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Database: UniProt
Entry: A5WAF4_PSEP1
LinkDB: A5WAF4_PSEP1
Original site: A5WAF4_PSEP1 
ID   A5WAF4_PSEP1            Unreviewed;       474 AA.
AC   A5WAF4;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   OrderedLocusNames=Pput_4994 {ECO:0000313|EMBL:ABQ81114.1};
OS   Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746 {ECO:0000313|EMBL:ABQ81114.1};
RN   [1] {ECO:0000313|EMBL:ABQ81114.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F1 {ECO:0000313|EMBL:ABQ81114.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT   "Complete sequence of Pseudomonas putida F1.";
RL   Submitted (MAY-2007) 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}.
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DR   EMBL; CP000712; ABQ81114.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5WAF4; -.
DR   KEGG; ppf:Pput_4994; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_3_6_6; -.
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          18..444
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        221
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        255
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ   SEQUENCE   474 AA;  52231 MW;  43C41F2F1E3A8F9D CRC64;
     MNSPSALPPL QFDLATTFAA QRQAFAGNPL PPAAQRRQWL KSLREALLSS QAELIEAISQ
     DFAGRSADET LLAELLPSVQ GLRHAEKHLQ SWMRTRRRRV GLAFQPASAQ VRYQPLGVVG
     IMVPWNYPLF LAIGPLTCAL AAGNRVMLKL SEATPATGLA LQQLLERVFP TDLVSVVLGE
     VEVGQAFARL PFDHLLFTGA TSVGRQVMQA AAHNLTPVTL ELGGKSPAIV SDDVPLDSAA
     ERIAFGKTLN AGQTCVAPDY VLVPRERLPA FSDAYQRAVH RLYPRIADNP DYTAIINPRQ
     LQRLQHLLDD ARAKGAQVLD LYPGEAPQGR RLPPHLLLDV NDSMQVMQDE IFGPLLPLVP
     YDGLDQALAY INQRPRPLAL YFFGYDRHTQ EHVLRHTHSG GVCLNDTLLH VAQDDLPFGG
     IGPSGMGHYH GHDGFLTFSK AKAVLAKQRF NAARLIYPPY GKALQRLVYK LFIR
//
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