ID   DMPC_PSEUF              Reviewed;         486 AA.
AC   P19059;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=2-hydroxymuconic semialdehyde dehydrogenase;
DE            Short=HMSD;
DE            EC=1.2.1.85;
GN   Name=dmpC;
OS   Pseudomonas sp. (strain CF600).
OG   Plasmid pVI150.
OC   Bacteria; Proteobacteria.
OX   NCBI_TaxID=79676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2194577; DOI=10.1016/0167-4781(90)90046-5;
RA   Nordlund I., Shingler V.;
RT   "Nucleotide sequences of the meta-cleavage pathway enzymes 2-hydroxymuconic
RT   semialdehyde dehydrogenase and 2-hydroxymuconic semialdehyde hydrolase from
RT   Pseudomonas CF600.";
RL   Biochim. Biophys. Acta 1049:227-230(1990).
CC   -!- FUNCTION: 2-hydroxymuconic acid semialdehyde can be converted to 2-
CC       hydroxypent-2,4-dienoate either directly by the action of 2-
CC       hydroxymuconic semialdehyde hydrolase (HMSH) or by the action of three
CC       sequential enzymes, the first of which is HMSD.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate + H2O + NAD(+) =
CC         (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:34219, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28080, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:71198; EC=1.2.1.85;
CC   -!- PATHWAY: Aromatic compound metabolism; benzoate degradation via
CC       hydroxylation.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; X52805; CAA36992.1; -; Genomic_DNA.
DR   AlphaFoldDB; P19059; -.
DR   SMR; P19059; -.
DR   UniPathway; UPA00156; -.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0043640; P:benzoate catabolic process via hydroxylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR017628; OHmuconic_semiald_DH.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR03216; OH_muco_semi_DH; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; NAD; Oxidoreductase; Plasmid.
FT   CHAIN           1..486
FT                   /note="2-hydroxymuconic semialdehyde dehydrogenase"
FT                   /id="PRO_0000056588"
FT   ACT_SITE        254
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        288
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   486 AA;  51683 MW;  F906FCA64185AA68 CRC64;
     MKEIKHFING AFVGSASGRT FEDVNPANGQ VIARVHEAGR AEVDAAVQAA RAALKGPWGK
     MSVSERAEIL HRVADGITAR FDEFLEAECL DTGKPKSLAS HIDIPRGAAN FKVFADLLKN
     VATEAFEMAT PDGSGAINYA VRRPKGVIGV ISPWNLPLLL MTWKVGPALA CGNTVVVKPS
     EETPLTTALL GEVMQAAGVP AGVYNVVHGF GPDSAGAFLT EHPDVNAITF TGETRTGEAI
     MRAAAKGVRP VSFELGGKNA GIVFADCDLD KAIEGSMRSV FANGGQVCLG TERLYVERPI
     FDEFVARLKA GAESLVIGTP DDPQANFGPL ISLQHREKVL SYYQKAVDEG ATVVTGGGVP
     EMPAELAGGA WVQPTIWTGL ADGAAVVTEE IFGPCCHIRP FDREEEAVEL ANSLPYGLAA
     TIWTENTSRA HRVAGQLEAG IVWVNSWFLR DLRTAFGGSK QSGIGREGGV HSLEFYTELK
     NICVKL