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Database: UniProt
Entry: W0BF57_9GAMM
LinkDB: W0BF57_9GAMM
Original site: W0BF57_9GAMM 
ID   W0BF57_9GAMM            Unreviewed;       455 AA.
AC   W0BF57;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=NAD-dependent aldehyde dehydrogenase {ECO:0000313|EMBL:AHE67074.1};
DE            EC=1.2.1.16 {ECO:0000313|EMBL:AHE67074.1};
GN   ORFNames=Loa_01525 {ECO:0000313|EMBL:AHE67074.1};
OS   Legionella oakridgensis ATCC 33761 = DSM 21215.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=1268635 {ECO:0000313|EMBL:AHE67074.1, ECO:0000313|Proteomes:UP000018838};
RN   [1] {ECO:0000313|EMBL:AHE67074.1, ECO:0000313|Proteomes:UP000018838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OR-10, ATCC 33761 {ECO:0000313|Proteomes:UP000018838};
RX   PubMed=23932911; DOI=10.1016/j.ijmm.2013.07.003;
RA   Brzuszkiewicz E., Schulz T., Rydzewski K., Daniel R., Gillmaier N.,
RA   Dittmann C., Holland G., Schunder E., Lautner M., Eisenreich W., Luck C.,
RA   Heuner K.;
RT   "Legionella oakridgensis ATCC 33761 genome sequence and phenotypic
RT   characterization reveals its replication capacity in amoebae.";
RL   Int. J. Med. Microbiol. 303:514-528(2013).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP004006; AHE67074.1; -; Genomic_DNA.
DR   RefSeq; WP_025385679.1; NZ_CP004006.1.
DR   AlphaFoldDB; W0BF57; -.
DR   STRING; 1268635.Loa_01525; -.
DR   KEGG; lok:Loa_01525; -.
DR   PATRIC; fig|1268635.3.peg.1551; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_6; -.
DR   Proteomes; UP000018838; Chromosome.
DR   GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro.
DR   GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR   CDD; cd07100; ALDH_SSADH1_GabD1; 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; IPR044148; ALDH_GabD1-like.
DR   InterPro; IPR047110; GABD/Sad-like.
DR   PANTHER; PTHR43217; SUCCINATE SEMIALDEHYDE DEHYDROGENASE [NAD(P)+] SAD; 1.
DR   PANTHER; PTHR43217:SF1; SUCCINATE SEMIALDEHYDE DEHYDROGENASE [NAD(P)+] SAD; 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:UP000018838}.
FT   DOMAIN          3..452
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        228
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   455 AA;  50200 MW;  A2B0913F8CBA644D CRC64;
     MQIKTINPAT EEILQSYPLF KEEQVHAFID AAHLCYQAWR KTSFSQRRQR MLKMAELLRK
     KQEEYAALMA KEMGKPLTAG KSEIEKCAWV CEHFAKQAEQ YLAPRLIQTE MTKTKVCYQP
     LGVVFAIMPW NFPFWQVFRF AAPTIMAGNA AILKHAPIST GAGNAIAELF LEAGFPEHLF
     QHFILDNELA AKVIANEKIV GVSLTGSEKA GSIVASHAAS HLKKSVLELG GNDPYIILAD
     ADLELAANCV VTSRMNNSGQ VCIAAKRTIV VDEVVEEFVE HIVKLVEKFQ MGNPLDPSTN
     FGPMARKDLR DTLHQQVLDS EKKGAKILRG GTVPHRKGFY YPPTILTNVS PGMPAFDDEL
     FGPVIAIVSA EDEAHAIRLA NQSKYGLGGA VFTSDLARGE KIATEEIEVG SCFVNTYVAS
     DPRVPFGGIK RSGFGREISR EGILEFVNTK TVSIK
//
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