ID   A0A0D2EX05_9EURO        Unreviewed;       673 AA.
AC   A0A0D2EX05;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00044146};
GN   ORFNames=Z517_08566 {ECO:0000313|EMBL:KIW78727.1};
OS   Fonsecaea pedrosoi CBS 271.37.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW78727.1, ECO:0000313|Proteomes:UP000053029};
RN   [1] {ECO:0000313|EMBL:KIW78727.1, ECO:0000313|Proteomes:UP000053029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW78727.1,
RC   ECO:0000313|Proteomes:UP000053029};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL   Submitted (JAN-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}.
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DR   EMBL; KN846973; KIW78727.1; -; Genomic_DNA.
DR   RefSeq; XP_013282535.1; XM_013427081.1.
DR   AlphaFoldDB; A0A0D2EX05; -.
DR   STRING; 1442368.A0A0D2EX05; -.
DR   GeneID; 25308056; -.
DR   VEuPathDB; FungiDB:Z517_08566; -.
DR   HOGENOM; CLU_005391_1_0_1; -.
DR   OrthoDB; 5743at2759; -.
DR   Proteomes; UP000053029; 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; cd07098; ALDH_F15-22; 1.
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: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; PS00070; ALDEHYDE_DEHYDR_CYS; 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:UP000053029};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        615..635
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          107..575
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        339
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   673 AA;  73372 MW;  D3B6F9F9EF917C7A CRC64;
     MLQLVNWATE SWWCLWSSEG HLAIPGVVCL CLIAALTIVI GRRLLSLSRE SAVRFTVRIP
     QELRSWNLED VIAGDDKPQV EACTNLSLAR PGANPCTQVS DGRIYPRCPA DGRRLGPPIT
     PASPSAIDSA VSAAARAQIQ WSQTTFSERR QVLRTLLRYV LDHQEDIVAA CCLDSGKTKI
     DACFGEILVT VEKLQWTIKH GERALRVSKR PSNLLMCYKS NAVVYEPLGV VAACVSWNYP
     FHNFISPVIS ALFAGNAIVV KPSEQTCWST LYFIDIIQGA LRACNHSVDL VQNVICLPEA
     ANYLTSHPGI SHITFIGSRD IAHKVCTSAA KALTPVTVEL GGKDPAIVLD DPKTIRTIDD
     VVSILMRGVF QSAGQNCIGI ERVIALPAIH DKLLAEILPK IKSLRLGSVL LSSPNNPPDM
     GAMISSRSFS RLETLISSAV AQGATLHCGG RRFNHPEYPR GTYFTPTLLS NVTPEMEIAQ
     NELFAPVFLL MKAVGVDDAI RIANSTNYAL GAGVFGHNQR DVQKCVRGVK AGMVAVNDFG
     AYYACSLPFG GVKGSGYGRF GGEEGLRALC NTKAVCEDHW LARSLGIQTR IPPKLQYPVS
     KHGWDVCKGV VGTGYAFTLG LGEWAASVVM LLAALMRKEQ RQQRHTGQWV DGWVGDTSWT
     GAKVENKLRE ERI
//