(data stored in SCRATCH zone)

SWISSPROT: C8U244_ECO10

ID   C8U244_ECO10            Unreviewed;       316 AA.
AC   C8U244;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=Acetaldehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01657, ECO:0000256|SAAS:SAAS00327776};
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=mhpF {ECO:0000256|HAMAP-Rule:MF_01657,
GN   ECO:0000313|EMBL:BAI29202.1};
GN   OrderedLocusNames=ECO103_0333 {ECO:0000313|EMBL:BAI29202.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29202.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29202.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Catalyzes the conversion of acetaldehyde to acetyl-CoA,
CC       using NAD(+) and coenzyme A. Is the final enzyme in the meta-
CC       cleavage pathway for the degradation of aromatic compounds.
CC       {ECO:0000256|HAMAP-Rule:MF_01657}.
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, ECO:0000256|SAAS:SAAS01120649};
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate
CC       degradation. {ECO:0000256|HAMAP-Rule:MF_01657}.
CC   -!- SUBUNIT: Interacts with MhpE. {ECO:0000256|HAMAP-Rule:MF_01657}.
CC   -!- SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01657, ECO:0000256|SAAS:SAAS00551863}.
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DR   EMBL; AP010958; BAI29202.1; -; Genomic_DNA.
DR   RefSeq; WP_000044314.1; NC_013353.1.
DR   SMR; C8U244; -.
DR   EnsemblBacteria; BAI29202; BAI29202; ECO103_0333.
DR   KEGG; eoh:ECO103_0333; -.
DR   HOGENOM; HOG000052149; -.
DR   KO; K04073; -.
DR   OMA; TSAYVHK; -.
DR   BioCyc; ECOL585395:ECO103_RS01740-MONOMER; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000000959; 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:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
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; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR03215; ac_ald_DH_ac; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U244.
DR   SWISS-2DPAGE; C8U244.
KW   Aromatic hydrocarbons catabolism {ECO:0000256|HAMAP-Rule:MF_01657,
KW   ECO:0000256|SAAS:SAAS00319161};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01657, ECO:0000256|SAAS:SAAS00319167};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01657,
KW   ECO:0000256|SAAS:SAAS00319162}.
FT   DOMAIN        5    123       Semialdhyde_dh. {ECO:0000259|SMART:
FT                                SM00859}.
FT   NP_BIND      11     14       NAD. {ECO:0000256|HAMAP-Rule:MF_01657}.
FT   NP_BIND     162    170       NAD. {ECO:0000256|HAMAP-Rule:MF_01657}.
FT   ACT_SITE    131    131       Acyl-thioester intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01657}.
FT   BINDING     289    289       NAD. {ECO:0000256|HAMAP-Rule:MF_01657}.
SQ   SEQUENCE   316 AA;  33442 MW;  A6918BDA5EF4876B CRC64;
     MSKRKVAIIG SGNIGTDLMI KILRHGQHLE MAVMVGIDPQ SDGLARARRM GVATTHEGVI
     GLMNMPEFAD IDIVFDATSA GAHVKNDAAL REAKPDIRLI DLTPAAIGPY CVPVVNLEAN
     VDQLNVNMVT CGGQATIPMV AAVSRVARVH YAEIIASIAS KSAGPGTRAN IDEFTETTSR
     AIEVVGGAAK GKAIIVLNPA EPPLMMRDTV YVLSDEASQD DIEASINEMA EAVQAYVPGY
     RLKQRVQFEV IPQDKPVNLP GVGQFSGLKT AVWLEVEGAA HYLPAYAGNL DIMTSSALAT
     AEKMAQSLAR KAGEAA
//

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