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Database: UniProt
Entry: Q6FN17_CANGA
LinkDB: Q6FN17_CANGA
Original site: Q6FN17_CANGA 
ID   Q6FN17_CANGA            Unreviewed;       527 AA.
AC   Q6FN17;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   Name=HFD1 {ECO:0000313|CGD:CAL0133859};
GN   OrderedLocusNames=CAGL0K03509g {ECO:0000313|CGD:CAL0133859,
GN   ECO:0000313|EMBL:CAG61338.1};
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG61338.1, ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG61338.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
CC       ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CR380957; CAG61338.1; -; Genomic_DNA.
DR   RefSeq; XP_448377.1; XM_448377.1.
DR   AlphaFoldDB; Q6FN17; -.
DR   STRING; 284593.Q6FN17; -.
DR   EnsemblFungi; CAGL0K03509g-T; CAGL0K03509g-T-p1; CAGL0K03509g.
DR   GeneID; 2890178; -.
DR   KEGG; cgr:CAGL0K03509g; -.
DR   CGD; CAL0133859; HFD1.
DR   VEuPathDB; FungiDB:CAGL0K03509g; -.
DR   eggNOG; KOG2456; Eukaryota.
DR   HOGENOM; CLU_005391_3_1_1; -.
DR   InParanoid; Q6FN17; -.
DR   OMA; EPCIQGQ; -.
DR   Proteomes; UP000002428; Chromosome K.
DR   GO; GO:0005811; C:lipid droplet; IEA:EnsemblFungi.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:EnsemblFungi.
DR   GO; GO:0018484; F:4-hydroxybenzaldehyde dehydrogenase activity; IEA:EnsemblFungi.
DR   GO; GO:0047770; F:carboxylate reductase activity; IEA:EnsemblFungi.
DR   GO; GO:0046185; P:aldehyde catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0032180; P:ubiquinone biosynthetic process from tyrosine; IEA:EnsemblFungi.
DR   CDD; cd07135; ALDH_F14-YMR110C; 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   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR036492,
KW   ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428}.
FT   DOMAIN          33..457
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        232
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ   SEQUENCE   527 AA;  59337 MW;  3D036832ED9AF20B CRC64;
     MAEILNYTEL SEIDAKISIS RNYFQQNRKE LANQKNVRSA DNKQRQFWLK KLYWSVKDHE
     EQILEALEKD FHRSRQESIS LEYVKLLGDI LHLIEGIPKW NKPKKVRDNS APFMFGNINI
     EKISRGNVLV ISPFNFPVLL ALAPVACALS AGNTVILKPS EMTPHCALVL EDIVKSCQLP
     EGVLQIVQGG VEQTTKLINS ESLDMIFYTG SPRVGSIVAQ AAAKNLVPCV LELGGKSPTF
     ITGSLQKKNL ETALKRIFFG AFGNAGQICV SPDYLLVHES IYDDVVKESG KVMKELYPDL
     NEHTEYTHMI HKASYDKTLE KLQKTKGRKV SAADVKIDNT SGKLMIPPTI VFDSDWDDAL
     MEEENFAPVL PVIKYTDIDA TIDKILSKHD TPLVQYIFSE KQKEIDHILA RLRSGDCIIC
     DTTIHVGIKD APFGGIGQSG YGNYGGVYGF DAFSHERIVL KQPFWVDFLL KLRYPPFTAK
     KVKLLKLATE RQPWFDREGN DHRSYKLIAM FSVTCALLAV GVKSFFV
//
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