ID F8Q0D8_SERL3 Unreviewed; 500 AA.
AC F8Q0D8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171};
GN ORFNames=SERLA73DRAFT_92037 {ECO:0000313|EMBL:EGN98588.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR EMBL; GL945481; EGN98588.1; -; Genomic_DNA.
DR AlphaFoldDB; F8Q0D8; -.
DR STRING; 936435.F8Q0D8; -.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_0_1; -.
DR InParanoid; F8Q0D8; -.
DR OMA; WNFPLDM; -.
DR OrthoDB; 216092at2759; -.
DR Proteomes; UP000008063; 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:UP000008063}.
FT DOMAIN 34..492
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 269
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 500 AA; 54210 MW; 5A2C9954F2DF1988 CRC64;
MSNTFVYQFD TPTFKGTATV PTGLFINGKF VEPVEGGTID VINPANGKLL TKISAGTAKD
VDIAVEAARV AYKERWGLKV PGAQRGRMLN KLADLMDQHQ QELAALEALD NGKAYNVAMA
ADLPSSAAVI RYYAGWADKI QGKTIETTEK KMAYTRHEPF GVVGAIIPWN FPLNMLTWKI
GPALATGNAV VLKPSELTPL TALRLCSLIN EAGFPPGVLN IVNGYGHTVG QAISEHMVIQ
KVAFTGSTMT GRKVMEAAAK SNLKNVSLEL GGKSPSIVFD DANLEQTVKW VAHGIYFNHG
QTCTAGSRIF IQAGIYDTFV QKFKEHSLTL KLGDPFETTT YQGPQVSQTQ FDRIMGYIES
GKSDGANLLI GGARHGTEGY FIQPTIFTEC KPSMKIVREE IFGPVAAVAR FTTEEEVIEL
ANDTSYGLAC CVFTQDVNRA IRVAHSIEAG TAWVNCANHS EVAIPFGGFK QSGIGRELGE
YALEHYTNVK AVHVNIGYEL
//
