ID G0WF52_NAUDC Unreviewed; 480 AA.
AC G0WF52;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN Name=NDAI0H02390 {ECO:0000313|EMBL:CCD26413.1};
GN OrderedLocusNames=NDAI_0H02390 {ECO:0000313|EMBL:CCD26413.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD26413.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD26413.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
CC ECO:0000256|RuleBase:RU003345}.
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DR EMBL; HE580274; CCD26413.1; -; Genomic_DNA.
DR RefSeq; XP_003671656.1; XM_003671608.1.
DR AlphaFoldDB; G0WF52; -.
DR STRING; 1071378.G0WF52; -.
DR GeneID; 11495944; -.
DR KEGG; ndi:NDAI_0H02390; -.
DR eggNOG; KOG2456; Eukaryota.
DR HOGENOM; CLU_005391_3_1_1; -.
DR OMA; AWMKDQK; -.
DR OrthoDB; 606537at2759; -.
DR Proteomes; UP000000689; Chromosome 8.
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 GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
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 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.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR036492,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT DOMAIN 40..455
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 231
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 268
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ SEQUENCE 480 AA; 54194 MW; 1FA3E40EA99C8AB8 CRC64;
MTTLQYTPLD DINSIIKTSK EFYLNRQIQL TKEKNPFKAD LEFRIEQLKK FYNAIATHED
EIIDALFADY HRAKQESIGL EINPLLNNIL HIIKNLRKWM KPTKVSDCSP PFMFGSIKVE
KIARGNVLVI APFNFPILLS LVPVAHAIGA GNSVVLKPSE QTPHTSMLIA KILNHAGFPK
GLVQIVQGSI DETSKLIKSK DFSMMFYTGS PKVGSIVAQE AAKNLIPCVL ELGGKSPTFI
TKSFSRKNLK TALRRIFFGS FGNSGQICVA PDYLVIHESL YDEAREIAKE LLKETFPLIT
KDAEYTHMIS ERSYNNALKK LENTQGTVYQ CESSLNSDSL CIPPTLIFDC NWDDTTMLEE
NFSPILPIIK YTDLDKTLDT IIDKYDAPLV QYIFSSSKSE ISHILMRLRS GDCIIGDTLI
HVGIKDSPFG GIGHSGYGNY GGIYGFNAFT HERTIFTQPF WMDFVLSMRY QPYNKEKQSY
//
