ID Q4K5E6_PSEF5 Unreviewed; 506 AA.
AC Q4K5E6;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:AAY94679.1};
DE EC=1.2.1.- {ECO:0000313|EMBL:AAY94679.1};
GN OrderedLocusNames=PFL_5469 {ECO:0000313|EMBL:AAY94679.1};
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY94679.1, ECO:0000313|Proteomes:UP000008540};
RN [1] {ECO:0000313|EMBL:AAY94679.1, ECO:0000313|Proteomes:UP000008540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5
RC {ECO:0000313|Proteomes:UP000008540};
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S.III.,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CP000076; AAY94679.1; -; Genomic_DNA.
DR RefSeq; WP_011063687.1; NC_004129.6.
DR AlphaFoldDB; Q4K5E6; -.
DR SMR; Q4K5E6; -.
DR STRING; 220664.PFL_5469; -.
DR World-2DPAGE; 0008:Q4K5E6; -.
DR GeneID; 57478433; -.
DR KEGG; pfl:PFL_5469; -.
DR PATRIC; fig|220664.5.peg.5586; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_2_6; -.
DR Proteomes; UP000008540; Chromosome.
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; cd07559; ALDH_ACDHII_AcoD-like; 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; PTHR43111; ALDEHYDE DEHYDROGENASE B-RELATED; 1.
DR PANTHER; PTHR43111:SF1; ALDEHYDE DEHYDROGENASE B-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}.
FT DOMAIN 34..493
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 506 AA; 55029 MW; 3AAB85A4855D5A5A CRC64;
MRYAHPGTEG AIVSFKSKYG NYIGGEFVAP VKGQYFTNTS PVNGQPIAEF PRSTAEDIDK
ALDAAHAAAD AWGATSVQAR SLILLKIADR IEQNLELLAI TETWDNGKAV RETLNADIPL
AADHFRYFAG CLRAQEGSAA EIDGNTVAYH IHEPLGVVGQ IIPWNFPILM AAWKLAPALA
AGNCVVLKPA EQTPLGITVL MEVIGDLLPP GVLNVVQGFG REAGEALATS KRIAKIAFTG
STPVGSHIMK CAAENIIPST VELGGKSPNI FFEDIMQAEP KFIEKAAEGL VLAFFNQGEV
CTCPSRALVQ ESIYDEFMQV VMKKIEQIKR GDPLDTDTMV GAQASEQQFD KILSYLDIAK
NEGAQLLTGG KVEKLEGDLS SGYYIQPTLL KGTNKMRVFQ EEIFGPVVSV TTFKDEAEAL
AIANDTEFGL GAGVWTRDIN RAYRMGRGIK AGRVWTNCYH LYPAHAAFGG YKKSGVGRET
HKMMLDHYQQ TKNLLVSYDI NPLGFF
//
