ID L0ITI4_9MYCO Unreviewed; 507 AA.
AC L0ITI4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=NAD-dependent aldehyde dehydrogenase {ECO:0000313|EMBL:AGB21511.1};
GN ORFNames=Mycsm_01088 {ECO:0000313|EMBL:AGB21511.1};
OS Mycobacterium sp. JS623.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB21511.1, ECO:0000313|Proteomes:UP000010844};
RN [1] {ECO:0000313|Proteomes:UP000010844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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; CP003078; AGB21511.1; -; Genomic_DNA.
DR RefSeq; WP_015305095.1; NC_019966.1.
DR AlphaFoldDB; L0ITI4; -.
DR STRING; 212767.Mycsm_01088; -.
DR KEGG; msa:Mycsm_01088; -.
DR PATRIC; fig|710686.3.peg.1095; -.
DR HOGENOM; CLU_005391_0_2_11; -.
DR OrthoDB; 6882680at2; -.
DR Proteomes; UP000010844; 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 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 PANTHER; PTHR43111; ALDEHYDE DEHYDROGENASE B-RELATED; 1.
DR PANTHER; PTHR43111:SF1; ALDEHYDE DEHYDROGENASE B-RELATED; 1.
DR Pfam; PF00171; Aldedh; 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|RuleBase:RU003345}.
FT DOMAIN 28..494
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 263
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 507 AA; 55345 MW; 1F88CA0678EA121E CRC64;
MTVYARPGTE RSVMSFKSRY ENYIGGQWVA PTAGRYFENA SPVNGLPFCE IPRSDEADIE
KALDAAHAAA PAWGKTTAAE RAVILNKIAD RIQENLESIA VAESWDNGKP VRETLNADIP
LAIDHFRYFA GAIRAQEGSL SQIDDETVAY HFHEPLGVVG QIIPWNFPIL MATWKLAPAI
AAGNAVVLKP AEQTPASILY LFELIGDLLP PGVVNIVNGF GLEAGKPLAS SKRISKIAFT
GETTTGRLIM QYASQNLIPV TLELGGKSPN IFFNDVMAQH DDYQDKALEG FTMFALNQGE
VCTCPSRSLI QADIFDEFLE LAAIRTKAVR QGDPLDTETM IGAQASEDQM EKILSYIDIG
KRDGAKLVTG GHRAELGGDL GGGYYVTPTV FTGTNDMRIF QEEIFGPVVA VTSFTDYDDA
INIANDTLYG LGAGVWSRDG NVAYRAGRDI KAGRVWTNCY HAYPAHAAFG GYKQSGIGRE
THKMMLDHYQ QTKNLLVSYS NKAQGFF
//
