ID K5WF15_PHACS Unreviewed; 487 AA.
AC K5WF15;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 22-FEB-2023, entry version 31.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN ORFNames=PHACADRAFT_251452 {ECO:0000313|EMBL:EKM57674.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM57674.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM57674.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM57674.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492}.
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DR EMBL; JH930470; EKM57674.1; -; Genomic_DNA.
DR RefSeq; XP_007393021.1; XM_007392959.1.
DR AlphaFoldDB; K5WF15; -.
DR STRING; 650164.K5WF15; -.
DR GeneID; 18915225; -.
DR KEGG; pco:PHACADRAFT_251452; -.
DR HOGENOM; CLU_005391_3_1_1; -.
DR InParanoid; K5WF15; -.
DR OrthoDB; 606537at2759; -.
DR Proteomes; UP000008370; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR036492};
KW Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 114..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..438
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 218
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
FT ACT_SITE 252
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ SEQUENCE 487 AA; 53292 MW; 56122CD16896CC59 CRC64;
MTRLEYTNID NVPKIHAELK ETFRSGKTRP VPFRKEQLAQ LAWLLKDNTD RIADAIHTDL
GRPAIESDLL DINPSIGEAK DAYDNVAKWA KTEKARWTFN FFAMRPKIRK EPKGVVLIIS
PFNFPVLLLL GHLASALAAG NTVVLKPSEL VPATSQLISD LISQYMDPGV VRVVNGDVSV
TTKLLELPWD HILYTGSSRV AKIICTAAAK HLTPVTTELG GKSPVIIDPK CDMKLAARRI
LWGKIANAGQ TCVAPDYVLV PREAQDALVN ELMEVYQTFY PEGDPATSAS FSRIVSQAHT
TRIKRLIDGT KGTVVVGGTV DVEKRYIAPT IIRDVPVDDS TMDEEIFGPV LPIVPVRDVE
EAIQIVNSRD HPLSLYVFTQ DAAFKENVFS RTQSGAALAN EVLVHVGATG LPFGGIGPSG
SGSLTGKHGF DAFTHLRSTL DNPKWVDAIM KGRYPPYTPE KLARLRTALK VRMPPRPGGA
RPAQKSA
//
