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Database: UniProt
Entry: A0A0Q0SSL7_9PSED
LinkDB: A0A0Q0SSL7_9PSED
Original site: A0A0Q0SSL7_9PSED 
ID   A0A0Q0SSL7_9PSED        Unreviewed;       476 AA.
AC   A0A0Q0SSL7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   ORFNames=AQS70_18965 {ECO:0000313|EMBL:KQB55278.1};
OS   Pseudomonas endophytica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1563157 {ECO:0000313|EMBL:KQB55278.1, ECO:0000313|Proteomes:UP000050342};
RN   [1] {ECO:0000313|EMBL:KQB55278.1, ECO:0000313|Proteomes:UP000050342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSTT44 {ECO:0000313|EMBL:KQB55278.1,
RC   ECO:0000313|Proteomes:UP000050342};
RA   Von Neubeck M., Huptas C., Wenning M., Scherer S.;
RT   "Pseudomonas helleri sp. nov. and Pseudomonas weihenstephanensis sp. nov.,
RT   isolated from raw cows milk.";
RL   Submitted (OCT-2015) 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:KQB55278.1}.
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DR   EMBL; LLWH01000014; KQB55278.1; -; Genomic_DNA.
DR   RefSeq; WP_055101347.1; NZ_LLWH01000014.1.
DR   AlphaFoldDB; A0A0Q0SSL7; -.
DR   STRING; 1563157.AQS70_18965; -.
DR   OrthoDB; 9812625at2; -.
DR   Proteomes; UP000050342; 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          19..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;  53066 MW;  E192AF60F3FC1DB1 CRC64;
     MSFDSTHPFS SSHSQSNLNS LFAQQREAYS AHPFPLLAQR HQWLNSLRDM LSREREVLID
     AISQDFSHRS PDETLFAELM PSLHSIDYTL KHLKRWMKPS SRHVGVMFQP ANAKVVYQPL
     GVIGVVVPWN YPLYLAMGPL IGALAAGNRV MLKLSEYTPA SGRLLKDLLG RIFPEDMVTV
     VLGDAQVAVA FCGLPFDHLL FTGSTHVGKQ VMRAAAENLT PVTLELGGKS PAIVSAEVPL
     KDAAQRIAWG KTLNAGQTCI APDYVLVPHD RVDGFVEAYR QAVQGFYPTL TDNPDYTAII
     SERQLARLEH LQSDATEKGA RLISLYAQGQ GRRMPHALLL EVNDDMQVMQ DEIFGPLLPI
     VAYHTLDEAL TYINSRPRPL ALYYFGYNKS EQQRVIENTH SGGVSINETL LHVAIDDLPF
     GGVGHSGMGH YHGHEGFMTF SQAKGVLVKQ RWNSSQAIYP PYGRKLVRLI QKLFIR
//
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