ID A0A0D2IRD0_9EURO Unreviewed; 621 AA.
AC A0A0D2IRD0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00044146};
GN ORFNames=Z518_03688 {ECO:0000313|EMBL:KIX05716.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX05716.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX05716.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX05716.1,
RC ECO:0000313|Proteomes:UP000053617};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN847477; KIX05716.1; -; Genomic_DNA.
DR RefSeq; XP_013272852.1; XM_013417398.1.
DR AlphaFoldDB; A0A0D2IRD0; -.
DR STRING; 1442369.A0A0D2IRD0; -.
DR GeneID; 25291759; -.
DR VEuPathDB; FungiDB:Z518_03688; -.
DR HOGENOM; CLU_005391_1_0_1; -.
DR OrthoDB; 5743at2759; -.
DR Proteomes; UP000053617; 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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000053617};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 95..551
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 315
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 621 AA; 67226 MW; 8A616DDF5FB2504F CRC64;
MLFDFHPERN TQEAGIVNIL LAFLSISTLL VTGILLNAKT ELTVRYNVPI PPPLQKTSPR
DIAEADYKLE DEGEVRNGQI YPRCPADGRS LGPPIVPATP SSIDSAISAA ANAQQQWSHT
TFSDRRRVLR ALLRYVLDHQ DEIVTACCLD SGKTKIDGGF GEILVTVEKL QWTIKHGEKA
LSPSMRPINL LMCYKENTVI YEPLGVVAAC VSWNYPFHNF MSPVISALFA GNAIVVKPSE
QTCWSTIYFT EIIRGALRAC GYSVDLIQNV ICLPEVADHL TSHPGLSHIT FIGSRQIAHR
VCTSAAKALT PVTVELGGKD PAIVLDDPKT IKSTDDVISI LMRGVFQSAG QNCIGIERII
ALPAIHDIIL NHALPRIQSL RLGSVLLSPS TCPPDMGAMI SSRNFQCLET LISSAVAQGA
ILHCGGKRYA HPQFPNGTYF RPTLLSNVTV DMAIAQTELF APVFLLMKAP SVDEAITIAN
STPYALGASV FGHDSANVSR CVHEIKAGMV AVNDFGAYYA CSMPFGGVGG SGYGRFGGAE
GLQALSNVKS VCQEAWWAKM LGIKTKIPLK LQYPVSPDGW NVSKGVVGTG YALGWSEWIG
CLLGLVKALS RRDDGELYEK K
//
