ID A0A060S5B7_PYCCI Unreviewed; 393 AA.
AC A0A060S5B7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171};
GN ORFNames=BN946_scf184851.g30 {ECO:0000313|EMBL:CDO69642.1};
OS Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO69642.1, ECO:0000313|Proteomes:UP000029665};
RN [1] {ECO:0000313|EMBL:CDO69642.1, ECO:0000313|Proteomes:UP000029665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM137 {ECO:0000313|EMBL:CDO69642.1,
RC ECO:0000313|Proteomes:UP000029665};
RA Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA Pontarotti P., Henrissat B., Record E.;
RT "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT breakdown.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {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:CDO69642.1}.
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DR EMBL; CCBP010000052; CDO69642.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060S5B7; -.
DR STRING; 5643.A0A060S5B7; -.
DR HOGENOM; CLU_005391_1_0_1; -.
DR OMA; MAYVNEH; -.
DR OrthoDB; 1478027at2759; -.
DR Proteomes; UP000029665; 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:UP000029665}.
FT DOMAIN 20..391
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 257
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 393 AA; 42081 MW; D1F7C7CB63179FDE CRC64;
MCAPATMSVP FTPLYIDGQW RPSSTGVTFD VRNPTSGKVV GTAAAASAED CTAAVEAASR
AFKTWENSPL SQRRDILIRA SDNFAKKREE VAKVAREETA ITEDWLPVNF EWPIDQMRDI
ASATMRLKGE TGLSIIPGGQ VFTQKRAIGV VIVPWNAPVI LTLRAVAVPI VCGNTVVLKT
SEYSPKLQAM IVEVLEEAGL PAGVLNCIST SKEDSPARTT DIIAHPKVRK INFTGSDVVG
RIIAQEAGKY LKPCVLELGG KAPVVVLNDA DIPRAARAIT SSALLHSGQI CMSTERVIVQ
KGAASELINT LTELFKRVKA GDPHLDRAAH IGALFSADSP GNAISMLKDA VDQGAKVLVG
DLTKEGAIMQ PHLVVDVKPG MRLWDRETFA PGK
//
