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Database: UniProt
Entry: N9RQE1_9GAMM
LinkDB: N9RQE1_9GAMM
Original site: N9RQE1_9GAMM 
ID   N9RQE1_9GAMM            Unreviewed;       322 AA.
AC   N9RQE1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=F885_02380 {ECO:0000313|EMBL:ENX60188.1};
OS   Acinetobacter higginsii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=70347 {ECO:0000313|EMBL:ENX60188.1, ECO:0000313|Proteomes:UP000013100};
RN   [1] {ECO:0000313|EMBL:ENX60188.1, ECO:0000313|Proteomes:UP000013100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANC 3880 {ECO:0000313|EMBL:ENX60188.1,
RC   ECO:0000313|Proteomes:UP000013100};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter sp. ANC 3880.";
RL   Submitted (FEB-2013) 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:ENX60188.1}.
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DR   EMBL; APSD01000028; ENX60188.1; -; Genomic_DNA.
DR   RefSeq; WP_005313986.1; NZ_KB850211.1.
DR   AlphaFoldDB; N9RQE1; -.
DR   PATRIC; fig|1217701.3.peg.2312; -.
DR   HOGENOM; CLU_062208_0_0_6; -.
DR   Proteomes; UP000013100; 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|HAMAP-Rule:MF_01657}.
FT   DOMAIN          10..128
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   ACT_SITE        136
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT   BINDING         16..19
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT   BINDING         167..175
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT   BINDING         294
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
SQ   SEQUENCE   322 AA;  34095 MW;  946E312965604112 CRC64;
     MNSQANNKIK AAIIGSGNIG SDLMIKMLRY GEHLEIAVMV GIDPESDGLA RAKRMNVATT
     HQGVQGLIDL PEFKDIDIVF DATSAGAHIK NDALLRQHKP NIRMVDLTPA AIGPYCVPVV
     NLEQHIDQPN VNMVTCGGQA TIPMVAAVSK IAKVHYAEIV ASISSKSAGP GTRANIDEFT
     ETTSKALETV GGATKGKAII VLNPAEPPLL MRDTVYVLSE AADQATVEAS VEQMVAEVQK
     YVAGYRLKQK VQFEVIPESA PLNIAGLGKF SGLKTSVFLE VEGAAHYLPA YAGNLDIMTS
     AALATGEKMA ASLQSQRASD EG
//
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