ID W7N6B7_GIBM7 Unreviewed; 480 AA.
AC W7N6B7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Aldehyde dehydrogenase (NAD+) {ECO:0000313|EMBL:EWG52162.1};
GN ORFNames=FVEG_10971 {ECO:0000313|EMBL:EWG52162.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG52162.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG52162.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
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|RuleBase:RU003345}.
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DR EMBL; DS022257; EWG52162.1; -; Genomic_DNA.
DR RefSeq; XP_018758353.1; XM_018900132.1.
DR AlphaFoldDB; W7N6B7; -.
DR STRING; 334819.W7N6B7; -.
DR EnsemblFungi; FVEG_10971T0; FVEG_10971T0; FVEG_10971.
DR GeneID; 30068515; -.
DR KEGG; fvr:FVEG_10971; -.
DR VEuPathDB; FungiDB:FVEG_10971; -.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_0_1; -.
DR OMA; NEWFERM; -.
DR OrthoDB; 216092at2759; -.
DR Proteomes; UP000009096; Chromosome 9.
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; ALDEDH 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:UP000009096}.
FT DOMAIN 25..471
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 249
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 480 AA; 52437 MW; 24EAC4006C1B33AA CRC64;
MTKPSINFKG GFVQIIDGQS APTKETRHGL NPANLQEMDK VPVATQQDLD RAVAAAKKAF
KAWSKTPYEE RRETVLAFAD AVDTHRDEFQ ALLTAEQGKP VPQAAYETDA AIEWMRGMAL
IPLPEDVLED TEQRTIISRY TPIGVVAALV PWNFPLLLAT GKIAPALLTG NVIIVKPSPF
TPYGGLKLVE LAQQFFPPGV VQSLSGDDKL GPWMTSHPGV DKISFTGSTA TGKAVLRSAS
STLKRVTLEL GGNDPAIIFP DVDIDKVAEK VAFFAFLNSG QICLNLKRIF VHQSIYLQFK
EALVKHVKSY TLGDGSKEGV THGPLQNAPQ FKRVKGFFED IEKEGWNVAV GGKIESSEGY
FVNPTIIDVP PETSRIVVEE PFGPIVPLLT WSSEEEVIER ANDTTMGLGA SIWCNDIRRA
HRIAREIQAG NVWVNTHFDL TPMAAFGGHK ESGIGTEWGA NGLKGFCNVQ TLFLNKNVVS
//