ID V2XPJ7_MONRO Unreviewed; 536 AA.
AC V2XPJ7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:ESK94475.1};
GN ORFNames=Moror_8133 {ECO:0000313|EMBL:ESK94475.1};
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:ESK94475.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK94475.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK94475.1,
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:ESK94475.1}.
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DR EMBL; AWSO01000135; ESK94475.1; -; Genomic_DNA.
DR RefSeq; XP_007846292.1; XM_007848101.1.
DR AlphaFoldDB; V2XPJ7; -.
DR STRING; 1381753.V2XPJ7; -.
DR KEGG; mrr:Moror_8133; -.
DR HOGENOM; CLU_005391_0_0_1; -.
DR OrthoDB; 1818863at2759; -.
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 CDD; cd07114; ALDH_DhaS; 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 PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR11699:SF198; DEHYDROGENASE FAMILY PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G03250)-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:UP000017559}.
FT DOMAIN 42..508
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 277
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 536 AA; 58153 MW; FD7F17D915DE0889 CRC64;
MLLLRSEVPF RPFCRQLSST VANAVAISQR YGPPRYGQRG IESESTEEFT VINPANGQEL
CKVTTASAED VKNTIDHAQT IFDSGVWSKA PAIVRSKVLS RLARMLEERI PELARMETLQ
TGRTIREMNA QLGRVPEWID YYAALLRTNQ AYVAPTQGKL LNYIQRVPLG VVAQITPFNH
PLFIAIKKIA PALAAGNSVI IKPSELAPIT VLEFAKMATE AGLPQGVLSV LPGFGTTTGK
AIVSNPLIRK VDVTAGTQTG RILGSIVGSN LASYTAELGG KAPIVVFNDA DMESAVNGVA
FAAFVASGQT CVSGARIIVQ DGIYDAFMKK FVGKSESIRR RMGDPLNPKS TMGTVISQKH
LNRIEGMIEQ TQGRIVVGGQ QMLGNSELDN FDFSSGSFFP PTIITEVEIN DLLWQEEIFG
PVVVVKRFSN EAEGIRLANA SRYGLGAGIW TSDLSKAHRV AAEVQAGLCW INTHHRNDPS
SPWGGMKESG IGRENGLEAF EAYSQSKSTI VNVASADETR KTDDWFAESA EGRRYG
//
