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Database: UniProt
Entry: A0A0N1PB61_LEPSE
LinkDB: A0A0N1PB61_LEPSE
Original site: A0A0N1PB61_LEPSE 
ID   A0A0N1PB61_LEPSE        Unreviewed;       584 AA.
AC   A0A0N1PB61;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Putative aldehyde dehydrogenase {ECO:0000313|EMBL:KPI85083.1};
GN   ORFNames=ABL78_5849 {ECO:0000313|EMBL:KPI85083.1};
OS   Leptomonas seymouri.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX   NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI85083.1, ECO:0000313|Proteomes:UP000038009};
RN   [1] {ECO:0000313|EMBL:KPI85083.1, ECO:0000313|Proteomes:UP000038009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI85083.1,
RC   ECO:0000313|Proteomes:UP000038009};
RX   PubMed=26317207;
RA   Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA   Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA   Yurchenko V.;
RT   "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT   Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT   donovani.";
RL   PLoS Pathog. 11:E1005127-E1005127(2015).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {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:KPI85083.1}.
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DR   EMBL; LJSK01000209; KPI85083.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1PB61; -.
DR   EnsemblProtists; KPI85083; KPI85083; ABL78_5849.
DR   VEuPathDB; TriTrypDB:Lsey_0209_0070; -.
DR   OMA; ILMRGTF; -.
DR   OrthoDB; 5743at2759; -.
DR   Proteomes; UP000038009; 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; 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}.
FT   DOMAIN          64..514
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        298
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   584 AA;  63906 MW;  AC9798DAFFEEAD77 CRC64;
     MLLCWFVVAD VLYRAYAVFK WIWACITQTV DRYTAPVIKV PLPEVNFPAA PAAEPLNPRS
     AGEGKIQCYD KGTNTPIGVV KAYTPDEVRE AVEKARKAQQ IWALTPFSTR RKLLFALMDY
     ILANQEFICK TACVECGKTM MDGTLGEMLT TFEKLRWTAS RGEEALQEEV RDVGLMTIHK
     RASVRYVPFG VIGAIVSWNY PFHNIYGPMI SALFAGNAFV GKVSEYSSFY ASYYESIVKD
     GLRQLGYSPD LVSFVTGFAD TGETIVSSVD KLTFIGSPGV GKIVMRNASA TLTPVVLELG
     GKDPAVICDD ADMKQVIPVV MRGNFQNCGQ NCVGLERIIA HEKVHDQLVE EVIRQVRGLT
     QGAASQGQYD LGAMTMGKAA IPKIQQLVDE TVKAGAKLVC GGKMNGDMFY PPTVLINVTP
     DMPIAQEEVF GPVMVIMKFK TDDEAVKMVN ACAYGLGSSV FSLNIPRAQA IADRIRTGMV
     NINDFGINYL CQSLPFGGVK ISGFDRFAGR EGLRGNCVVR ASTTDRIPGV KTEIPAILQY
     PIRPAAFTFM ENLAQVIYGR LPNMITSAMK LATIKPDSAD KKTA
//
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