ID   ALDH_MYCTO              Reviewed;         507 AA.
AC   P9WNY0; L0T3T1; O53743; P63937;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Probable aldehyde dehydrogenase;
DE            EC=1.2.1.3;
GN   OrderedLocusNames=MT0474;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK44698.1; -; Genomic_DNA.
DR   PIR; F70827; F70827.
DR   RefSeq; WP_003402294.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WNY0; -.
DR   SMR; P9WNY0; -.
DR   EnsemblBacteria; AAK44698; AAK44698; MT0474.
DR   GeneID; 45424420; -.
DR   KEGG; mtc:MT0474; -.
DR   PATRIC; fig|83331.31.peg.504; -.
DR   HOGENOM; CLU_005391_0_2_11; -.
DR   Proteomes; UP000001020; 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   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 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   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..507
FT                   /note="Probable aldehyde dehydrogenase"
FT                   /id="PRO_0000427048"
FT   ACT_SITE        263
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        302
FT                   /evidence="ECO:0000250"
FT   BINDING         219..225
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   507 AA;  54575 MW;  4AB57CB742244451 CRC64;
     MTVFSRPGSA GALMSYESRY QNFIGGQWVA PVHGRYFENP TPVTGQPFCE VPRSDAADID
     KALDAAHAAA PGWGKTAPAE RAAILNMIAD RIDKNAAALA VAEVWDNGKP VREALAADIP
     LAVDHFRYFA AAIRAQEGAL SQIDEDTVAY HFHEPLGVVG QIIPWNFPIL MAAWKLAPAL
     AAGNTAVLKP AEQTPASVLY LMSLIGDLLP PGVVNVVNGF GAEAGKPLAS SDRIAKVAFT
     GETTTGRLIM QYASHNLIPV TLELGGKSPN IFFADVLAAH DDFCDKALEG FTMFALNQGE
     VCTCPSRSLI QADIYDEFLE LAAIRTKAVR QGDPLDTETM LGSQASNDQL EKVLSYIEIG
     KQEGAVIIAG GERAELGGDL SGGYYMQPTI FTGTNNMRIF KEEIFGPVVA VTSFTDYDDA
     IGIANDTLYG LGAGVWSRDG NTAYRAGRDI QAGRVWVNCY HLYPAHAAFG GYKQSGIGRE
     GHQMMLQHYQ HTKNLLVSYS DKALGFF