ID C4Y5K5_CLAL4 Unreviewed; 461 AA.
AC C4Y5K5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171};
GN ORFNames=CLUG_03439 {ECO:0000313|EMBL:EEQ39311.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ39311.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ39311.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ39311.1,
RC ECO:0000313|Proteomes:UP000007703};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CH408079; EEQ39311.1; -; Genomic_DNA.
DR RefSeq; XP_002616198.1; XM_002616152.1.
DR AlphaFoldDB; C4Y5K5; -.
DR STRING; 306902.C4Y5K5; -.
DR GeneID; 8497128; -.
DR KEGG; clu:CLUG_03439; -.
DR VEuPathDB; FungiDB:CLUG_03439; -.
DR HOGENOM; CLU_005391_1_0_1; -.
DR InParanoid; C4Y5K5; -.
DR OMA; IIQREMG; -.
DR OrthoDB; 1478027at2759; -.
DR Proteomes; UP000007703; 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; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR PANTHER; PTHR43353:SF6; CYTOPLASMIC ALDEHYDE DEHYDROGENASE (EUROFUNG); 1.
DR PANTHER; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000007703}.
FT DOMAIN 42..457
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 461 AA; 48838 MW; 98CE049CEA78959B CRC64;
MLSVIPSLVN GAPVVSSVRI PVLSSGGKLL HHYSPLPSSV SLDQVARNAF VGFQKWSARP
ASERADVLRA AASTIGAKHD FYVERHMELG APRGFADVCA RAAANSFSES ASALVRAEGC
VAQSHVAPLA LALRTPVGPV LSLAPWNAPT VLWARALAAP LAAGCSVVAK GTEKAPSLAY
FYAQDLLAAG VDKEAVQLVH VSPENQRSAT EALIARPEIR KVNFTGSTEV GAQVAAAAAQ
SLTPVLLELG GKNVSVVCQD AHIDRAAFSA VLSAWMHQGQ ICMCLDNVYV HEAVYDDFLA
RVAFHAQKLA SSPDAAIPFH NADKVRRMVD EALSGGARVV WGDAKRFPLV LADVPPQSAL
ATRETFGPVL SIFRFSDAED VLSRINALSY GLKASVWSSN VMEALAMARR LDFGSVHING
STVHDEASLP HGGVKSSGYG RFNGMWGIDE FSYTKVVTMS S
//
