ID A0A066XZ69_COLSU Unreviewed; 481 AA.
AC A0A066XZ69;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Putative aldehyde dehydrogenase {ECO:0000313|EMBL:KDN71240.1};
GN ORFNames=CSUB01_11106 {ECO:0000313|EMBL:KDN71240.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN71240.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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:KDN71240.1}.
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DR EMBL; JMSE01000223; KDN71240.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066XZ69; -.
DR STRING; 1173701.A0A066XZ69; -.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_0_1; -.
DR OMA; LWTDEVF; -.
DR OrthoDB; 216092at2759; -.
DR Proteomes; UP000027238; 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; 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; 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; 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:UP000027238}.
FT DOMAIN 25..475
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 26..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 251
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 481 AA; 52770 MW; 19AE4B7D22D210B0 CRC64;
MATNGTSKLD WTKFYNVIDG KLETTSKTRH NVNPSTLEAN PEVPVSTPED VDRAVQAGKK
AQEAWAETPY EERQKALVKF AEAFEAHVEE FALMLSKEQG KPVQFAQIEI IESIKHFKGM
SELPFPDEVV DNNPDRRVIT RYTPLGVAVG IVPWNFPILL ACGKIAPALV TGNAFILKPS
PFTPYCNLKL VELAQQFFPP GVFQALSGDD NLGPWLTAHP GVDKVSFTGS TATGKRVMES
CSKTLKRITL ELGGNDAAIV FPDVDVKAIA PKITMLALYN SGQVCIAIKR IYIHEDIYDE
LVAEIANVIK NMPVGDGQQE GTVLGPVQNQ MQFERVKELL KDIEEQKLKL AAGSTAPATN
GKGYFITPTM VDNPPDNSRI VVEEPFGPVF PVLKWSDEKD VIRRANDTLM GLGASVWCKD
LEKAESVAKK IKAGNVWINT HLELQYNAPF GGHKQSGIGH EYGVGGLKSY CNAQSLFITK
A
//
