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Database: UniProt
Entry: A0A1A2BE94_9MYCO
LinkDB: A0A1A2BE94_9MYCO
Original site: A0A1A2BE94_9MYCO 
ID   A0A1A2BE94_9MYCO        Unreviewed;       488 AA.
AC   A0A1A2BE94;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:OBF66390.1};
GN   ORFNames=A5753_06665 {ECO:0000313|EMBL:OBF66390.1};
OS   Mycobacterium sp. 852002-51971_SCH5477799-a.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834106 {ECO:0000313|EMBL:OBF66390.1, ECO:0000313|Proteomes:UP000091887};
RN   [1] {ECO:0000313|EMBL:OBF66390.1, ECO:0000313|Proteomes:UP000091887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=852002-51971_SCH5477799-a {ECO:0000313|EMBL:OBF66390.1,
RC   ECO:0000313|Proteomes:UP000091887};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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:OBF66390.1}.
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DR   EMBL; LZIF01000063; OBF66390.1; -; Genomic_DNA.
DR   RefSeq; WP_067124938.1; NZ_LZIF01000063.1.
DR   AlphaFoldDB; A0A1A2BE94; -.
DR   STRING; 1834106.A5753_06665; -.
DR   Proteomes; UP000091887; 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; cd07089; ALDH_CddD-AldA-like; 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          15..481
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        259
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   488 AA;  51228 MW;  A6B07D639E3A365E CRC64;
     MTIVAEQRTY VAGSWITGDD VVSVENPADE SHVADITATP LPEVRRAIAE ARRSFDDGVW
     ADAPPSERAR VLHALIDHVE AARDALVPTL VAEAGQSKFF AEMTQLRAGA AIGRHTIDLY
     QSMSHEEASP VPVDDLVRGR VALSIRRHEP VGVVTAITPY NAALIMGFQK LIPALMAGNS
     VILRPSPLTP ISSLIFGAAA DAAGLPPGVL SVVVESGIAG AELLTSDPGV DMVSFTGSTL
     AGRRILAQAA PTVKRVSLEL GGKSAQIYLP DAVHRAAGGA FVAVASTAGQ ACVAATRMLV
     PQDKKDEVLD AVSAMYKLIK VGPPSDESAM MGPVISAAQR DKCEKYVKLA EEHGGKVFCG
     GGRPAGLDRG YYFEPTVLDL PTNANPAAQE EIFGPIIGVL GYRDIDDAVA IANDSIYGLS
     GQVYGTDAAA ALQVARRLRT GAVNVNTTVF SAYAPSGGYK QSGLGRERGP DGIREFQEVK
     HMSIGELK
//
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