GenomeNet

Database: UniProt
Entry: F3L4P8_9GAMM
LinkDB: F3L4P8_9GAMM
Original site: F3L4P8_9GAMM 
ID   F3L4P8_9GAMM            Unreviewed;       296 AA.
AC   F3L4P8;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   13-SEP-2023, entry version 48.
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=EYZ66_12970 {ECO:0000313|EMBL:QHJ89152.1}, IMCC3088_2649
GN   {ECO:0000313|EMBL:EGG28696.1};
OS   Aequoribacter fuscus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC   Aequoribacter.
OX   NCBI_TaxID=2518989 {ECO:0000313|EMBL:EGG28696.1, ECO:0000313|Proteomes:UP000005615};
RN   [1] {ECO:0000313|EMBL:EGG28696.1, ECO:0000313|Proteomes:UP000005615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC3088 {ECO:0000313|EMBL:EGG28696.1,
RC   ECO:0000313|Proteomes:UP000005615};
RX   PubMed=21551310; DOI=10.1128/JB.05111-11;
RA   Jang Y., Oh H.M., Kang I., Lee K., Yang S.J., Cho J.C.;
RT   "Genome sequence of strain IMCC3088, a proteorhodopsin-containing marine
RT   bacterium belonging to the OM60/NOR5 clade.";
RL   J. Bacteriol. 193:3415-3416(2011).
RN   [2] {ECO:0000313|EMBL:QHJ89152.1, ECO:0000313|Proteomes:UP000464557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC3088 {ECO:0000313|EMBL:QHJ89152.1,
RC   ECO:0000313|Proteomes:UP000464557};
RA   Li S.-H.;
RT   "Halieaceae_genomes.";
RL   Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
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; AEIG01000086; EGG28696.1; -; Genomic_DNA.
DR   EMBL; CP036423; QHJ89152.1; -; Genomic_DNA.
DR   RefSeq; WP_009576807.1; NZ_CP036423.1.
DR   AlphaFoldDB; F3L4P8; -.
DR   STRING; 2518989.IMCC3088_2649; -.
DR   KEGG; afus:EYZ66_12970; -.
DR   eggNOG; COG4569; Bacteria.
DR   OrthoDB; 9786743at2; -.
DR   Proteomes; UP000005615; Unassembled WGS sequence.
DR   Proteomes; UP000464557; Chromosome.
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|ARBA:ARBA00022797,
KW   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:QHJ89152.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005615}.
FT   DOMAIN          6..120
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   ACT_SITE        131
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT   BINDING         273
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
SQ   SEQUENCE   296 AA;  31394 MW;  C4A574888BB3DA5F CRC64;
     MTKKFKAAII GPGNIGTDLL MKCLRSDVIE PVWMVGIEES AGIKRAREYG LRVSTDGVDG
     LVAAFNEAPV DFAFDATSAY VHAENSRKLN KLGVMMIDLT PAAIGPYCVP PVNLDAIMAD
     TPKDNVNMVT CGGQATIPLV ASVSRVQPVS YAEIVATVAS KSVGMGTRDN IDEFTRTTSA
     AIAQVGGADE GKAIIIINPA EPPLIMRDTV HCLTKEPADA EAITASVKDM IKEVQTYVPG
     YRLLNDPIID GNRVTITVEV EGLGDFLPKY AGNLDIMTAA GLKTAEMIAR RKLAAG
//
DBGET integrated database retrieval system