ID A0A0D2G736_9EURO Unreviewed; 491 AA.
AC A0A0D2G736;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Unplaced genomic scaffold supercont1.7, whole genome shotgun sequence {ECO:0000313|EMBL:KIW76448.1};
GN ORFNames=Z517_11194 {ECO:0000313|EMBL:KIW76448.1};
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:KIW76448.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW76448.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW76448.1,
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; KN846975; KIW76448.1; -; Genomic_DNA.
DR RefSeq; XP_013280256.1; XM_013424802.1.
DR AlphaFoldDB; A0A0D2G736; -.
DR STRING; 1442368.A0A0D2G736; -.
DR GeneID; 25310684; -.
DR VEuPathDB; FungiDB:Z517_11194; -.
DR HOGENOM; CLU_005391_0_0_1; -.
DR OrthoDB; 216092at2759; -.
DR Proteomes; UP000053029; 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:UP000053029}.
FT DOMAIN 23..486
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 320..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 258
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 491 AA; 52430 MW; 7EFB1A0A2BE23A89 CRC64;
MVSDAGVPDV GDVETRLFIN NEFVEAKDGK TFPVINPATE EIFQHVSEAS AADVDLAVSA
AEAAFPAWSA LGGFQRAAYF YKLADLVEQS NSKLALIEAS SMGRPVGTYT EGLASARFLR
YMAGKATDVQ GTSSTQTPGF LNLTLREPYG VCAAITPWNA PVTMLMFKMA PALIAGNTLV
VKSSEKAPLT SLYVASLARA AGFPPGVLNV LSGFGTPCGA ALASHMKIRK ISFTGSVRTG
KAIKEAAAKS NLKMVTLELG GKSPLVIFED ADLDKAAEAA AKSILLNSGQ ACIASTRVYV
AKTAMEAFCQ KFVQSLKDLG ANPSSGNDPR VPGTRRGPQA TQSQFESILS YIKEAERSGY
GIIAGGKREG QRGFFVEPTI IYEPDEQSRV MREEIFGPVA CVKGFETEED VIRRANDSEF
GLYASVYTKD ISRALRVGRA FESGTVGINC TSPMMTHDMP FGGVKQSGEG RELGKTAVDD
WTQLKTMYIA M
//
