ID M2RK08_CERS8 Unreviewed; 486 AA.
AC M2RK08;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171};
GN ORFNames=CERSUDRAFT_151449 {ECO:0000313|EMBL:EMD38802.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD38802.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD38802.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD38802.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR EMBL; KB445794; EMD38802.1; -; Genomic_DNA.
DR AlphaFoldDB; M2RK08; -.
DR STRING; 914234.M2RK08; -.
DR HOGENOM; CLU_005391_1_0_1; -.
DR OrthoDB; 1478027at2759; -.
DR Proteomes; UP000016930; 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; PTHR42986; BENZALDEHYDE DEHYDROGENASE YFMT; 1.
DR PANTHER; PTHR42986:SF1; BENZALDEHYDE DEHYDROGENASE YFMT; 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|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000016930}.
FT DOMAIN 18..461
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 255
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 486 AA; 51848 MW; 05E338636F2F52D0 CRC64;
MSIPFTSLYI GGQYRPASDG GTYEVRNPHS QQVVGTAAAA TSQDCKDAVD AAHKAYLSWE
QTPLTTRRDI FLKAADLLQE ERFRNPFTEA LVQETASVDF MVAFNLRGTA ASLRNYAATI
LNYKGQSFPS ANPGGNVAEV RKAKGVVFGI APWNAPLILT IRAMAVPVLC GNAVVLKCSE
ISPRTQSVVT GLFKEAGLPD GVLNFISTSR SDAPTRVAEI IANPLVRVVN FTGSDVVGRI
IAGEAAKYLK PCVFELGGKS PVVVLEDADI DRAARAIASS ALLHSGQICM STERVIVARK
VAPALTSALT VLFKKVQAGG PGSDISALFR EDSAVKVTDM IKDATEKGAK LLVGDGTRDG
AVVQPHLVTD VKTDMWIWNR ETFGPVTTVI EFDTVDEAIE LANTSDYSLT AALWTQNLNN
AFDVGSRIRA SHINLNGPTV HTESSGRGIG GLGGATGYGH FDVDSFTDIR TLVIHPAQNP
WYPVVG
//
