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}.
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; 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
//