVEEPF GPIVPLLRWT DEDDVLRRAN GLRTGLGASV
WSRDVERAER MARQLSAGSV WVNSHFDVAP HVPFGGHKES GVGVEWGIEG FKQYTNSTSL
WVWKKVFD
//
