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Database: UniProt
Entry: A0A010T0G0_PSEFL
LinkDB: A0A010T0G0_PSEFL
Original site: A0A010T0G0_PSEFL 
ID   A0A010T0G0_PSEFL        Unreviewed;       496 AA.
AC   A0A010T0G0;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase {ECO:0000313|EMBL:EXF96398.1};
GN   ORFNames=HK44_015720 {ECO:0000313|EMBL:EXF96398.1};
OS   Pseudomonas fluorescens HK44.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1042209 {ECO:0000313|EMBL:EXF96398.1, ECO:0000313|Proteomes:UP000022611};
RN   [1] {ECO:0000313|EMBL:EXF96398.1, ECO:0000313|Proteomes:UP000022611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HK44 {ECO:0000313|EMBL:EXF96398.1,
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:EXF96398.1}.
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DR   EMBL; AFOY02000002; EXF96398.1; -; Genomic_DNA.
DR   RefSeq; WP_019689635.1; NZ_AFOY02000002.1.
DR   AlphaFoldDB; A0A010T0G0; -.
DR   PATRIC; fig|1042209.11.peg.284; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_2_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; cd07112; ALDH_GABALDH-PuuC; 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; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR11699:SF291; NADP_NAD-DEPENDENT ALDEHYDE DEHYDROGENASE PUUC; 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          34..491
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   496 AA;  53179 MW;  A9F2D0C3C2955760 CRC64;
     MAITRSDWEQ RFQSLTIEGR AFIDGHYCSA LSRDTFECVS PVDGRFLANV ASTDEADANV
     AVQVARRAFE SGVWAKLAPA ERKRILIRFA DLILANQEEL ALLETLDMGK PIGDAMSIDI
     PATANAIRWS AEAIDKIYDE VAATPHDQLG LVTREPSGVV AAIVPWNFPL IMASWKFAPA
     LAAGNSFILK PSEKSPLTAI RIAQLALDAG IPKGVFNVLP GFGHTVGKAL ALHMDVDVLA
     FTGSTAIAKQ LLIYAGQSNM KRVWLEAGGK SPNVVFADAP DLRAAAQAAA SAIAFNQGEV
     CTAGSRLLVE RSIREQFIPL LVEALQAWKP GHALDPATTV GAVVDQRQLD NVLRYISIGK
     EQGAQLIAGG NRTLEDTGGL YVEPAIFDGV TNAMTIAREE IFGPVLSLIT FDTAEEALAI
     ANDSIFGLAA GVWTSNLSKA HTFARGLRAG SVWVNQYDGG DMTAPFGGFK QSGNGRDKSL
     HAFDKYTELK ATWIKL
//
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