ID XYLG_PSEPU Reviewed; 486 AA. AC P23105; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 02-SEP-2026, entry version 118. DE RecName: Full=2-hydroxymuconic semialdehyde dehydrogenase; DE Short=HMSD; DE EC=1.2.1.85; GN Name=xylG; OS Pseudomonas putida (Arthrobacter siderocapsulatus). OG Plasmid TOL pWW0. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1791759; DOI=10.1111/j.1365-2958.1991.tb02091.x; RA Horn J.M., Harayama S., Timmis K.N.; RT "DNA sequence determination of the TOL plasmid (pWWO) xylGFJ genes of RT Pseudomonas putida: implications for the evolution of aromatic RT catabolism."; RL Mol. Microbiol. 5:2459-2474(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=PAO; RX PubMed=1339433; DOI=10.1016/s0021-9258(18)42252-1; RA Steele M.I., Lorenz D., Hatter K., Park A., Sokatch J.R.; RT "Characterization of the mmsAB operon of Pseudomonas aeruginosa PAO RT encoding methylmalonate-semialdehyde dehydrogenase and 3-hydroxyisobutyrate RT dehydrogenase."; RL J. Biol. Chem. 267:13585-13592(1992). RN [3] RP PROTEIN SEQUENCE OF 1-15, AND CATALYTIC ACTIVITY. RX PubMed=7868591; DOI=10.1128/jb.177.5.1196-1201.1995; RA Inoue J., Shaw J.P., Rekik M., Harayama S.; RT "Overlapping substrate specificities of benzaldehyde dehydrogenase (the RT xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the RT xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida."; RL J. Bacteriol. 177:1196-1201(1995). 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. Can oxidize not only 2- CC hydroxymuconic semialdehyde and its analogs but also benzaldehyde and CC its analogs. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate + NAD(+) + H2O = CC (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H(+); 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 Evidence={ECO:0000269|PubMed:7868591}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 8.3 for the oxidation of 2-hydroxymuconic semialdehyde, CC and 9.6 for that of benzaldehyde.; CC -!- PATHWAY: Aromatic compound metabolism; benzoate degradation via CC hydroxylation. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000305}. 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; M64747; AAA26053.1; -; Genomic_DNA. DR PIR; E42902; E42902. DR RefSeq; WP_011005908.1; NC_003350.1. DR AlphaFoldDB; P23105; -. DR SMR; P23105; -. DR KEGG; ag:AAA26053; -. DR BioCyc; MetaCyc:MONOMER-3402; -. DR UniPathway; UPA00156; -. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:RHEA. DR GO; GO:0043640; P:benzoate catabolic process via hydroxylation; IEA:UniProtKB-UniPathway. DR CDD; cd07093; ALDH_F8_HMSADH; 1. DR FunFam; 3.40.309.10:FF:000009; Aldehyde dehydrogenase A; 1. DR FunFam; 3.40.605.10:FF:000007; NAD/NADP-dependent betaine aldehyde dehydrogenase; 1. DR Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1. DR Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 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 NCBIfam; TIGR03216; OH_muco_semi_DH; 1. DR PANTHER; PTHR43720; 2-AMINOMUCONIC SEMIALDEHYDE DEHYDROGENASE; 1. DR PANTHER; PTHR43720:SF2; 2-AMINOMUCONIC SEMIALDEHYDE DEHYDROGENASE; 1. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; ALDH-like; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 1: Evidence at protein level; KW Aromatic hydrocarbons catabolism; Direct protein sequencing; NAD; KW Oxidoreductase; Plasmid. FT CHAIN 1..486 FT /note="2-hydroxymuconic semialdehyde dehydrogenase" FT /id="PRO_0000056594" FT ACT_SITE 254 FT /evidence="ECO:0000250" FT ACT_SITE 288 FT /evidence="ECO:0000250" FT CONFLICT 11..12 FT /note="EL -> AF (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 486 AA; 51761 MW; 854303F121B2FFBD CRC64; MKEIKHFISG ELVGSASGKL FDNVSPANGQ VIGRVHEAGR AEVDAAVRAA RAALKGPWGK MTVAERAEIL HRVADGITAR FGEFLEARMP GHRQAEVAGQ PHRHSARRAN FKVFADLLKN VANEAFEMAT PDGAGALNYG VRRPKGVIGV ISPWNLPLLL MTWKVGPALA CGNCVVVKPS EETPLTATLL GEVMQAAGVP AGVYNVVHGF GGDSAGAFLT EHPDVDAYTF TGETGTGETI MRAAAKGVRQ VSLELGGKNA GIVFADCDMD KAIEGTLRSA FANCGQVCLG TERVYVERPI FDAFVARLKA GAEALKIGEP NDPEANFGPL ISHKPREKVP SYYQQAVDDG ATVVTGGGVP EMPAHLAGGA WVQPTIWTGL ADDSAVVTEE IFGPCCHIRP FDSEEEAIEL ANSLPYGLAS AIWTENVRRA HRVAGQIEAG IVWVNSWFLR DLRTAFGGSK QSGIGREGGV HSLEFYTELK NICVKL //