ID   A6FJ42_9GAMM            Unreviewed;       521 AA.
AC   A6FJ42;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=aldehyde dehydrogenase (NAD(+)) {ECO:0000256|ARBA:ARBA00024226};
DE            EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226};
GN   ORFNames=PE36_09898 {ECO:0000313|EMBL:EDM64843.1};
OS   Moritella sp. PE36.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Moritellaceae; Moritella.
OX   NCBI_TaxID=58051 {ECO:0000313|EMBL:EDM64843.1, ECO:0000313|Proteomes:UP000004278};
RN   [1] {ECO:0000313|EMBL:EDM64843.1, ECO:0000313|Proteomes:UP000004278}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PE36 {ECO:0000313|EMBL:EDM64843.1,
RC   ECO:0000313|Proteomes:UP000004278};
RA   Yayanos A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (JUN-2007) 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}.
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:EDM64843.1}.
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DR   EMBL; ABCQ01000080; EDM64843.1; -; Genomic_DNA.
DR   RefSeq; WP_006034397.1; NZ_ABCQ01000080.1.
DR   AlphaFoldDB; A6FJ42; -.
DR   STRING; 58051.PE36_09898; -.
DR   OrthoDB; 9812625at2; -.
DR   Proteomes; UP000004278; Unassembled WGS sequence.
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}.
FT   DOMAIN          34..496
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   521 AA;  56275 MW;  13F7EB9CAC405A31 CRC64;
     MHEAILKTVL GDFYAQDKHY GSAFLGDQCF DSETKVDVIS PNNGQKFVSI SHAQPDVIEN
     VINSAKTEFY HWRSVPAPQR GELVRLFAEK ARAAKHQLAT IISLEAGKPF QESLGEVQEL
     IDVCDFAVGL SRQLYGLTIA TERPNHRMME QWHPIGPVVI ITAFNFPMAV WAWNATLSLI
     CGNSIIWKPS SQTPLSALAC HRLLLSAIKQ FGGNAELSSI VFGEKTQVEQ LVDHKDIALV
     SATGSCAMGR AVNCRVAARL GRTLLELGGN NAMIVCPSAD LELAIRAITF SALGTSGQRC
     TTLRRLIVHS SLKHQVLTKL EAIYKTVSIG DPFDGLNLMG PLINQHAIDS MTVSINTAIS
     QGGKLITGGE RVSNLSNKGK EEHGFYITPA IVDIDPQADI VQQETFAPLL YVHSYDSLEQ
     AIAIQNSVSQ GLSSAIFTKD MAEAEIFMSA NGSDCGLVNV NIGTSGAEIG GAFGGEKDTG
     GGRESGSDAW KSYMRRMTNT INYGSELPLA QGISFDMPKG E
//