ID E9DTL7_METAQ Unreviewed; 696 AA.
AC E9DTL7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00044146};
GN ORFNames=MAC_00855 {ECO:0000313|EMBL:EFY93072.1};
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN [1] {ECO:0000313|EMBL:EFY93072.1, ECO:0000313|Proteomes:UP000002499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY93072.1,
RC ECO:0000313|Proteomes:UP000002499};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
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; GL698472; EFY93072.1; -; Genomic_DNA.
DR RefSeq; XP_007807195.1; XM_007809004.1.
DR AlphaFoldDB; E9DTL7; -.
DR STRING; 655827.E9DTL7; -.
DR GeneID; 19245166; -.
DR KEGG; maw:MAC_00855; -.
DR eggNOG; KOG2454; Eukaryota.
DR HOGENOM; CLU_005391_1_0_1; -.
DR InParanoid; E9DTL7; -.
DR OMA; ILMRGTF; -.
DR OrthoDB; 5743at2759; -.
DR Proteomes; UP000002499; 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; cd07098; ALDH_F15-22; 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 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:UP000002499}.
FT DOMAIN 175..639
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 410
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 696 AA; 75496 MW; 2BCB0223291684D7 CRC64;
MSSSWWSNFP PVNPTPKPGR QSKPDMPLCK HQLLKSSWLL RNRQKSRAVA SREYFSSALN
QWRPSSWSGW RRGGTTSATT RLRDLTFRTD LSKAPVLLFL PTQLLTVPDI HRTTTLQIGC
AITAILISSI VTRLLVRAHA NSTPRPIRYR VPPAKLPETR TTVEQTSIRI PGTSAIQCYA
PATGQFLGLV NPSTPDGIDR AVAAASAAQR TWRQTSFRER RAVLRSLMQY VLDNAEDICR
VAGLDSGKTM VDAQLGEILV TVERIQWTLL HGEKALRPSR RPTNLLMAYK RNTVHYEPLG
VVSALVSWNY PFHNMMGPVI SALFAGNGIV VKVSEQTAWS SAHFAEIARG ALAAHGHDAG
LVQTVACWPQ TAGHLTSHPG ISHVTFIGSQ SVAHHVAASA ARSLTPVVAE LGGKDPFVVL
DSAARDLARI AEVVLRGTFQ AAGQNCIGIE RVIAAGRVYD RLVDMLAPRV RALRLGPDAD
VGAMISDASF DRLEELIAEA VSQGARLLAG GKRYDHPDYP SGHYFQPTLL VDVTTDMRIA
QHECFAPVLT MLRAKSSSAE DMLAVANAPN FGLGASVHGS ERDPAMGPIV RGLKAGMVAV
NDFAAYYAVQ LPFGGVAGSG YGRFAGEEGL RGLCNVKSVC EDRFWWMGIR TGIPPPVQYP
VPSQKKGWAF TQGVVEVGYG DGPRKIKGLG KILGNM
//