ID F0ZGT1_DICPU Unreviewed; 468 AA.
AC F0ZGT1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN ORFNames=DICPUDRAFT_150618 {ECO:0000313|EMBL:EGC36848.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC36848.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
CC ECO:0000256|RuleBase:RU003345}.
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DR EMBL; GL871015; EGC36848.1; -; Genomic_DNA.
DR RefSeq; XP_003286646.1; XM_003286598.1.
DR AlphaFoldDB; F0ZGT1; -.
DR STRING; 5786.F0ZGT1; -.
DR EnsemblProtists; EGC36848; EGC36848; DICPUDRAFT_150618.
DR GeneID; 10504018; -.
DR KEGG; dpp:DICPUDRAFT_150618; -.
DR eggNOG; KOG2456; Eukaryota.
DR InParanoid; F0ZGT1; -.
DR OMA; AWMKDQK; -.
DR OrthoDB; 606537at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IBA:GO_Central.
DR GO; GO:0030587; P:sorocarp development; IEA:EnsemblProtists.
DR CDD; cd07087; ALDH_F3-13-14_CALDH-like; 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 InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR036492,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064}.
FT DOMAIN 26..432
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 216
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 250
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ SEQUENCE 468 AA; 52438 MW; F845C84E114FF237 CRC64;
MSSSTGVALS SVSKNLRKVF LSQKTRKMDW RFSQLKALKK LISENKEDIT AAVKKDLGKH
EFEIHQTEIV MVQAECEETI SHLESWNKTE KVYSPIHFKP GSSYILKEPL GVVLIMSPWN
YPVNLALVPL IGAIAGGNCA LVKLSRHSYN VSKLLYELLT KYMDPECFVF DYEGGAQYIT
ELLEYKWDHI FFTGSVKVGK IVYAAAAKYL TPVTLELGGK NPCIVDKDTD IKFTARRLIW
GKCWNAGQTC IGLDYLLVHK SILQPLIEEF KSVLKEFFGE DIKKSPSFAR IISKAAAERL
ASLFTNGKVV IGGEADIEER YISPTVIVDP DLDSPLMTEE IFGPVLPIVA YENIDEAIEF
IQNRPHPLTL YCFSRDQSIQ DKVLDGTQSG SVMLNDCLLH FTNPQLPFGG IGDSGIGAYH
GKLTFDTFTH RRALVQSTTK KFLDLPLRYP PYTPMSDNIA SKIIGSGW
//
