ID A0PMJ5_MYCUA Unreviewed; 488 AA.
AC A0PMJ5;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=NAD-dependent aldehyde dehydrogenase, AldA_1 {ECO:0000313|EMBL:ABL03564.1};
GN Name=aldA_1 {ECO:0000313|EMBL:ABL03564.1};
GN OrderedLocusNames=MUL_0939 {ECO:0000313|EMBL:ABL03564.1};
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=362242 {ECO:0000313|EMBL:ABL03564.1, ECO:0000313|Proteomes:UP000000765};
RN [1] {ECO:0000313|EMBL:ABL03564.1, ECO:0000313|Proteomes:UP000000765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99 {ECO:0000313|EMBL:ABL03564.1,
RC ECO:0000313|Proteomes:UP000000765};
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D., Davies J.K., Jenkin G.A., Small P.L., Jones L.M., Tekaia F.,
RA Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {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; CP000325; ABL03564.1; -; Genomic_DNA.
DR RefSeq; WP_011739187.1; NC_008611.1.
DR AlphaFoldDB; A0PMJ5; -.
DR KEGG; mul:MUL_0939; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_0_11; -.
DR Proteomes; UP000000765; Chromosome.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd07089; ALDH_CddD-AldA-like; 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 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; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345}.
FT DOMAIN 22..484
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 258
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 488 AA; 51289 MW; 029ECF0EDAB91481 CRC64;
MAERALPESL VDTYQLYIDG RWVEPENGRY DDVSPSTGMV IATAPDASVS QVGDAVDAAR
RAFDAGPWPA MSHQERGHCL AQLGAALQDY ADAYFTLSQV EWGCTANERR LQIDASASAA
RRAGHLASTL GDQPIQSASG AAVLCHEPLG VVSILTPWNF PHSLNVMKLS RALAGGNTVV
LKPSPLTPLA GLALARIIHE HTDIPPGVVN VVTPGGIEAS KVLTVDPRID MVSFTGSSAV
GCEVMAAAAG TMKRVLLECG GKSASIVLDD AECSDELLAR MLFESCLLHA GQACILHSRL
LLPEAMHDEI VDRLVALARA VRVGDPADPD VQMGPLISAA QRSRVEDQVA RALRDGATLA
AGGRRPATPE AGFYYEPTIL TGVTPDAHIA QNEVFGPVLS VLRYRDDDDA VAIANNSQYG
LSGAVWGGDA DRAVRVARRI RTGQIAVNGF GPGDAPFGGF KQSGLGREGG GIAGLHQYME
PKAIGMPG
//
