ID G3J476_CORMM Unreviewed; 507 AA.
AC G3J476;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Aldehyde dehydrogenase X {ECO:0000313|EMBL:EGX95798.1};
GN ORFNames=CCM_00452 {ECO:0000313|EMBL:EGX95798.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX95798.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX95798.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX95798.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(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; JH126399; EGX95798.1; -; Genomic_DNA.
DR RefSeq; XP_006665675.1; XM_006665612.1.
DR AlphaFoldDB; G3J476; -.
DR STRING; 983644.G3J476; -.
DR GeneID; 18162487; -.
DR KEGG; cmt:CCM_00452; -.
DR VEuPathDB; FungiDB:CCM_00452; -.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_0_1; -.
DR InParanoid; G3J476; -.
DR OMA; DAQSFSC; -.
DR OrthoDB; 216092at2759; -.
DR Proteomes; UP000001610; 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; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR PANTHER; PTHR11699:SF206; ALDEHYDE DEHYDROGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-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:UP000001610}.
FT DOMAIN 27..461
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 260
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 507 AA; 54833 MW; 41292D6A94E38806 CRC64;
MPPPFKTPAV TDLTKFWING EYVEPLNKEV FTVRNPKNDQ VVSRNVPIGG PQDVDNAVKH
AEAAFQGDWS RFSSAQRGLC LSRLADIMDE HLEGLLRLDT MTGGNPVSLI PTREKNYIVN
GLRYMSGWCD KFKGEYMPDD DGFVKLVRHE PLGVCAAICP FNSPIATAFH KIGPALVTGN
VIIVKPSEKT PFGTLALGPL IAMAGIPSGV VQVISGHGTT GELLARHMRI RKISFTGSVA
TGKKIQVASA QSNLKRATLE LGGKSPAVIF DDANLENALE WTVKAIMARS GQVCIAASRV
YVQKSIAKEF IQRYQQKMLD AAKSMGDPED PNVAYGPLVD KISFERVKGM LERAKDQAEL
VVGGGVIGNS GCFIEPTVFV NPKPGAEIVT DEVFGPVSVI DTFETEEEVL AKANDTEFGL
MAGVFTRDIT RALRVSSKFE SGVVGINCVS YVRPTSIHGA KDGVDQHELY TQSLYVQNCQ
PTRGFQESGP ALQAMVMRPT GGSAVQS
//
