ID V2X2P0_MONRO Unreviewed; 499 AA.
AC V2X2P0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:ESK93383.1};
GN ORFNames=Moror_1794 {ECO:0000313|EMBL:ESK93383.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK93383.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK93383.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK93383.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK93383.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWSO01000201; ESK93383.1; -; Genomic_DNA.
DR RefSeq; XP_007847317.1; XM_007849126.1.
DR AlphaFoldDB; V2X2P0; -.
DR STRING; 1381753.V2X2P0; -.
DR KEGG; mrr:Moror_1794; -.
DR HOGENOM; CLU_005391_0_1_1; -.
DR OrthoDB; 216092at2759; -.
DR Proteomes; UP000017559; 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 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:UP000017559}.
FT DOMAIN 30..491
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 268
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 499 AA; 54464 MW; 389CC09BCB5CD087 CRC64;
MSTTFSHEFN TPAFKGKVSF PTGLFIDGKF VDGADKTTID VVNPTNGQVI AKIAEGTAKD
VDIAVAAAQK AFDTVWGLNA PGAQRAKLLT KLWQAMEAIQ EELAALEALD NGKTFGWAMN
VDTTFAIETI RYYAGWADKV HGQVQETTED KLTYSRHEPI GVVGQIIPWN FPLLMFSWKI
GPALACGNTI VIKPSEFTPM SALRVCSLIQ DIFPPGVVNV VNGYGNTVGN AISSHMHIEK
VAFTGSTLVG RKVMEAAAKS NLKNVTLELG GKSPNIIFND ADLEQAVNWS AHGVFWNHGQ
ACCAGTRIFV QSGIYDKFLE KFTQKAREIK LGDPFAQDSM QGPQVSQIQY DRIMNYIQSG
KDEGATIHLG GDRFGNEGYF INPTIFTGTK PEMKIVQEEI FGPVGVVIKF EDEEDVIHQA
NDTMYGLAAA VFSQDINRAL RTAHRLKAGT AWVNCANTLN ENVPFGGFKQ SGIGRELGEY
ALHNYTAVKA VHVNLGIKM
//
