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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//