ID A0A0L0K4T2_9ACTN Unreviewed; 297 AA.
AC A0A0L0K4T2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
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 Name=bphJ {ECO:0000313|EMBL:GAV41755.1};
GN ORFNames=IQ63_20545 {ECO:0000313|EMBL:KND33117.1}, Saa2_04669
GN {ECO:0000313|EMBL:GAV41755.1};
OS Streptomyces acidiscabies.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=42234 {ECO:0000313|EMBL:KND33117.1, ECO:0000313|Proteomes:UP000037151};
RN [1] {ECO:0000313|EMBL:KND33117.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NCPPB 4445 {ECO:0000313|EMBL:KND33117.1};
RA Chen X.-L., Norrbom A., Zhu C.-D.;
RT "A systematic study of Ichneumonosoma Meijere, Pelmatops Enderlein,
RT Pseudopelmatops Shiraki and Soita Walker (Diptera: Tephritidae).";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000037151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
RA Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT "Genome sequencing of plant-pathogenic Streptomyces species.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:GAV41755.1, ECO:0000313|Proteomes:UP000186713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2 {ECO:0000313|EMBL:GAV41755.1}, and a2
RC {ECO:0000313|Proteomes:UP000186713};
RG Cross-ministerial Strategic Innovation Promotion Program (SIP) consortium;
RA Tomihama T., Ikenaga M., Sakai M., Okubo T., Ikeda S.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:GAV41755.1, ECO:0000313|Proteomes:UP000186713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=a2 {ECO:0000313|Proteomes:UP000186713}, and A2
RC {ECO:0000313|EMBL:GAV41755.1};
RA Tomihama T., Ikenaga M., Sakai M., Okubo T., Ikeda S.;
RT "Draft genome of pathogenic Streptomyces sp. in Japan.";
RL Submitted (JAN-2017) 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 -!- 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:KND33117.1}.
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DR EMBL; BCML01000038; GAV41755.1; -; Genomic_DNA.
DR EMBL; JPPY01000129; KND33117.1; -; Genomic_DNA.
DR RefSeq; WP_050371968.1; NZ_KQ257822.1.
DR AlphaFoldDB; A0A0L0K4T2; -.
DR PATRIC; fig|42234.21.peg.4237; -.
DR OrthoDB; 9786743at2; -.
DR Proteomes; UP000037151; Unassembled WGS sequence.
DR Proteomes; UP000186713; 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 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:GAV41755.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037151}.
FT DOMAIN 8..121
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 129
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
FT BINDING 269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01657"
SQ SEQUENCE 297 AA; 31272 MW; E2ADA6FDC5E0554E CRC64;
MQATGRLSVS VLGAGLIGLD LATKIMRSDR LDLRLVAGRD EAAPGLRRAA RRGVPVATGG
IQSLVDAEED FDVVFDATNA SCHAEHAEKL AASGALLVDL TPSRVGQMIV PTVNRADIGS
HRDISMVTCG GQACVPILHA IAKAHRIDHI EVVTTAATLS VGHASRLNLD EYVATTRDAI
RLFTGVENVK ALVNISPARP AATFRVAMYL LGQDLTTESV RSLVAGAAAE IRTYVKGFDV
NVCTVNDSMA FVSVEVTSAG DRLPHYAGNL DIINSAAIQA AEYYAADRLA LAGRETA
//
