ID A0A0S2DFB3_LYSEN Unreviewed; 510 AA.
AC A0A0S2DFB3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=aldehyde dehydrogenase (NAD(+)) {ECO:0000256|ARBA:ARBA00024226};
DE EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226};
GN ORFNames=FE772_09085 {ECO:0000313|EMBL:QCW25798.1}, GLE_1765
GN {ECO:0000313|EMBL:ALN57120.1};
OS Lysobacter enzymogenes.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=69 {ECO:0000313|EMBL:ALN57120.1, ECO:0000313|Proteomes:UP000061569};
RN [1] {ECO:0000313|EMBL:ALN57120.1, ECO:0000313|Proteomes:UP000061569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3 {ECO:0000313|EMBL:ALN57120.1,
RC ECO:0000313|Proteomes:UP000061569};
RA Kobayashi D.Y.;
RT "Genome sequences of Lysobacter enzymogenes strain C3 and Lysobacter
RT antibioticus ATCC 29479.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QCW25798.1, ECO:0000313|Proteomes:UP000308311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC36 {ECO:0000313|EMBL:QCW25798.1,
RC ECO:0000313|Proteomes:UP000308311};
RA Feng T.;
RT "Intraspecies Signal LeDSF and Interspecies Signal Indole Synergistically
RT Regulate the Twitching Motility of Lysobacter enzymogenes.";
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CP013140; ALN57120.1; -; Genomic_DNA.
DR EMBL; CP040656; QCW25798.1; -; Genomic_DNA.
DR RefSeq; WP_057947036.1; NZ_CP040656.1.
DR AlphaFoldDB; A0A0S2DFB3; -.
DR STRING; 69.GLE_1765; -.
DR KEGG; lez:GLE_1765; -.
DR PATRIC; fig|69.6.peg.1741; -.
DR OrthoDB; 9812625at2; -.
DR Proteomes; UP000061569; Chromosome.
DR Proteomes; UP000308311; Chromosome.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR CDD; cd07130; ALDH_F7_AASADH; 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; IPR044638; ALDH7A1-like.
DR PANTHER; PTHR43521; ALPHA-AMINOADIPIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43521:SF1; ALPHA-AMINOADIPIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR Pfam; PF00171; Aldedh; 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|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000061569}.
FT DOMAIN 28..491
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 264
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 510 AA; 54229 MW; 7345DA6E70A93B33 CRC64;
MTHPVLAALG LKDNESGTYL GHGEWSKTAD AGVLEPVNPT DGEVLARVQA SSQSDYDTIV
ERAQAAFAVW RTTPAPRRGE AIRLCSDALR KHKDALGSLV ALEMGKSKPE GDGEVQEMID
IGDFAVGLSR QLYGLTMHSE RPGHRMYEQW HPLGIVGIIS AFNFPVAVWA WNSFIAAICG
DISIWKPSPK TPLSAIASMK ICNEALRAGG FPDLFFLFND AGTELASNFV DDKRIGLVSF
TGSTKVGRAV GERVARRMGR SLLELGGNNA IIVDASADLK LAIPAIAFGA VGTAGQRCTT
TRRLFVHESI HDDVLAKLVA AYKQVEKKIG DPTDPANLMG PLNSQDGVQA YLDAIAKAKA
SGGKVETGGE RIDRKGNFVL PAIVTGLTND AEVVQTETFA PILYVMKFSR LEDAIALQND
VPQGLSSSIF TANLKAAEAF LSAAGSDCGI ANVNIGTSGA EIGGAFGGEK ETGGGRESGS
DAWRAYMRRQ TNTINYSDAL PLAQGIKFDL
//
