ID R7SM92_DICSQ Unreviewed; 500 AA.
AC R7SM92;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:EJF56132.1};
GN ORFNames=DICSQDRAFT_158024 {ECO:0000313|EMBL:EJF56132.1};
OS Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Dichomitus.
OX NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF56132.1, ECO:0000313|Proteomes:UP000053319};
RN [1] {ECO:0000313|EMBL:EJF56132.1, ECO:0000313|Proteomes:UP000053319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF56132.1,
RC ECO:0000313|Proteomes:UP000053319};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR EMBL; JH719483; EJF56132.1; -; Genomic_DNA.
DR RefSeq; XP_007371134.1; XM_007371072.1.
DR AlphaFoldDB; R7SM92; -.
DR GeneID; 18837833; -.
DR KEGG; dsq:DICSQDRAFT_158024; -.
DR HOGENOM; CLU_005391_0_0_1; -.
DR OMA; HGIGYYP; -.
DR OrthoDB; 216092at2759; -.
DR Proteomes; UP000053319; 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:UP000053319}.
FT DOMAIN 30..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; 54781 MW; 077CC97BB1A10301 CRC64;
MPETFKYTFD TPVFKGDVEV PLGLYIDGKF VDGSNSTYID VINPTNGKTT TRISEGTPKD
VDIAVKAAHK AFETTWGLNT TGVDRSRLLN KLADLMEKEQ DVLSALEALD NGKTFNWAKR
GDVSHSITCI RYYAGWADKV LGQTIETSEA KLTYTRHEPI GVVGQIIPWN FPLQMMAWKI
GPALATGCAI VLKPSEFTPL TALYMAKLID QVGFPAGAFN LVNGYGSIVG QALAEHPDIE
KIAFTGSTLV GRKIMEASAK SNLKKVTLEL GGKSPTIVFD DADLDQAVKW AAFGIYYNHG
QCCCAGSRIF VHANIYDEFL QRFTAHTQTL KVGDPFSPET FQGPQINQQQ YDRIMGYIES
GKAEGAKVHY GGHRVGNEGY YISPTIFTET KPNMKIVQEE IFGPVCVVIK FSDDDDIVKQ
ANDSVYGLAA AVFSQNVTRA LSTAHKLKAG TVWVNVANML YPNVPFGGYK QSGIGRELGE
YALANYTAVK AVQVNLLIKM
//
