ID A0A3N2Q5G8_9PEZI Unreviewed; 459 AA.
AC A0A3N2Q5G8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00044146};
GN ORFNames=SODALDRAFT_326080 {ECO:0000313|EMBL:ROT41898.1};
OS Sodiomyces alkalinus F11.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT41898.1, ECO:0000313|Proteomes:UP000272025};
RN [1] {ECO:0000313|EMBL:ROT41898.1, ECO:0000313|Proteomes:UP000272025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F11 {ECO:0000313|EMBL:ROT41898.1,
RC ECO:0000313|Proteomes:UP000272025};
RX PubMed=30368956; DOI=10.1111/mec.14912;
RA Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA Grigoriev I.V., Debets A.J.M.;
RT "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT shifted to a protein diet.";
RL Mol. Ecol. 27:4808-4819(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00024149};
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR EMBL; ML119051; ROT41898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2Q5G8; -.
DR STRING; 1314773.A0A3N2Q5G8; -.
DR OrthoDB; 178592at2759; -.
DR Proteomes; UP000272025; 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; cd07102; ALDH_EDX86601; 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:UP000272025}.
FT DOMAIN 6..427
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 233
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 459 AA; 49615 MW; 0D2E5C52C9E8C574 CRC64;
MSVEVLTTIS PTTNEPILTR NGVSQAELDE LPNVATEAFQ TWRKTPLADR QGIVRKALRL
LADKKDDLAE ELAVQMGRPV AYGGAEVLTA IKRADYLLKV SDEALQDTDG EPEKGFKRFI
RKVPVGPVLV IFAWNYPYLI LVNSLIPALL AGNTVILKPS PQTPTVVERV AEVFAEAGLP
TGVLQYFHAG SPTQIETIVR NLKVKLVAFT GSVAGGLAVQ KAAADRIVHV GLELGGKDPA
YVRADVDVAW AAGEIVDGAV FNSGQSCCAI ERVYVDEAIH DDFVAAAQEV LRGYRLGSPF
DKATQVGPVV SRRAREAIEA QIKDALERGA QDATPESETF ANLPPKGNFV KPTLLTGVDH
GMAVMREETF GPVIPVMKVR GDAEAVRLMN DSEFGLTASI WTKDTEKGYE LAEEVEAGTV
FVNRADYPSP VSRVSLGSLT SRPGPITARG NEEIRWNEN
//
