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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//