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Database: UniProt/TrEMBL
Entry: A1T550_MYCVP
LinkDB: A1T550_MYCVP
Original site: A1T550_MYCVP 
ID   A1T550_MYCVP            Unreviewed;       507 AA.
AC   A1T550;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   SubName: Full=Aldehyde dehydrogenase (NAD(+)) {ECO:0000313|EMBL:ABM12300.1};
DE            EC=1.2.1.3 {ECO:0000313|EMBL:ABM12300.1};
GN   OrderedLocusNames=Mvan_1468 {ECO:0000313|EMBL:ABM12300.1};
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM12300.1, ECO:0000313|Proteomes:UP000009159};
RN   [1] {ECO:0000313|EMBL:ABM12300.1, ECO:0000313|Proteomes:UP000009159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1 {ECO:0000313|Proteomes:UP000009159};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP000511; ABM12300.1; -; Genomic_DNA.
DR   RefSeq; WP_011778726.1; NZ_JACKSD010000152.1.
DR   AlphaFoldDB; A1T550; -.
DR   STRING; 350058.Mvan_1468; -.
DR   KEGG; mva:Mvan_1468; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_2_11; -.
DR   OMA; VWTRDAH; -.
DR   Proteomes; UP000009159; 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; cd07116; ALDH_ACDHII-AcoD; 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   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;  55036 MW;  D9EFC2659CEC4A2A CRC64;
     MTVYARPGAD GSLMSFKPRY DNFIGGQWVA PNAGRYFENP SPVTGQPFTE VARSDESDIE
     KALDAAHAAA PAWGKTSAAE RAVILNKIAD RIEENLESIA LAESWDNGKP IRETLNADIP
     LAVDHFRYFA GAIRAQEGSL SEIDDDTVAY HFHEPLGVVG QIIPWNFPIL MAVWKLAPAL
     AAGNAIVLKP AEQTPASILY LMELIADLLP AGVINVVNGF GVEAGKPLAS SNRIAKIAFT
     GETTTGRLIM QYASQNLIPV TLELGGKSPN IFFNDVLAQA DNYQDKALEG FTMFALNQGE
     VCTCPSRSLI QADIYDEFLA LAAIRTKAVR QGDPLDTETM IGAQASNDQL EKILSYIEIG
     KSEGAQVVTG GERAELGGDL NGGYYVAPTI FTGHNKMRIF QEEIFGPVVA VTSFTDYDDA
     ISIANDTLYG LGAGVWSRDG NTAYRAGRDI KAGRVWTNCY HQYPAHAAFG GYKQSGIGRE
     NHKMMLDHYQ QTKNLLVSYS DKALGFF
//
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