ID   ALDH_MYCTU              Reviewed;         507 AA.
AC   P9WNY1; 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 45.
DE   RecName: Full=Probable aldehyde dehydrogenase;
DE            EC=1.2.1.3;
GN   OrderedLocusNames=Rv0458; ORFNames=MTV038.02;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP43191.1; -; Genomic_DNA.
DR   PIR; F70827; F70827.
DR   RefSeq; NP_214972.1; NC_000962.3.
DR   RefSeq; WP_003402294.1; NZ_NVQJ01000002.1.
DR   AlphaFoldDB; P9WNY1; -.
DR   SMR; P9WNY1; -.
DR   STRING; 83332.Rv0458; -.
DR   iPTMnet; P9WNY1; -.
DR   PaxDb; P9WNY1; -.
DR   DNASU; 886306; -.
DR   GeneID; 45424420; -.
DR   GeneID; 886306; -.
DR   KEGG; mtu:Rv0458; -.
DR   TubercuList; Rv0458; -.
DR   eggNOG; COG1012; Bacteria.
DR   OMA; ILMGAWK; -.
DR   PhylomeDB; P9WNY1; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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   GO; GO:0052562; P:suppression by symbiont of host immune response; IDA:MTBBASE.
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   1: Evidence at protein level;
KW   Acetylation; NAD; Oxidoreductase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:21969609"
FT   CHAIN           2..507
FT                   /note="Probable aldehyde dehydrogenase"
FT                   /id="PRO_0000056449"
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"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0007744|PubMed:21969609"
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