ID G0VGL4_NAUCC Unreviewed; 522 AA.
AC G0VGL4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN Name=NCAS0F01510 {ECO:0000313|EMBL:CCC70635.1};
GN OrderedLocusNames=NCAS_0F01510 {ECO:0000313|EMBL:CCC70635.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC70635.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC70635.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
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).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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; HE576757; CCC70635.1; -; Genomic_DNA.
DR RefSeq; XP_003676990.1; XM_003676942.1.
DR AlphaFoldDB; G0VGL4; -.
DR STRING; 1064592.G0VGL4; -.
DR GeneID; 11527441; -.
DR KEGG; ncs:NCAS_0F01510; -.
DR eggNOG; KOG2456; Eukaryota.
DR HOGENOM; CLU_005391_3_1_1; -.
DR InParanoid; G0VGL4; -.
DR OMA; AWMKDQK; -.
DR OrthoDB; 606537at2759; -.
DR Proteomes; UP000001640; Chromosome 6.
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; 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; 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:UP000001640}.
FT DOMAIN 41..454
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 522 AA; 58661 MW; C505E4B443A35A05 CRC64;
MATLNYTPLE VIDTKIQSSR NFYLARQLQL SHEKSPAKAD LLFRQTQLKK LYNSILKHEE
NLIQAMFQDY HRARQESIGT EINPLLNATL HIINHLSKWM KPKRVSDNSP PFICGSIKVE
KIARGNVLVI SPFNFPVLLA LVPVAHAIGA GNSVILKPSE RTAHTALVMQ RIIEEAGFPD
GLVQVVQGAI DETQRLITSK DLDMIFYTGS PTVGSIIAQE AAKNLTPCVL ELGGKSPTFI
TENFNDKNLK TALKRIFFGA FGNSGQICVS PDYLLVHESK YNKVAALAKE VLIEMFPEVN
DSTEFTHLIS ETAYNTTLKK LEATSGEKFQ AKSDLSDTNI CVPPTLIFNC QWEDSTMQQE
NFAPILPVLK YSNLDDTLDK IIATHNNPLV QYIFSDSNEE ISHILLRLKS GDCVINDTIL
HVGIQDAPFG GIGNSGYGNY GGIYGFNAFT HERTFFKQPF WNDVFLSMRY APFTQKKTKL
IKATTRNMSS FDKNGHEYWY LNKWFPLSFL IIISGMLYKA LV
//