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Database: UniProt
Entry: A0A067PDF2_PLEOS
LinkDB: A0A067PDF2_PLEOS
Original site: A0A067PDF2_PLEOS 
ID   A0A067PDF2_PLEOS        Unreviewed;       631 AA.
AC   A0A067PDF2;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171};
GN   ORFNames=PLEOSDRAFT_1074008 {ECO:0000313|EMBL:KDQ33896.1};
OS   Pleurotus ostreatus PC15.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX   NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ33896.1, ECO:0000313|Proteomes:UP000027073};
RN   [1] {ECO:0000313|Proteomes:UP000027073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA   LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA   Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA   Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT   white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; KL198004; KDQ33896.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067PDF2; -.
DR   STRING; 1137138.A0A067PDF2; -.
DR   VEuPathDB; FungiDB:PLEOSDRAFT_1074008; -.
DR   HOGENOM; CLU_005391_1_0_1; -.
DR   InParanoid; A0A067PDF2; -.
DR   OrthoDB; 5743at2759; -.
DR   Proteomes; UP000027073; 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; 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   Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027073}.
FT   DOMAIN          99..572
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        337
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   631 AA;  70428 MW;  C330C1B70F2C92AB CRC64;
     MSVLLDILIY PFLKLRSTDD NDLDAPPGFG FVVPLSLFWG FGIYQVIRRY HKIHNSPKPF
     EWHKPLEAEP AWESIPIKDA SITSHLEKEE IMPAFAARDR KYITSFDPAT SFHIATVIAD
     NAQEIGMKIR RASEAQASWK DTTFTQRRRF MRSLLKWLVD NQEACAQVAC RDTGKTLIDA
     ALGEILTTCS KLEWLIAHGE KALRPESRSS NLILSYKKSE VHYEPLGVVA GIVSWNYPLH
     NSWSPIIAAL FAGNGIVLKC SEKVVWSTGW FVGAITECLR ACGHDPELVQ LVCCYPEEAE
     ALTKSPEIKH ITFIGSDTVG KKVAIAAAEN LTPVTLELGG KDPAIILPDT DLKKWLSLWM
     RGIYQNAGQN CIGIERLIVH SSQYDDLREL LSERVSKLRL GSVLTPTQEG YVYTVDCGAM
     IDGDRFYSLE RLITSAEENG AYVEGGKKFE HVYLNQGTYF SPTIVGPVSP EEEIAQTELF
     APIALLMIYE DVEEAIDIAN GTKYGLGASV FGPDQRQCLQ VAKELQCGMV SINDFGVFYL
     NQDLPFGGTK ASGYGRFGGP EGLRALTNPK AIMVDRWPSF IQTSIPKVLD YPLRSLSSSW
     DFTSGLVRFV YADSWRTRVQ GLITLWRAAR K
//
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