ID A0A103XNB4_CYNCS Unreviewed; 428 AA.
AC A0A103XNB4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Aldehyde dehydrogenase, conserved site-containing protein {ECO:0000313|EMBL:KVH93921.1};
GN ORFNames=Ccrd_004028 {ECO:0000313|EMBL:KVH93921.1};
OS Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC Carduinae; Cynara.
OX NCBI_TaxID=59895 {ECO:0000313|EMBL:KVH93921.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVH93921.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVH93921.1};
RX PubMed=26786968; DOI=10.1038/srep19427;
RA Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT "The genome sequence of the outbreeding globe artichoke constructed de novo
RT incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL Sci. Rep. 6:19427-19427(2016).
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:KVH93921.1}.
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DR EMBL; LEKV01004585; KVH93921.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A103XNB4; -.
DR STRING; 59895.A0A103XNB4; -.
DR EnsemblPlants; KVH93921; KVH93921; Ccrd_004028.
DR Gramene; KVH93921; KVH93921; Ccrd_004028.
DR OMA; GMWKIAP; -.
DR Proteomes; UP000243975; 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; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR11699:SF293; RETINAL DEHYDROGENASE 1-RELATED; 1.
DR Pfam; PF00171; Aldedh; 2.
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:UP000243975}.
FT DOMAIN 20..247
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 252..418
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 239
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 428 AA; 46287 MW; 0BF371DB18503DB1 CRC64;
MSSRKHDIKF TKLFINGEFV DSISGNTFET IDPATEQVLA TVAEGRKEDV DLAARRKILL
KFADLIDENA DELATLEVID GGKLFAPVRY FEVPISSETF RYFAGAADKI RGATLKMSSN
IQAYTLREPV GVVGHIIPWN GPAYMFATKV APALAAGCTM VVKPAEQTPL TVLFFAHLSK
MAGVPDGVIN VVNGFGNTAG AAVSSHMDID AVTFTGSTEV GRAVMHAAAS SNLKPVSLEL
GGKSPFIKLE VMVKGWATGD PFDLATRHGP QNNKQQYKKV LSCIENGKKE GATLVTGGKP
FGKKGYYIEP TLFTNVTDDM SLAKEEIFGP VISVFKFKTM DEVIKRANAT KYGLASGVMT
KNIDIANTVS RSIRAGAVWV NCFIALDRDA PHGGYKMSGF GREQGLEALE HYLQVKTVAT
PIYDSPWL
//