ID A8PYW0_MALGO Unreviewed; 511 AA.
AC A8PYW0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171};
GN ORFNames=MGL_1733 {ECO:0000313|EMBL:EDP44336.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP44336.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP44336.1, ECO:0000313|Proteomes:UP000008837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
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:EDP44336.1}.
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DR EMBL; AAYY01000004; EDP44336.1; -; Genomic_DNA.
DR RefSeq; XP_001731550.1; XM_001731498.1.
DR AlphaFoldDB; A8PYW0; -.
DR STRING; 425265.A8PYW0; -.
DR GeneID; 5855857; -.
DR KEGG; mgl:MGL_1733; -.
DR VEuPathDB; FungiDB:MGL_1733; -.
DR InParanoid; A8PYW0; -.
DR OMA; GMWKIAP; -.
DR OrthoDB; 216092at2759; -.
DR Proteomes; UP000008837; 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 CDD; cd07091; ALDH_F1-2_Ald2-like; 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 Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000008837}.
FT DOMAIN 30..496
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 267
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 511 AA; 55480 MW; 652C7452A92CDA1D CRC64;
MSETCTVVTP TGREITVPTG LLIDGGFRPA QANDKLDVYN PATGSVIASI SGGDQADVDA
AVRAARNAFD NAWGKHTTPD QRAALLNKWA DLIEAHTDEL AELESLNNGK PVWISKSMDI
ATSVKTLRYY AGLADKLNGR TIELAEGKRL AFTRLVPYGV CGQIIPWNYP IMMFAWKVAP
ALAAGNTIVM KPAEITPLTA QKLAELSIEA GFPSGVVNVV NGLGSKVGKA ISEHKGINKV
AFTGSTATGR TIASAASASN LKKVSLELGG KSPMIVFEDA DLEQSAKWIA MGFLFNMGQN
CTAGTRVFIH NSIKDKFLNL LLDTMKQHKV GDPFDPSTFQ GPQVSESQYK RILSYIQSGK
EQGAKVLYGG EPYKMEDEKF KNGYWIQPTL FGDCKKGMKI VDEEIFGPVA CVFTFDTEEE
AIEMANDTDY GLAAGVFSKD SDRCMRVVHA LEAGTVWCNN QQILNPAVPF GGMKQSGIGR
ELGYEGIHEY VQTKAINWNY GEKLEWPPSG H
//
