ID   A0A2S8YR88_9PSED        Unreviewed;       476 AA.
AC   A0A2S8YR88;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   ORFNames=CQZ98_02515 {ECO:0000313|EMBL:PRA60112.1};
OS   Pseudomonas sp. MYb115.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1848717 {ECO:0000313|EMBL:PRA60112.1, ECO:0000313|Proteomes:UP000239970};
RN   [1] {ECO:0000313|EMBL:PRA60112.1, ECO:0000313|Proteomes:UP000239970}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MYb115 {ECO:0000313|EMBL:PRA60112.1,
RC   ECO:0000313|Proteomes:UP000239970};
RA   Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA   Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA   Kaleta C., Schulenburg H.;
RT   "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT   from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
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:PRA60112.1}.
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DR   EMBL; PCQM01000001; PRA60112.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S8YR88; -.
DR   Proteomes; UP000239970; 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   GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR   CDD; cd07133; ALDH_CALDH_CalB; 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|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR036492}.
FT   DOMAIN          33..445
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        225
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        259
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ   SEQUENCE   476 AA;  52634 MW;  906B60D45B60D07C CRC64;
     MTADIAYMQN AQQPLSELNE LFTAQRLAYA GNPMPSAAQR QQWLKVLRDV LDTQRDRLIK
     AISEDFSNRS ADETLFAELM PSLHNIDYAS KHLRGWMKAS RRKVGVAFQP ASAKVVYQPL
     GVVGVIVPWN YPLYLAIGPL VGALAAGNRV MLKLSESTPA TGQLLKELLA HIFPQDLVTV
     VLGEADVGIA FSSLPFDHLL FTGATSVGKH VMRAAAENLT PVTLELGGKS PAIVSHDVPL
     KDAAERIAFG KTLNAGQTCV APDYVLVPEG RVDAFVDAYR QAVRRFYPTL VNNPDYTAII
     NQRQLARLNS YVSDATSKGA QLIPIYDQDQ DRRMSHSLLL NVSDEMLVMQ DEIFGPLLPI
     VPYSTLDQAF AYINQRPRPL ALYYFGYNKS EQNRVLHETH SGGVCLNDTL LHVAQDDMPF
     GGIGPSGMGH YHGHEGFLTF SKAKGVLIKQ RFNAAKLIYP PYGKSIQKLI QKLFIR
//