ID Q7DAD9_MYCTO Unreviewed; 491 AA. AC Q7DAD9; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 24-JAN-2024, entry version 112. DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492}; GN OrderedLocusNames=MT0155 {ECO:0000313|EMBL:AAK44379.1}; OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=83331 {ECO:0000313|EMBL:AAK44379.1, ECO:0000313|Proteomes:UP000001020}; RN [1] {ECO:0000313|EMBL:AAK44379.1, ECO:0000313|Proteomes:UP000001020} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 1551 / Oshkosh {ECO:0000313|Proteomes:UP000001020}; 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., DeBoy R., Dodson R., Gwinn M., Haft D., Hickey E., RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M., Salzberg S.L., RA Delcher A., Utterback T., Weidman J., Khouri H., Gill J., Mikula A., RA Bishai W., Jacobs Jr 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 -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492, 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; AE000516; AAK44379.1; -; Genomic_DNA. DR RefSeq; WP_003913557.1; NZ_KK341227.1. DR AlphaFoldDB; Q7DAD9; -. DR KEGG; mtc:MT0155; -. DR HOGENOM; CLU_005391_3_1_11; -. DR Proteomes; UP000001020; 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 GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro. DR CDD; cd07087; ALDH_F3-13-14_CALDH-like; 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 InterPro; IPR012394; Aldehyde_DH_NAD(P). DR PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1. DR PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1. DR Pfam; PF00171; Aldedh; 1. DR PIRSF; PIRSF036492; ALDH; 1. DR SUPFAM; SSF53720; ALDH-like; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 3: Inferred from homology; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR036492}; KW Reference proteome {ECO:0000313|Proteomes:UP000001020}. FT DOMAIN 23..462 FT /note="Aldehyde dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF00171" FT REGION 1..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 10..33 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 239 FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1, FT ECO:0000256|PROSITE-ProRule:PRU10007" FT ACT_SITE 273 FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1" SQ SEQUENCE 491 AA; 53453 MW; EAD772943D6A2987 CRC64; MMTTESVARK TQKSETEAPR EPAPVSDEKQ TDVAKTVARL RKTFASGRTR SVEWRKQQLR ALQKLMDENE DAIAAALAED LDRNPFEAYL ADIATTSAEA KYAAKRVRRW MRRRYLLLEV PQLPGRGWVE YEPYGTVLII GAWNYPFYLT LGPAVGAIAA GNAVVLKPSE IAAASAHLMT ELVYRYLDTE AIAVVQGDGA VSQELIAQGF DRVMFTGGTE IGRKVYEGAA PHLTPVTLEL GGKSPVIVAA DADVDVAAKR IAWIKLLNAG QTCVAPDYVL ADATVRDELV SKITAALTKF RSGAPQGMRI VNQRQFDRLS GYLAAAKTDA AADGGGVVVG GDCDASNLRI QPTVVVDPDP DGPLMSNEIF GPILPVVTVK SLDDAIRFVN SRPKPLSAYL FTKSRAVRER VIREVPAGGM MVNHLAFQVS TAKLPFGGVG ASGMGAYHGR WGFEEFSHRK SVLTKPTRPD LSSFIYPPYT ERAIKVARRL F //