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Database: UniProt
Entry: A0A010T3X7_PSEFL
LinkDB: A0A010T3X7_PSEFL
Original site: A0A010T3X7_PSEFL 
ID   A0A010T3X7_PSEFL        Unreviewed;       481 AA.
AC   A0A010T3X7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:EXF92267.1};
GN   ORFNames=HK44_011950 {ECO:0000313|EMBL:EXF92267.1};
OS   Pseudomonas fluorescens HK44.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1042209 {ECO:0000313|EMBL:EXF92267.1, ECO:0000313|Proteomes:UP000022611};
RN   [1] {ECO:0000313|EMBL:EXF92267.1, ECO:0000313|Proteomes:UP000022611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HK44 {ECO:0000313|EMBL:EXF92267.1,
RC   ECO:0000313|Proteomes:UP000022611};
RX   PubMed=21742869; DOI=10.1128/JB.05530-11;
RA   Chauhan A., Layton A.C., Williams D.E., Smartt A.E., Ripp S.,
RA   Karpinets T.V., Brown S.D., Sayler G.S.;
RT   "Draft genome sequence of the polycyclic aromatic hydrocarbon-degrading,
RT   genetically engineered bioluminescent bioreporter Pseudomonas fluorescens
RT   HK44.";
RL   J. Bacteriol. 193:5009-5010(2011).
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:EXF92267.1}.
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DR   EMBL; AFOY02000018; EXF92267.1; -; Genomic_DNA.
DR   RefSeq; WP_019691871.1; NZ_AFOY02000018.1.
DR   AlphaFoldDB; A0A010T3X7; -.
DR   PATRIC; fig|1042209.11.peg.4798; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_6; -.
DR   OrthoDB; 9812625at2; -.
DR   Proteomes; UP000022611; 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:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   CDD; cd07097; ALDH_KGSADH-YcbD; 1.
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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000022611}.
FT   DOMAIN          22..476
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        250
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   481 AA;  51110 MW;  395A74C5B20BB9DE CRC64;
     MADVKRYDNY IDGQWGAGAE YSANINPSEL SDVIGEYAKA DLAQVNAAID AARAAFPAWS
     TSGIQARSDA LDKVGSEILA RREELGTLLA REEGKTLPEA IGEVSRAGNI FKFFAGECLR
     LSGDYLPSVR PGVNVEVTRE ALGVVGLITP WNFPIAIPAW KIAPALAYGN CVVLKPAELV
     PGCAWALAEI ISRAGFPAGV FNLVMGSGRV IGDAMVNSPK VDGISFTGSV GVGRQIAVNC
     VSRQAKVQLE MGGKNPQIIL DDADLKQAVE LSVQSAFYST GQRCTASSRL IVTAGIHDKF
     VEAMAERMKS IKVGHALKSG TDIGPVVSQA QLEQDLKYID IGQSEGARLV SGGGLVTCDT
     EGYYLAPTLF ADSEAAMRIS REEIFGPVAN IVRVADYDAA LAMANDTEFG LSAGIATTSL
     KYANHFKRHS QAGMVMVNLP TAGVDYHVPF GGRKGSSYGS REQGRYAQEF YTVVKTSYIG
     S
//
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