GenomeNet

Database: UniProt
Entry: A0A1A5X4F1_9BURK
LinkDB: A0A1A5X4F1_9BURK
Original site: A0A1A5X4F1_9BURK 
ID   A0A1A5X4F1_9BURK        Unreviewed;       316 AA.
AC   A0A1A5X4F1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=A6456_24310 {ECO:0000313|EMBL:OBR47948.1}, C7399_10295
GN   {ECO:0000313|EMBL:PZW88612.1};
OS   Paraburkholderia tropica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=92647 {ECO:0000313|EMBL:OBR47948.1, ECO:0000313|Proteomes:UP000093802};
RN   [1] {ECO:0000313|Proteomes:UP000093802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P-31 {ECO:0000313|Proteomes:UP000093802};
RA   Kaur C., Selvakumar G., Ganeshamurthy A.N.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OBR47948.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P-31 {ECO:0000313|EMBL:OBR47948.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:PZW88612.1, ECO:0000313|Proteomes:UP000248793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIr-6529 {ECO:0000313|EMBL:PZW88612.1,
RC   ECO:0000313|Proteomes:UP000248793};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT   to study the core and pangenomes of soil and plant-associated
RT   prokaryotes.";
RL   Submitted (JUN-2018) 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: 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:OBR47948.1}.
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; LXGI01000107; OBR47948.1; -; Genomic_DNA.
DR   EMBL; QKZC01000002; PZW88612.1; -; Genomic_DNA.
DR   RefSeq; WP_065064297.1; NZ_QKZC01000002.1.
DR   AlphaFoldDB; A0A1A5X4F1; -.
DR   STRING; 92647.SAMN05216550_10193; -.
DR   OrthoDB; 9786743at2; -.
DR   Proteomes; UP000093802; Unassembled WGS sequence.
DR   Proteomes; UP000248793; 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|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|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01657}; Reference proteome {ECO:0000313|Proteomes:UP000093802}.
FT   DOMAIN          7..125
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   ACT_SITE        133
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT   BINDING         13..16
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT   BINDING         164..172
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT   BINDING         291
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
SQ   SEQUENCE   316 AA;  33149 MW;  B5F35E8F7F83632E CRC64;
     MASEKLKAAI IGSGNIGTDL MIKIMRNSRH LEMAAMVGID PNSDGLARAA RLGVATTHEG
     AEGLTRLPVF NDIDFVFDAT SAGAHVKNDA LLRKLKPSIR MIDLTPAAIG PYCVPVVNLD
     AQIDAPNVNM VTCGGQATIP VVAAVSRVAK VHYAEIVASI SSKSAGPGTR ANIDEFTETT
     SKAIEVVGGA AKGKAIIVLN PAEPPVMMRD TVYTLSELAD RDAIEKSIED TVAKVNAYVP
     GYRLKQKVQF DEIPANAPLT IPGLGTFSGL KTSVFLEVEG AAHYLPAYAG NLDIMTSAAL
     ATAERMAHTL LSVQGA
//
DBGET integrated database retrieval system