ID A0A0N1H9D2_9EURO Unreviewed; 476 AA.
AC A0A0N1H9D2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:KPI38746.1};
GN ORFNames=AB675_5819 {ECO:0000313|EMBL:KPI38746.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI38746.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI38746.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI38746.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KPI38746.1}.
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DR EMBL; LFJN01000017; KPI38746.1; -; Genomic_DNA.
DR RefSeq; XP_017998709.1; XM_018146058.1.
DR AlphaFoldDB; A0A0N1H9D2; -.
DR STRING; 1664694.A0A0N1H9D2; -.
DR GeneID; 28737938; -.
DR OrthoDB; 216092at2759; -.
DR Proteomes; UP000038010; 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; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR PANTHER; PTHR11699:SF204; ALDEHYDE DEHYDROGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 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:UP000038010}.
FT DOMAIN 20..450
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 254
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 476 AA; 51054 MW; B367B2E60A75A495 CRC64;
MGSVASDTPI ETRLFINGEF VPSKSGKTFE VKNPATLKHV AHVSEASVED VDIAVEAAKA
AFPAWSALAA MERQGWLYKL ADAFDAELSE ISRLEALSMG KPTYQDVSAM GTAIMRYQVG
KAYDIQGETS LHTPGFVNMT FRQPFGVTAG IIPWNVTWLM LIMKMTPALV SGNTMVLKTS
EKSPLSPLIA GKAMKKIGFP KGVFNIVHGF GRPTGEALSK HMEIRKLSFT GSAPTGRLIK
KAAAESNLKN VTLELGGKSP LLIFPDADLS KAVPAAAYSI LMNSGQACIA SSRVYVHESI
AQDFITQMKT AMQSMGKSGD PLAEGTLRGP QADQLQFDRV LSFLDHAKEQ KVPTALGGSK
ESNTGGLYIE PTIFTSVPED SKLMREEIFG PVVCINTFTD EAEVLKRAND TEYGLYGSVF
TRDVSRALRI AKSLEAGTIG INCTSRLLVL ICRLAGSSRV GRGGKGASMS LIIGLS
//