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Database: UniProt
Entry: A0A1X0JHG7_9MYCO
LinkDB: A0A1X0JHG7_9MYCO
Original site: A0A1X0JHG7_9MYCO 
ID   A0A1X0JHG7_9MYCO        Unreviewed;       500 AA.
AC   A0A1X0JHG7;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:ORB62382.1};
GN   ORFNames=BST47_23905 {ECO:0000313|EMBL:ORB62382.1};
OS   Mycolicibacterium tusciae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=75922 {ECO:0000313|EMBL:ORB62382.1, ECO:0000313|Proteomes:UP000192411};
RN   [1] {ECO:0000313|EMBL:ORB62382.1, ECO:0000313|Proteomes:UP000192411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44153 {ECO:0000313|Proteomes:UP000192411};
RA   Tortoli E., Trovato A., Cirillo D.M.;
RT   "The new phylogeny of genus Mycobacterium.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00024149};
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {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:ORB62382.1}.
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DR   EMBL; MVIM01000016; ORB62382.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X0JHG7; -.
DR   STRING; 75922.BST47_23905; -.
DR   eggNOG; COG1012; Bacteria.
DR   OrthoDB; 6882680at2; -.
DR   Proteomes; UP000192411; Unassembled WGS sequence.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProt.
DR   GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
DR   CDD; cd07139; ALDH_AldA-Rv0768; 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; PTHR42804; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42804:SF1; ALDEHYDE DEHYDROGENASE-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          29..490
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   500 AA;  53232 MW;  B83D782A3EAA42FB CRC64;
     MTQTVAHKTP AGEPAYRTQW DKLFIGGKWV EPASSEVIEV RSPATGEVVG KVPLATEADV
     NAACAAARKA FDEGPWPHMK PQERAAILAA AIKGMEERAD ELKYLLAAET GQPQTIVDMM
     QYGAAMSAFQ YYAGAADKFP WRDIRDGVYG QTLVVREPIG VVGAVTAWNV PFFLAANKLG
     PAFLAGCTVV LKPAAETPLS VFAMAEIFAE AGLPEGVLSI VPGGPETGRA LTSNPELDKF
     TFTGSSAVGK EIAKIAAEKL KPCTLELGGK SAAIILEDAD LDATLPMLGF SGVMNSGQAC
     VAQTRILAPR SRYDEVVEKL SNFISAMPVG LPDDPNAAIG PLISEKQRER VEGYIKKGVE
     EGARIVTGGG RPEGLDSGWF VQPTVFADVD NSMTIAQEEI FGPVLAVIPY ETEEDAIRIA
     NDSVYGLAGS VWTTDNKKAI EIAKKIRTGT YAVNMYAFDP CAPFGGYKNS GVGRENGPEG
     IEAYVEPKSV LLPFGYTPED
//
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