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Database: UniProt/TrEMBL
Entry: Q73UF5_MYCPA
LinkDB: Q73UF5_MYCPA
Original site: Q73UF5_MYCPA 
ID   Q73UF5_MYCPA            Unreviewed;       509 AA.
AC   Q73UF5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 102.
DE   RecName: Full=aldehyde dehydrogenase (NAD(+)) {ECO:0000256|ARBA:ARBA00024226};
DE            EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226};
GN   Name=aldB {ECO:0000313|EMBL:AAS05963.1};
GN   OrderedLocusNames=MAP_3413 {ECO:0000313|EMBL:AAS05963.1};
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316 {ECO:0000313|EMBL:AAS05963.1, ECO:0000313|Proteomes:UP000000580};
RN   [1] {ECO:0000313|EMBL:AAS05963.1, ECO:0000313|Proteomes:UP000000580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10 {ECO:0000313|Proteomes:UP000000580};
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS05963.1; -; Genomic_DNA.
DR   RefSeq; WP_003874510.1; NZ_CP106873.1.
DR   AlphaFoldDB; Q73UF5; -.
DR   STRING; 262316.MAP_3413; -.
DR   KEGG; mpa:MAP_3413; -.
DR   PATRIC; fig|262316.17.peg.3628; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_2_11; -.
DR   OMA; DAWKVYM; -.
DR   Proteomes; UP000000580; 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:UP000000580}.
FT   DOMAIN          35..490
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   509 AA;  53478 MW;  63A85AB63D331421 CRC64;
     MTLPTAAELR ARAADALRSL GAHVELGAPD AHGLPASTPI TGEVLFTVAP TTSDQAEHTI
     TQATQAFSEW RRTPAPVRGA LVARLGELLR AHRDELAALV TLEVGKITSE AAGEVQEMID
     ICQFAVGLSR QLYGRTIASE RPGHRLSETW HPLGVVGVIT AFNFPVAVWA WNAALALVCG
     DTVVWKPSEL TPLTALATQA LIARAAADVG APPGVSAVVL GDRELGELLV DDERVALVSA
     TGSVRMGRAV GPRVAARFGR VLLELGGNNA AVVTPSADLD LAVRAVVFAA AGTAGQRCTT
     LRRLIVHRSV ADEVVARVVS ALRRLPIGDP FEPGTLVGPL IHETAYRDMV GALESARADG
     GEVIDGDRRH PFAVEHPSSY YVAPAVVRMP AQTPIVATET FAPILYVLTY DRLDDAIALN
     NAVPQGLSSA IFTTDLREAE RFLDESDCGI ANVNIGTSGA EIGGAFGGEK QTGGGRESGS
     DSWKAYMRQS TNTVNYSGAL PLAQGVEFG
//
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