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P23105 (XYLG_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-hydroxymuconic semialdehyde dehydrogenase

Short name=HMSD
EC=1.2.1.-
Gene names
Name:xylG
Encoded onPlasmid TOL pWW0
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

2-hydroxymuconic acid semialdehyde can be converted to 2-hydroxypent-2,4-dienoate either directly by the action of 2-hydroxymuconic semialdehyde hydrolase (HMSH) or by the action of three sequential enzymes, the first of which is HMSD. Can oxidize not only 2-hydroxymuconic semialdehyde and its analogs but also benzaldehyde and its analogs.

Pathway

Aromatic compound metabolism; benzoate degradation via hydroxylation.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.3 for the oxidation of 2-hydroxymuconic semialdehyde, and 9.6 for that of benzaldehyde.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4864862-hydroxymuconic semialdehyde dehydrogenase
PRO_0000056594

Sites

Active site2541 By similarity
Active site2881 By similarity

Experimental info

Sequence conflict11 – 122EL → AF AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P23105 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 854303F121B2FFBD

FASTA48651,761
        10         20         30         40         50         60 
MKEIKHFISG ELVGSASGKL FDNVSPANGQ VIGRVHEAGR AEVDAAVRAA RAALKGPWGK 

        70         80         90        100        110        120 
MTVAERAEIL HRVADGITAR FGEFLEARMP GHRQAEVAGQ PHRHSARRAN FKVFADLLKN 

       130        140        150        160        170        180 
VANEAFEMAT PDGAGALNYG VRRPKGVIGV ISPWNLPLLL MTWKVGPALA CGNCVVVKPS 

       190        200        210        220        230        240 
EETPLTATLL GEVMQAAGVP AGVYNVVHGF GGDSAGAFLT EHPDVDAYTF TGETGTGETI 

       250        260        270        280        290        300 
MRAAAKGVRQ VSLELGGKNA GIVFADCDMD KAIEGTLRSA FANCGQVCLG TERVYVERPI 

       310        320        330        340        350        360 
FDAFVARLKA GAEALKIGEP NDPEANFGPL ISHKPREKVP SYYQQAVDDG ATVVTGGGVP 

       370        380        390        400        410        420 
EMPAHLAGGA WVQPTIWTGL ADDSAVVTEE IFGPCCHIRP FDSEEEAIEL ANSLPYGLAS 

       430        440        450        460        470        480 
AIWTENVRRA HRVAGQIEAG IVWVNSWFLR DLRTAFGGSK QSGIGREGGV HSLEFYTELK 


NICVKL 

« Hide

References

[1]"DNA sequence determination of the TOL plasmid (pWWO) xylGFJ genes of Pseudomonas putida: implications for the evolution of aromatic catabolism."
Horn J.M., Harayama S., Timmis K.N.
Mol. Microbiol. 5:2459-2474(1991) [PubMed: 1791759] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Characterization of the mmsAB operon of Pseudomonas aeruginosa PAO encoding methylmalonate-semialdehyde dehydrogenase and 3-hydroxyisobutyrate dehydrogenase."
Steele M.I., Lorenz D., Hatter K., Park A., Sokatch J.R.
J. Biol. Chem. 267:13585-13592(1992) [PubMed: 1339433] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: PAO.
[3]"Overlapping substrate specificities of benzaldehyde dehydrogenase (the xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida."
Inoue J., Shaw J.P., Rekik M., Harayama S.
J. Bacteriol. 177:1196-1201(1995) [PubMed: 7868591] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-15.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64747 Genomic DNA. Translation: AAA26053.1.
PIRE42902.
RefSeqNP_542865.1. NC_003350.1.

3D structure databases

ProteinModelPortalP23105.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1218748.

Phylogenomic databases

ProtClustDBCLSK862335.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3402.

Family and domain databases

InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR017628. OHmuconic_semiald_DH.
[Graphical view]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR03216. OH_muco_semi_DH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYLG_PSEPU
AccessionPrimary (citable) accession number: P23105
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: September 21, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families