ID   A0A0N9XHB5_MYCFO        Unreviewed;       516 AA.
AC   A0A0N9XHB5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=aldehyde dehydrogenase (NAD(+)) {ECO:0000256|ARBA:ARBA00024226};
DE            EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226};
GN   ORFNames=XA26_18070 {ECO:0000313|EMBL:ALI25654.1};
OS   Mycolicibacterium fortuitum (Mycobacterium fortuitum).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1766 {ECO:0000313|EMBL:ALI25654.1, ECO:0000313|Proteomes:UP000057134};
RN   [1] {ECO:0000313|EMBL:ALI25654.1, ECO:0000313|Proteomes:UP000057134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT6 {ECO:0000313|EMBL:ALI25654.1,
RC   ECO:0000313|Proteomes:UP000057134};
RX   PubMed=26507234; DOI=10.1128/mBio.01520-15;
RA   Costa K.C., Bergkessel M., Saunders S., Korlach J., Newman D.K.;
RT   "Enzymatic Degradation of Phenazines Can Generate Energy and Protect
RT   Sensitive Organisms from Toxicity.";
RL   MBio 6:e01520-e01515(2015).
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; CP011269; ALI25654.1; -; Genomic_DNA.
DR   RefSeq; WP_054601654.1; NZ_CP011269.1.
DR   AlphaFoldDB; A0A0N9XHB5; -.
DR   STRING; 1766.XA26_18070; -.
DR   KEGG; mft:XA26_18070; -.
DR   PATRIC; fig|1766.6.peg.1788; -.
DR   Proteomes; UP000057134; 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:UP000057134}.
FT   DOMAIN          45..496
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        272
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   516 AA;  54242 MW;  B8DAD1E367EB9A2D CRC64;
     MTTTERTDLP TAKELRRRVR QALDAVGARA ELGEPTAPGP GLHASTPISG DVLFTLPEDS
     ADQVDAAIAA AAQSFSSWRT TPAPVRGALV ARLGELLIEH KADLATLVTV EAGKITSEAL
     GEVQEMIDIC QFAVGLSRQL YGRTIASERP GHRLMETWHP LGVVGVITAF NFPVAVWSWN
     TAIALVCGDT VVWKPSELTP LTAIACQALI ERAATDVGAP AEVSRLILGG RELGEQLVDD
     PRVALVSATG SVRMGQQVAP RVAARFGKVL LELGGNNAAI VAPSADLDLA VRAIVFSAAG
     TAGQRCTSLR RLIVHSSIAD DLVSRIVSAY QSLPIGDPSV DGTLVGPLIH TRAYRDMVGA
     LEQARADGGK VFGGQRHDLG DEGAFYVAPA VVRMPAQTPV VHTETFAPIL YVLTYDDLNE
     AIDLNNAVPQ GLSSAIFTTD VREAERFMAA DGSDCGIANV NIGTSGAEIG GAFGGEKHTG
     GGRESGSDAW KAYMRRATNT VNYSSELPLA QGVHFG
//