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Database: UniProt
Entry: X7YKS9_MYCKA
LinkDB: X7YKS9_MYCKA
Original site: X7YKS9_MYCKA 
ID   X7YKS9_MYCKA            Unreviewed;       312 AA.
AC   X7YKS9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Acetaldehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01657};
DE            EC=1.2.1.10 {ECO:0000256|HAMAP-Rule:MF_01657};
DE   AltName: Full=Acetaldehyde dehydrogenase [acetylating] {ECO:0000256|HAMAP-Rule:MF_01657};
GN   ORFNames=I545_6433 {ECO:0000313|EMBL:EUA07401.1};
OS   Mycobacterium kansasii 662.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1299326 {ECO:0000313|EMBL:EUA07401.1, ECO:0000313|Proteomes:UP000020561};
RN   [1] {ECO:0000313|EMBL:EUA07401.1, ECO:0000313|Proteomes:UP000020561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=662 {ECO:0000313|EMBL:EUA07401.1,
RC   ECO:0000313|Proteomes:UP000020561};
RA   Brown-Elliot B., Wallace R., Lenaerts A., Ordway D., DeGroote M.A.,
RA   Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N.,
RA   Fraser C.M., Hine E., Shefchek K.A., Das S.P., Tettelin H.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + NAD(+) + propanal = H(+) + NADH + propanoyl-CoA;
CC         Xref=Rhea:RHEA:36027, ChEBI:CHEBI:15378, ChEBI:CHEBI:17153,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.87;
CC         Evidence={ECO:0000256|ARBA:ARBA00023503};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36028;
CC         Evidence={ECO:0000256|ARBA:ARBA00023503};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetaldehyde + CoA + NAD(+) = acetyl-CoA + H(+) + NADH;
CC         Xref=Rhea:RHEA:23288, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.10;
CC         Evidence={ECO:0000256|ARBA:ARBA00023526};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23289;
CC         Evidence={ECO:0000256|ARBA:ARBA00023526};
CC   -!- SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009244, ECO:0000256|HAMAP-Rule:MF_01657}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EUA07401.1}.
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DR   EMBL; JAOA01000017; EUA07401.1; -; Genomic_DNA.
DR   RefSeq; WP_023368393.1; NZ_JAOA01000017.1.
DR   AlphaFoldDB; X7YKS9; -.
DR   GeneID; 29700275; -.
DR   PATRIC; fig|1299326.3.peg.6185; -.
DR   Proteomes; UP000020561; Unassembled WGS sequence.
DR   GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_01657; Ac_ald_DH_ac; 1.
DR   InterPro; IPR003361; Acetaldehyde_dehydrogenase.
DR   InterPro; IPR015426; Acetylaldehyde_DH_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   NCBIfam; TIGR03215; ac_ald_DH_ac; 1.
DR   Pfam; PF09290; AcetDehyd-dimer; 1.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   PIRSF; PIRSF015689; Actaldh_dh_actl; 1.
DR   SMART; SM00859; Semialdhyde_dh; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism {ECO:0000256|HAMAP-Rule:MF_01657};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01657};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01657,
KW   ECO:0000313|EMBL:EUA07401.1}.
FT   DOMAIN          6..119
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   ACT_SITE        127
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT   BINDING         12..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT   BINDING         162..170
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT   BINDING         281
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
SQ   SEQUENCE   312 AA;  32880 MW;  E5AD6F0A90338330 CRC64;
     MPSKASVAIV GSGNISTDLL YKLLRSDWLE PRWMVGIDPE SEGLARARKL GLETTHEGVD
     WLLAQSEKPD LVFEATSAYV HKAAAPKYAE AGIRAIDLTP AAVGPAVIPP ANLREHLDAP
     NVNMITCGGQ ATIPIVYAVS RALVEKGGVP YAEIVASVAS VSAGPGTRAN IDEFTKTTSR
     GVQTIGGAAR GKAIIILNPA DPPMIMRDTI FCAIPEDADR DAIAKSIRDV VAEVQTYVPG
     YRLLNEPQFD EPSLNSGGQA VVTTFVEVEG AGDYLPPYAG NLDIMTAAAT KVGEEIARKS
     KDVTLSATGG TR
//
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