ID A0A094FCM1_9PEZI Unreviewed; 487 AA.
AC A0A094FCM1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171};
GN ORFNames=V500_06262 {ECO:0000313|EMBL:KFY88589.1};
OS Pseudogymnoascus sp. VKM F-4518 (FW-2643).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420913 {ECO:0000313|EMBL:KFY88589.1, ECO:0000313|Proteomes:UP000029284};
RN [1] {ECO:0000313|EMBL:KFY88589.1, ECO:0000313|Proteomes:UP000029284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4518 (FW-2643) {ECO:0000313|Proteomes:UP000029284};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY88589.1}.
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DR EMBL; JPKC01002042; KFY88589.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094FCM1; -.
DR STRING; 1420913.A0A094FCM1; -.
DR HOGENOM; CLU_005391_0_0_1; -.
DR Proteomes; UP000029284; 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; cd07106; ALDH_AldA-AAD23400; 1.
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; IPR044086; LUC3-like.
DR PANTHER; PTHR11699:SF263; ALDEHYDE DEHYDROGENASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 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:UP000029284}.
FT DOMAIN 31..482
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 255
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 487 AA; 52959 MW; 9579E671FA74EBC1 CRC64;
MAEVTNDSSK KEFNFTTFHN VINGELKTTS TTRHGISPHT KKALAEVPLS TAKDVDDAVA
AARAAFPKWK KTSFEERAKG LTALSATIYE YQQEFIKLNG YELGAPVSIA EILVHMAAGW
LSETAKLQPK DEIVEDTPER EVRVRYLPLG VAVGIVPWNL PLHCTAAKIA AAVIAGNCII
IKPSPYTPYS GLKLVEMAQK FFPPGVIQVL SGDDSLGQLL TEHLGVDKIS FTGSTATGKK
VMESASKSLK RVTLELGGND AAIVTKNIDV ATIAPALAGI IFSNSSQVCL AIKRLYVHES
IFEEFRDALV AAVKAFKLGE GVGEGENDPT VNIGPVQNEM QYERIKGFFN DIEKEGWKVA
VGGKIEESPG YFINPTIIDR PKEDSRIVVE EPFGPILPIL SWSDEDDVIA RANNTRMGLG
ASVWTNDKVE ARHIAEQIEA GSVWVNSHME VNPNYPFGGH KDSGIGYENG LGGVKAYCNV
QTLYLKK
//
