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Database: UniProt
Entry: W9Y2W6_9EURO
LinkDB: W9Y2W6_9EURO
Original site: W9Y2W6_9EURO 
ID   W9Y2W6_9EURO            Unreviewed;       476 AA.
AC   W9Y2W6;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=NAD-dependent aldehyde dehydrogenase {ECO:0000313|EMBL:EXJ76814.1};
GN   ORFNames=A1O5_01322 {ECO:0000313|EMBL:EXJ76814.1};
OS   Cladophialophora psammophila CBS 110553.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ76814.1, ECO:0000313|Proteomes:UP000019471};
RN   [1] {ECO:0000313|EMBL:EXJ76814.1, ECO:0000313|Proteomes:UP000019471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ76814.1,
RC   ECO:0000313|Proteomes:UP000019471};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL   Submitted (MAR-2013) 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:EXJ76814.1}.
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DR   EMBL; AMGX01000001; EXJ76814.1; -; Genomic_DNA.
DR   RefSeq; XP_007740131.1; XM_007741941.1.
DR   AlphaFoldDB; W9Y2W6; -.
DR   STRING; 1182543.W9Y2W6; -.
DR   GeneID; 19186058; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   HOGENOM; CLU_005391_1_0_1; -.
DR   OrthoDB; 178592at2759; -.
DR   Proteomes; UP000019471; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd07102; ALDH_EDX86601; 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   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   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019471};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        131..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..468
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        240
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   476 AA;  51924 MW;  EB08BB6507226061 CRC64;
     MVAEIITTIS PTTNEPILTR HGKSPEEILR LGTTAQSAFK SYRKSHPSLE SRQQIISKAL
     NLLLERQDAL ARELTEQMGR PISYTAKEIT TAVKRAEYMI RVAPEVLERD ATIPGEQEQG
     FKRYITRKEP VGVVLVIFAW NYPYLILVNS LIPALLAGCA VILKPSPQTP TIVEHIVDIF
     DAAGLPQKVI QYLHCGSPTD LKPLILSPEV NHICFTGSVA AGIAIQTLAA SRVSCSVGLE
     LGGKDPAYIR PDVDAAWAAE EIVDGAIFNS GQSCCAIERV YVHADIYDSF LKEVKKVLEG
     YRVGDPLEKS THVGPVVSKR SKEAIEKQVA DAIAAGAVDQ TPHNESFKSP AGPKAGNWVA
     PVLLTNVNHN MSIMRDETFG PVIPLQKVSG DEEAIALMND SQFGLTASIW TKDTPKGEEL
     CGLVQAGTVF VNRADFPSPD LAWTGWKDSG RGVTLSKLAF EQFVKVKSFH VKNYPK
//
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