ID M2ZR13_9PSEU Unreviewed; 300 AA.
AC M2ZR13;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=H074_07466 {ECO:0000313|EMBL:EME62784.1};
OS Amycolatopsis decaplanina DSM 44594.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1284240 {ECO:0000313|EMBL:EME62784.1, ECO:0000313|Proteomes:UP000054226};
RN [1] {ECO:0000313|EMBL:EME62784.1, ECO:0000313|Proteomes:UP000054226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44594 {ECO:0000313|EMBL:EME62784.1,
RC ECO:0000313|Proteomes:UP000054226};
RX PubMed=23558534;
RA Kaur N., Kumar S., Bala M., Raghava G.P., Mayilraj S.;
RT "Draft Genome Sequence of Amycolatopsis decaplanina Strain DSM 44594T.";
RL Genome Announc. 1:E0013813-E0013813(2013).
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01657};
CC -!- SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009244, ECO:0000256|HAMAP-Rule:MF_01657}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:EME62784.1}.
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DR EMBL; AOHO01000036; EME62784.1; -; Genomic_DNA.
DR RefSeq; WP_007029415.1; NZ_AOHO01000036.1.
DR AlphaFoldDB; M2ZR13; -.
DR PATRIC; fig|1284240.4.peg.1505; -.
DR OrthoDB; 9786743at2; -.
DR Proteomes; UP000054226; 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:EME62784.1}.
FT DOMAIN 7..120
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 128
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT BINDING 159..167
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT BINDING 278
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
SQ SEQUENCE 300 AA; 31388 MW; A4A4A774387E0048 CRC64;
MAQRKAVAAI VGPGNIGTDL LAKLRRSEHV EVRYMVGVDP DSDGLAKAAE LGLETSARGV
DWLLSRDELP DLVFEATSAK AHLANAPRYA TAGIRAVDLT PAAVGPFTCP AVGLPERLDV
PNVNLITCGG QATIPIVHAV SRVTPVPYAE IVASVSSRSA GPGTRANIDE FTATTARGIE
LVGGASRGKA IIIINPVEPP MIMRDTVFCA IDPDADFDAV SESIHRMVET VQGYVPGYTL
KADPQFDPPR PGWGGQARVA VFLEVAGNGD FLPKYAGNLD IMTAAAARVG DLLATQEVAA
//
